CN108603185B - 酶变体以及编码它们的多核苷酸 - Google Patents
酶变体以及编码它们的多核苷酸 Download PDFInfo
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- CN108603185B CN108603185B CN201680076825.9A CN201680076825A CN108603185B CN 108603185 B CN108603185 B CN 108603185B CN 201680076825 A CN201680076825 A CN 201680076825A CN 108603185 B CN108603185 B CN 108603185B
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Abstract
本发明涉及具有α‑淀粉酶活性的多肽。本发明还涉及编码这些多肽的多核苷酸；包含这些多核苷酸的核酸构建体、载体、和宿主细胞；以及使用这些多肽的方法。
Description
序列表的引用
本申请包含计算机可读形式的序列表，将其通过引用结合在此。
背景技术
技术领域
本发明涉及α-淀粉酶变体(即，具有α-淀粉酶活性的多肽)、编码α-淀粉酶的核酸、生产α-淀粉酶的方法、包括α-淀粉酶的组合物以及使用α-淀粉酶的方法。
相关技术领域的说明
α-淀粉酶(α-1,4-葡聚糖-4-葡聚糖水解酶，E.C.3.2.1.1)构成一组酶，这些酶催化淀粉以及其他直链和支链1,4-糖苷寡糖和多糖的水解。
α-淀粉酶在工业上用于若干种已知应用的用途具有悠久历史，这些用途如洗涤剂、烘焙、酿造、淀粉液化和糖化，例如在制备高果糖糖浆中或用作从淀粉生产乙醇的一部分。α-淀粉酶的这些应用和其他应用是已知的并且利用源自微生物的α-淀粉酶，特别是细菌α-淀粉酶。
芽孢杆菌α-淀粉酶如特妙淀粉酶、AA560(SEQ ID NO:2；还参见WO 2000/060060)和SP707(SEQ ID NO:8；还参见Tsukamoto等人，1988，Biochem.Biophys.Res.Comm.[生物化学和生物物理研究通讯]151:25-31)形成特定的已经用于洗涤剂中的α-淀粉酶的组。这些淀粉酶已经经修饰以改进洗涤剂中的稳定性。例如，WO 96/23873披露了α-淀粉酶SP690、SP722(SEQ ID NO:5)和SP707(SEQ ID NO:8)的缺失型突变体(还参见WO 96/23873的SEQID NO:1、2和7)以改进这些淀粉酶的稳定性。WO 96/23873进一步披露了取代型突变体针对氧化来稳定淀粉酶。具有改进的特性的另外的α-淀粉酶突变体披露在WO 2006/002643和WO01/66712中。
因而，修饰天然存在的淀粉酶来改进某些特性是已知的。
本发明的目的是提供具有α-淀粉酶活性的多肽(α-淀粉酶)，该多肽具有增强的洗涤性能，尤其是在高温(例如在40℃或更高)下。
发明内容
本发明涉及对应于衍生自芽孢杆菌属的α-淀粉酶的变体具有α-淀粉酶活性的多肽。具体而言，本发明的多肽包含SEQ ID NO:1的氨基酸序列或由其组成，其中这些氨基酸中的一个或多个发生突变(例如，通过取代或缺失)，使得该多肽展现增强的洗涤性能(尤其在40℃或更高的温度下)。
本发明还涉及编码变体α-淀粉酶多肽的多核苷酸；包含这些多核苷酸的核酸构建体、载体、和宿主细胞；以及生产这些变体α-淀粉酶多肽的方法。
本发明还涉及包含这些变体α-淀粉酶多肽的洗涤剂组合物，以及这些洗涤剂组合物在家庭和工业清洗过程(如衣物清洗和餐具洗涤)中的用途。
定义
α-淀粉酶：术语“α-淀粉酶”(α-1,4-葡聚糖-4-葡聚糖水解酶，E.C.3.2.1.1)构成一组酶，这些酶催化淀粉以及其他直链和支链1,4-糖苷寡糖和多糖的水解。出于本发明的目的，根据实例1中所述的程序测定α-淀粉酶活性。在一方面，本发明的变体具有SEQ IDNO:1的成熟多肽的α-淀粉酶活性的至少20％，例如至少40％、至少50％、至少60％、至少70％、至少80％、至少90％、至少95％、或至少100％。
氨基酸：如本文使用的，术语‘氨基酸’包括标准二十种遗传编码的氨基酸及其相应的处于‘d’型(与天然‘l’型进行对比)的立体异构体、ω-氨基酸、其他天然存在的氨基酸、非常规氨基酸(例如α,α-双取代的氨基酸、N-烷基氨基酸等)和化学衍生的氨基酸。可以通过与功能性侧集团反应来实现一个或多个氨基酸的化学衍生物。此类衍生的分子包括例如，其中游离氨基基团已经衍生形成胺盐酸盐、对甲苯磺酰基基团、羧基苯氧基基团、叔丁氧基羰基基团、氯乙酰基基团或甲酰基基团的那些分子。游离羧基基团可以被衍生形成盐、甲酯和乙酯或其他类型的酯和酰肼。游离羟基基团可被衍生化以形成O-酰基或O-烷基衍生物。作为化学衍生物还包括那些包含二十种标准氨基酸的天然存在的氨基酸衍生物的肽。例如：4-羟脯氨酸可以取代脯氨酸；5-羟赖氨酸可以取代赖氨酸；3-甲基组氨酸可以取代组氨酸；高丝氨酸可以取代丝氨酸并且鸟氨酸取代赖氨酸。只要维持必要的活性，衍生物也包括包含一个或多个添加或缺失的肽。其他包括的修饰是酰胺化、氨基末端酰化(例如乙酰化或巯基乙酸酰胺化)、末端羧基酰胺化(例如用氨或甲胺)、和类似的末端修饰。
当明确列举氨基酸，如‘丙氨酸’或‘Ala’或‘A’时，除非另有明确说明，否则该术语是指L-丙氨酸和D-丙氨酸。其他非常规氨基酸也可以是本发明多肽的适合组分，只要所需功能特性由多肽保留即可。对于所示的肽，适当时，每个编码的氨基酸残基由单字母代号表示，对应于常规氨基酸的普通名称。在一个实施例中，本发明的多肽包含l-氨基酸或由其组成。
cDNA：术语“cDNA”意指可以通过从获得自真核或原核细胞的成熟的、剪接的mRNA分子进行反转录而制备的DNA分子。cDNA缺乏可以存在于对应基因组DNA中的内含子序列。早先的初始RNA转录物本是mRNA的前体，其在呈现为成熟的剪接的mRNA之前要经一系列步骤进行加工，包括剪接。
编码序列：术语“编码序列”意指一种多核苷酸，该多核苷酸直接规定了变体的氨基酸序列。编码序列的边界一般由开放阅读框架决定，该开放阅读框架从起始密码子(如ATG、GTG或TTG)开始并且以终止密码子(如TAA、TAG或TGA)结束。编码序列可为基因组DNA、cDNA、合成DNA或其组合。
控制序列：术语“控制序列”意指为编码本发明的变体的多核苷酸的表达所需的核酸序列。每个控制序列对于编码该变体的多核苷酸来说可以是天然的(即，来自相同基因)或外源的(即，来自不同基因)，或相对于彼此是天然的或外源的。此类控制序列包括但不限于前导子、聚腺苷酸化序列、前肽序列、启动子、信号肽序列和转录终止子。最少，控制序列包括启动子、以及转录和翻译终止信号。出于引入促进控制序列与编码变体的多核苷酸的编码区域连接的特异性限制位点的目的，控制序列可以提供有接头。
增强的洗涤性能：术语“增强的洗涤性能”或“改进的洗涤性能”意指与SEQ ID NO:1的亲本α淀粉酶相比，本发明的多肽在洗涤过程(如衣物洗涤或餐具洗涤)中提供清洗效果(例如去除污渍)的能力是改进的。可以使用本领域熟知的方法来确定洗涤性能，如使用自动机械应力测定(AMSA)或自动餐具洗涤(ADW)(参见实例2和3)。本领域技术人员将会理解，仅在一些或者可能所有的洗涤条件下(例如在40℃或更高(例如在40℃和/或在50℃)的洗涤温度下、和/或有或没有漂白剂的存在)，可以实现增强的洗涤性能。
表达：术语“表达”包括涉及变体的产生的任何步骤，包括(但不限于)转录、转录后修饰、翻译、翻译后修饰、以及分泌。
表达载体：术语“表达载体”意指一种直链或环状DNA分子，该分子包括编码一种变体的一种多核苷酸并且可操作地连接至提供用于其表达的控制序列。
片段：术语“片段”意指具有在SEQ ID NO:1的成熟多肽的氨基和/或羧基末端不存在的一个或多个(例如若干个)氨基酸的多肽；其中该片段具有α-淀粉酶活性。在一方面，片段包含SEQ ID NO:1的至少200个连续的氨基酸残基，例如SEQ ID NO:1的至少300个连续的氨基酸残基、或至少350个连续的氨基酸残基、或至少400个连续的氨基酸残基、或至少450个连续的氨基酸残基。
宿主细胞：术语“宿主细胞”意指易于用包含本发明的多核苷酸的核酸构建体或表达载体转化、转染、转导等的任何细胞类型。术语“宿主细胞”涵盖由于复制过程中发生的突变而与亲本细胞不同的亲本细胞的任何后代。
改进因子：术语“改进因子”意指计算根据本发明的变体的具体特性的改进的定量方式。改进因子可以根据以下公式确定：
可以使用其他公式来确定改进因子。本领域技术人员知道目前提出的公式以及计算改进因子的替代方法。
根据本发明，1.0的值对应于针对亲本α-淀粉酶观察到的比活性。高于1.0的值指示与亲本α-淀粉酶相比所测试的变体的比活性的改进。因此，>1.0的任何值指示与亲本α-淀粉酶相比该变体的特性(如比活性)的改进。1.0的值表明变体的特性与亲本α-淀粉酶至少相当。
分离的：术语“分离的”意指在自然界中不存在的形式或环境中的一种物质。分离的物质的非限制性实例包括(1)任何非天然发生的物质，(2)包括但不限于任何酶、变体、核酸、蛋白质、肽或辅因子的任何物质，该物质至少部分地从与其本质相关的一种或多种或所有天然存在的成分中去除；(3)相对于天然发现的物质通过人工修饰的任何物质；或(4)通过相对于与其天然相关的其他组分，增加该物质的量而修饰的任何物质(例如，编码该物质的基因的多个拷贝；比与编码该物质的基因天然相关联的启动子更强的启动子的使用)。分离的物质可以存在于发酵液样品中。
成熟多肽：术语“成熟多肽”意指在翻译和任何翻译后修饰如N-末端加工、C-末端截短、糖基化作用、磷酸化作用等之后处于其最终形式的多肽。本领域内公知，宿主细胞可以产生由相同多核苷酸表达的两种或更多种不同的成熟多肽(即，具有不同的C-末端和/或N-末端氨基酸)的混合物。
成熟多肽编码序列：术语“成熟多肽编码序列”意指编码具有α-淀粉酶活性的成熟多肽的多核苷酸。
突变：在本发明多肽的上下文中，术语“突变”意指在参考氨基酸序列(即SEQ IDNO:1)内的一个或多个氨基酸通过用不同的氨基酸取代或通过缺失而改变。此外，突变可以对应于在参考氨基酸序列内一个或多个额外的氨基酸的插入。
核酸构建体：术语“核酸构建体”意指单-链或双-链的核酸分子，该核酸分子是从天然存在的基因中分离的，或以本来不存在于自然界中的方式被修饰成包含核酸的区段，或者其是合成的，该核酸分子包括一个或多个控制序列。
可操作地连接：术语“可操作地连接”意思指这样一种配置，在该配置中，一个控制序列被放置在相对于多核苷酸的编码序列适当的位置处，这样使得该控制序列引导该编码序列的表达。
亲本或亲本α-淀粉酶：术语“亲本”或“亲本α-淀粉酶”意指SEQ ID NO:1的α-淀粉酶(通过诺维信公司(Novozymes A/S)在商品名“
Plus”下商品化；参见WO2006/002643)。
序列一致性：两个氨基酸序列之间或两个核苷酸序列之间的相关性是通过参数“序列一致性”进行描述。
出于本发明的目的，使用如在EMBOSS包(EMBOSS：欧洲分子生物学开放软件套件，Rice等人，2000,Trends Genet.[遗传学趋势]16:276-277)(优选5.0.0版或更新版本)的Needle程序中所实施的Needleman-Wunsch算法(Needleman和Wunsch,1970,J.Mol.Biol.[分子生物学杂志]48:443-453)来确定两个氨基酸序列之间的序列一致性。使用的参数可以是缺口开放罚分10、缺口扩展罚分0.5、以及EBLOSUM62(BLOSUM62的EMBOSS版本)取代矩阵。将标记为“最长一致性”的尼德尔输出(使用-非简化(-nobrief)选项获得)用作百分比一致性并且如下计算：
(同一的残基X 100)/(比对长度-比对中的空位总数)
可替代地，所使用的参数可以是空位开放罚分10，空位延伸罚分0.5和EDNAFULL(NCBI NUC4.4的EMBOSS版本)取代矩阵。将标记为“最长一致性”的尼德尔输出(使用-非简化(-nobrief)选项获得)用作百分比一致性并且如下计算：
(同一的脱氧核糖核苷酸×100)/(比对长度-在比对中的空位总数)
子序列：术语“子序列”意指使一个或多个(例如，若干个)核苷酸从成熟多肽编码序列的5'端和/或3'端缺失的多核苷酸；其中该子序列编码具有α-淀粉酶活性的片段。
变体：术语“变体”意指相对于SEQ ID NO:1的“亲本”α-淀粉酶的位置，在一个或多个(例如，若干个)位置包含突变(即，取代、插入、和/或缺失)的具有α-淀粉酶活性的多肽。取代意指用不同的氨基酸替代占用某一位置的氨基酸；缺失意指去除占用某一位置的氨基酸；并且插入意指在邻接并且紧随占用某一位置的氨基酸之后添加氨基酸。本发明的变体具有SEQ ID NO:1的成熟多肽的至少20％，例如至少40％、至少50％、至少60％、至少70％、至少80％、至少90％、至少95％或至少100％的α-淀粉酶活性。
野生型α-淀粉酶：术语“野生型α-淀粉酶”意指由天然存在的微生物(例如自然界中发现的细菌、酵母或丝状真菌)表达的α-淀粉酶。
变体命名规则
具有α-淀粉酶活性的本发明的多肽对应于衍生自芽孢杆菌属的α-淀粉酶的变体(如在SEQ ID NO:1中显示)(其由诺维信公司(Novozymes A/S)，在商品名Stainzyme PlusTM下销售)。
本发明多肽中的变体(即突变的氨基酸)通过参考SEQ ID NO:2(其对应于枯草芽孢杆菌的成熟蛋白AA560)的氨基酸编号来定义。以下以粗体、下划线显示了相对于SEQ IDNO:1的氨基酸序列差异。
相应地，SEQ ID NO:2中的氨基酸位置1至182对应于SEQ ID NO:1中的相同编号，SEQ ID NO:2的氨基酸位置183至184在SEQ ID NO:1中不存在，并且SEQ ID NO:2的氨基酸位置185至485分别对应于SEQ ID NO:1的位置183至483。
因此，出于本发明的目的，使用在SEQ ID NO:2中披露的成熟多肽来确定另一种α-淀粉酶多肽中的对应氨基酸残基。将另一种α-淀粉酶的氨基酸序列与SEQ ID NO:2中披露的成熟多肽进行比对，并且基于该比对，使用如在EMBOSS包(EMBOSS：欧洲分子生物学开放软件套件，Rice等人，2000，Trends Genet.[遗传学趋势]16:276-277)(优选5.0.0版或更新版本)的尼德尔程序中所实施的尼德尔曼-翁施算法(Needleman和Wunsch，1970，J.Mol.Biol.[分子生物学杂志]48:443-453)来确定与SEQ ID NO:2中所披露的成熟多肽中的任何氨基酸残基相对应的氨基酸位置编号。使用的参数是缺口开放罚分10、缺口扩展罚分0.5、以及EBLOSUM62(BLOSUM62的EMBOSS版本)取代矩阵。
可以通过使用若干计算机程序，使用其对应默认参数比对多个多肽序列来确定在另一种α-淀粉酶中的对应氨基酸残基的鉴定，所述计算机程序包括但不限于MUSCLE(通过对数预期的多序列比较；版本3.5或更新版本；Edgar，2004，Nucleic Acids Research[核酸研究]32:1792-1797)，MAFFT(版本6.857或更新版本；Katoh和Kuma，2002，Nucleic AcidsResearch[核酸研究]30:3059-3066；Katoh等人，2005，Nucleic Acids Research[核酸研究]33:511-518；Katoh和Toh，2007，Bioinformatics[生物信息学]23:372-374；Katoh等人，2009，Methods in Molecular Biology[分子生物学方法]537:_39-64；Katoh和Toh，2010，Bioinformatics[生物信息学]26:_1899-1900)，以及采用ClustalW(1.83或更新版本；Thompson等人，1994，Nucleic Acids Research[核酸研究]22:4673-4680)的EMBOSS EMMA。
当其他α-淀粉酶与SEQ ID NO:2的成熟多肽相背离使得传统的基于序列的比较方法不能检测其相互关系时(Lindahl和Elofsson，2000，J.Mol.Biol.[分子生物学杂志]295:613-615)，可以应用其他成对序列比较算法。在基于序列的搜索中较高的敏感度可使用搜索程序来获得，这些搜索程序采用多肽家族的概率表现(谱)来搜索数据库。例如，PSI-BLAST程序通过迭代数据库搜索过程来产生多个谱，并且能够检测远距离同源物(Atschul等人，1997,Nucleic Acids Res.[核酸研究]25:3389-3402)。如果多肽的家族或超家族具有在蛋白结构数据库中的一个或多个代表，甚至可以实现更高的敏感度。程序如GenTHREADER(Jones,1999,J.Mol.Biol.[分子生物学杂志]287:797-815；McGuffin和Jones,2003,Bioinformatics[生物信息学]19:874-881)利用来自多种来源(PSI-BLAST、二级结构预测、结构比对谱和溶剂化势)的信息作为预测查询序列的结构折叠的神经网络的输入。类似地，Gough等人，2000,J.Mol.Biol.[分子生物学杂志]313:903-919的方法可以用于比对未知结构的序列与存在于SCOP数据库中的超家族模型。这些比对进而可以用于产生多肽的同源性模型，并且使用出于该目的而开发的多种工具可以评估此类模型的准确度。
对于已知结构的蛋白质，若干工具和资源可用于检索并产生结构比对。例如，蛋白质的SCOP超家族已经在结构上进行比对，并且那些比对是可访问且可下载的。可以使用多种算法如距离比对矩阵(Holm和Sander,1998,Proteins[蛋白质]33:88-96)或组合延伸(Shindyalov和Bourne,1998,Protein Engineering[蛋白质工程]11:739-747)比对两种或更多种蛋白质结构，并且这些算法的实施可以另外用于查询具有感兴趣结构的结构数据库，以便发现可能的结构同源物(例如，Holm和Park,2000,Bioinformatics[生物信息学]16:566-567)。
在描述本发明的α-淀粉酶变体中，以下所述的命名法适于引用方便。采用了已接受的IUPAC单字母和三字母的氨基酸缩写。
取代：对于氨基酸取代，使用以下命名法：原始氨基酸、位置、被取代的氨基酸。因此，在位置226处的苏氨酸被丙氨酸取代表示为“Thr226Ala”或者“T226A”。多个突变由加号(“+”)分开，例如“Gly205Arg+Ser411Phe”或“G205R+S411F”表示在位置205和位置411处的甘氨酸(G)和丝氨酸(S)分别被精氨酸(R)和苯丙氨酸(F)取代。
缺失：对于氨基酸缺失，使用以下命名法：原始氨基酸、位置、*。因此，将在位置195处的甘氨酸的缺失表示为“Gly195*”或“G195*”。多个缺失由加号(“+”)分开，例如，“Gly195*+Ser411*”或“G195*+S411*”。
插入：对于氨基酸插入，使用以下命名法：原始氨基酸、位置、原始氨基酸、插入的氨基酸。因此，将在位置195处的甘氨酸之后插入赖氨酸表示为“Gly195GlyLys”或“G195GK”。将多个氨基酸的插入表示为[原始氨基酸、位置、原始氨基酸、插入氨基酸#1、插入氨基酸#2等]。例如，在位置195处的甘氨酸之后插入赖氨酸和丙氨酸被表示为“Gly195GlyLysAla”或“G195GKA”。
在此类情况下，通过将小写字母添加至在所插入的氨基酸残基之前的氨基酸残基的位置编号中来对所插入的氨基酸残基进行编号。在以上实例中，该序列因此将是：
| <u>亲本：</u> | <u>变体：</u> |
| 195 | 195 195a 195b |
| G | G-K-A |
多种改变：包含多种改变的变体由加号(“+”)分开，例如“Arg170Tyr+Gly195Glu”或“R170Y+G195E”表示在位置170和位置195处的精氨酸和甘氨酸分别被酪氨酸和谷氨酸取代。
不同改变：在可以在某一位置引入不同的改变的情况下，所述不同的改变由逗号分开，例如“Arg170Tyr,Glu”表示在位置170处的精氨酸被酪氨酸或谷氨酸取代。因此，“Tyr167Gly,Ala+Arg170Gly,Ala”表示以下变体：
“Tyr167Gly+Arg170Gly”、“Tyr167Gly+Arg170Ala”、“Tyr167Ala+Arg170Gly”以及“Tyr167Ala+Arg170Ala”。
本发明的详细描述
具有α-淀粉酶活性的多肽
本发明涉及变体α-淀粉酶多肽，该变体α-淀粉酶多肽在SEQ ID NO:1的成熟多肽的氨基酸序列内的一个或多个(例如，若干个)位置处包含突变，其中与SEQ ID NO:1的多肽相比，该变体展现增强的洗涤性能。
在一个实施例中，本发明涉及包含SEQ ID NO:1的变体氨基酸序列的多肽，其中与SEQ ID NO:1的多肽相比，该多肽具有α-淀粉酶活性并展现增强的洗涤性能。
在一个实施例中，该变体氨基酸序列在SEQ ID NO:1的氨基酸位置167处包含突变。
因此，在一个实施例中，该变体氨基酸序列在SEQ ID NO:1的氨基酸位置167处包含取代，如W167Y。
亲本α-淀粉酶的氨基酸序列显示如下：
本发明的多肽代表SEQ ID NO:1的亲本α淀粉酶的变体，该变体在家庭和/或工业清洗过程(如衣物清洗和餐具洗涤)中展现增强的洗涤性能。可以使用本领域熟知的方法来确定洗涤性能，如使用自动餐具洗涤(ADW)(参见实例2)或自动机械应力测定(AMSA)(参见实例3)。
在一个实施例中，多肽在高温洗涤过程中展现增强的洗涤性能，例如其中温度是至少40℃，如至少45℃、如至少50℃、如至少55℃、以及如至少60℃。
在一个实施例中，使用经淀粉染色的三聚氰胺瓷砖在自动餐具洗涤(ADW)测定中评估增强的洗涤性能。用于确定本发明多肽的这种增强的洗涤性能的示例性洗涤条件包括：
a.标准ADW洗涤剂、具有漂白剂、在40℃下、以及10min的洗涤循环；
b.标准ADW洗涤剂、没有漂白剂、在40℃下、以及10min的洗涤循环；
c.标准ADW洗涤剂、具有漂白剂、在50℃下、以及20min的洗涤循环；以及
d.标准ADW洗涤剂、没有漂白剂、在50℃下、以及20min的洗涤循环；
其中所述标准ADW洗涤剂包含甲基甘氨酸二乙酸的三钠盐(如Trilon M颗粒SG)、柠檬酸钠、碳酸钠、硅酸钠、硫酸钠、多磷酸盐和硅酸盐阻垢剂(如Acusol 588G)和Surfac23-6.5。
除了增强的洗涤性能之外，本领域技术人员将会理解相对于SEQ ID NO:1的亲本α淀粉酶，本发明的多肽还可以展现一种或多种以下特性的改进：
(i)底物特异性；
(ii)底物结合；
(iii)比活性；
(iv)热稳定性
(v)pH稳定性曲线；
(vi)Ca2+依赖性；
(vii)氧化稳定性；
(viii)增加的/减少的pI；和/或
(ix)对表面活性剂的敏感性。
用于确定多肽的以上特性的测定描述于WO 2006/002643、WO 2001/066712和EP 2264 460A中。
本发明的多肽可以比SEQ ID NO:1的亲本α-淀粉酶更长或更短。因此，该多肽的长度可以是1000个或更少氨基酸，例如900个、800个、700个、600个、500个、400个、300个、200个、175个、150个、125个、100个或更少氨基酸。在一个实施例中，该多肽的长度是在400个和600个氨基酸之间，例如长度在450个和500个之间、在460个和500个之间、或在470个和490个氨基酸之间。
本发明的变体多肽在相对于SEQ ID NO:1的“亲本”α-淀粉酶的一个或多个氨基酸位置处包含突变(即，取代、插入、和/或缺失)。
这些氨基酸改变可以具有微小性质，即，不会显著地影响蛋白的折叠和/或活性的保守氨基酸取代或插入；典型为1-30个氨基酸的小缺失；小的氨基或羧基-末端延伸，如氨基末端的甲硫氨酸残基；多至20-25个残基的小接头肽；或小的延伸，其通过改变净电荷或另一功能(如聚组氨酸段、抗原表位或结合结构域)来促进纯化。
保守取代的实例是在下组之内：碱性氨基酸(精氨酸、赖氨酸及组氨酸)、酸性氨基酸(谷氨酸和天冬氨酸)、极性氨基酸(谷氨酰胺和天冬酰胺)、疏水性氨基酸(亮氨酸、异亮氨酸及缬氨酸)、芳香族氨基酸(苯丙氨酸、色氨酸及酪氨酸)及小氨基酸(甘氨酸、丙氨酸、丝氨酸、苏氨酸及甲硫氨酸)。一般不会改变比活性的氨基酸取代是本领域已知的并且例如由H.Neurath和R.L.Hill,1979,于The Proteins[蛋白质],Academic Press[学术出版社],New York[纽约]中进行了描述。常见取代是Ala/Ser、Val/Ile、Asp/Glu、Thr/Ser、Ala/Gly、Ala/Thr、Ser/Asn、Ala/Val、Ser/Gly、Tyr/Phe、Ala/Pro、Lys/Arg、Asp/Asn、Leu/Ile、Leu/Val、Ala/Glu和Asp/Gly。
可替代地，这些氨基酸变化具有这样的性质：改变多肽的物理化学特性。例如，氨基酸改变可以提高多肽的热稳定性、改变底物特异性、改变最适pH等。
可以根据本领域中已知的程序，如定点诱变或丙氨酸扫描诱变(Cunningham和Wells,1989,Science[科学]244:1081-1085)来鉴定多肽中的必需氨基酸。在后一项技术中，在分子中的每个残基处引入单个丙氨酸突变，并且测试所得突变分子的α-淀粉酶活性以鉴定对分子的活性关键的氨基酸残基。还参见，Hilton等人，1996,J.Biol.Chem.[生物化学杂志]271:4699-4708。酶或其他生物学相互作用的活性位点还可以通过对结构的物理分析来确定，如通过这样的技术确定：如核磁共振、晶体学、电子衍射或光亲和标记，连同对推定的接触位点氨基酸进行突变。参见，例如，de Vos等人，1992，Science[科学]255:306-312；Smith等人，1992,J.Mol.Biol.[分子生物学杂志]224:899-904；Wlodaver等人，1992，FEBS Lett.[欧洲生化学会联合会快报]309:59-64。还可以从与相关多肽的比对来推断必需氨基酸的身份。
在一个可替代的或另外的实施例中，本发明的多肽是SEQ ID NO:1的α-淀粉酶的变体，该变体在对应于以下位置的一个或多个位置处具有突变(如取代、缺失、和/或插入)：10、25、30、37、40、48、51、54、64、81、86、93、98、105、108、109、113、116、118、121、130、135、138、142、167、174、175、178、182、186、187、189、195、198、202、203、206、208、210、214、218、235、238、242、243、246、247、250、255、257、259、260、261、265、267、269、270、274、275、276、281、295、298、299、311、319、320、334、339、360、365、366、383、384、385、394、398、402、404、416、434、460、469、474、和482，其中编号是根据列于SEQ ID NO:2中的氨基酸序列。
因此，相对于SEQ ID NO:2的氨基酸序列，该多肽可以包含以下取代中的一个或多个：M10L、N25K、D30N、K37H、K37L、K37M、K37R、K37V、S40T、W48F、A51Q、A51T、N54S、Y64W、T81S、Q86H、Q86I、Q86L、K93H、K93R、Q98R、M105Y、M105F、M105I、M105L、K108R、G109A、G109M、A113E、M116I、M116L、M116A、M116V、M116F、K118Q、K118H、K118N、K118R、E121H、E130H、E130Q、Y135H、E138Q、K142R、K142Q、W167Y、W167H、N174Q、N174*、N175Q、Y178W、T182G、A186D、A186G、W187Y、W189H、F195N、Y198F、L202M、Y203H、Y203N、Y203G、Y203F、I206L、M208F、M208L、M208V、H210N、V214R、V214T、V214I、R218N、I235V、I235L、I235M、V238T、V238A、K242P、Y243F、Y243M、T246V、T246I、T246L、T246M、R247K、I250L、I250V、S255K、I257A、K259N、N260D、M261L、M261A、A265G、F267Y、K269S、K269N、N270G、A274K、I275L、E276Q、K281H、F295Y、F295W、Y298W、Y298F、Y299W、Y299F、Q311T、Q311H、Q311R、Q319H、Q319R、K320H、K320R、S334T、S339A、E360F、S365M、S365C、V366I、K383Q、K383R、S384E、K385H、K385Q、K385R、Q394K、Y398W、N402Y、Y404W、E416L、A434D、G460E、W469F、V474C、和W482Y。
例如，本发明的多肽可以选自下组，该组由以下组成：具有以下突变的SEQ ID NO:1的氨基酸序列的多肽；E360F+S365C(即，具有基于SEQ ID NO:1的氨基酸序列的多肽，但是具有突变E360F和S365C)、K37H+L202M、M261L、H210N、Y243F、K108R、V474C、G460E、T81S、K269S+N270G+A274K、K37V+L202M、L202M+Q311R、N174Q+L202M、K385H、K385Q、K385R、K383Q、K320H、K320R、E276Q、K93R、K93H、Q98R、K118Q、K118H、K118N、E130H、E130Q、E138Q、K142R、K142Q、E416L、Q394K、S384E、Y64W、K37R、D30N、F295Y、Y243M、Y178W、K281H、K269N、Y198F、Q311T、F195N、I257A、S255K、R247K、Y404W、Y398W、Q319H、Q319R、Q311H、Q311R、Y299W、N260D、K259N、Y299F、A434D、V366I、S365M、S339A、N174*、I235V、I250L、I250V、K37V、K37M、K37L、Y203H、S40T、W187Y、V238T、M105Y、M105F、M105I、I206L、T182G、M116I、Y135H、Y203N、Y203G、N25K、M116L、A265G、F295Y、A265G、K242P、V214R、M208F、Y198F、W482Y、V214T、V214I、M261A、M105F、M208L、M116A、N174Q、N174*+N175Q、I235L、A265G、M105L、K37H、Q311R、W469F、Y203F、G109A、N175Q、W48F、M116V、M116F、F295W、Y298W、M208V、M208F、M10L+M261L、W187Y+M208L、Y298F、W167Y、W167H、W189H、F295Y、I235M、Y243F+F267Y、K37V+P45R+K383R、D30N+N33D+K37V+K383R、W167Y+H210N+S339A+V366I、S339A+V366I、W167Y+H210N+S339A、H210N+S339A、W167Y+H210N、W167Y+L202M+H210N+Y299F+S339A+V366I、W167Y+H210N+Y243F+S339A+V366I、W167Y+H210N+S339A+V366I+W482Y、M116F+W167Y+H210N+S339A+V366I、W48F+W167Y+H210N+S339A+V366I、W167Y+H210N+Y299F+S339A+V366I、W167Y+L202M+H210N+S339A+V366I、W167Y+L202M+H210N+Y299F+S339A、W167Y+H210N+S339A+W482Y、M116F+W167Y+H210N+S339A、W48F+W167Y+H210N+S339A、W167Y+H210N+Y299F+S339A、W167Y+L202M+H210N+S339A、W167Y+L202M+Y299F、W167Y+Y243F、M116F+W167Y、W48F+W167Y、W167Y+Y299F、W167Y+L202M、W167Y+H210N+V366I、W167Y+V366I、H210N+V366I、W167Y+S339A+V366I、D30N+N33D+K37V+L202M+K383R、D30N+N33D+K37V+W48F+K383R、D30N+N33D+K37V+M116F+K383R、D30N+N33D+K37V+K383R+W482Y、A51T、A51T+N54S、S334T、T246M、T246L、T246V、T246I、A186G、A51Q+G109M+Y203G、V238A+S334T、A51T+L202M、L202M+T246L、A51T+N174Q+L202M+T246I+S334T、A51T+N174Q+L202M+Q311R+S334T、I235L+T246M+I250L、A186D+L202M、A186D+L202M+N270G+N402Y、A186D+L202M+S339A、A186D+F195N+L202M、K37H+A51T+L202M、K37V+、A51T+L202M、A51T+L202M+S365C、A51T+L202M+S339A、A51T+L202M+Q311T、A51T+L202M+M261L、A51T+L202M+H210N、A51T+L202M+N270G、A51T+F195N+L202M、A51T+L202M+Q319H、A51T+L202M+Q319R、A51T+L202M+Q311H、A51T+L202M+R247K、A51T+L202M+Q311R、A51T+L202M+Y398W、A51T+L202M+Y299W、A51T+K108R+L202M、A51T+L202M+Y243F、A51T+L202M+V474C、A51T+L202M+G460E、N174Q+L202M+A265G+Q311R+S334T、A51T+L202M+T246V+A265G+Q311R、A51T+L202M+A265G+Q311R、K37H+L202M+T246V+S334T、L202M+T246V+S334T+E416L、L202M+T246V+S334T+N402Y、L202M+T246V+S334T+V366I、L202M+T246V+S334T+S365M、L202M+T246V+S334T+S365C、L202M+T246V+M261L+S334T、D30N+L202M+H210N+T246V+S334T、L202M+T246V+N270G+S334T、F195N+L202M+T246V+S334T、L202M+T246V+Q319H+S334T、L202M+T246V+Q319R+S334T、L202M+T246V+Q311H+S334T、L202M+T246V+Q311R+S334T、L202M+T246V+S334T+Y398W、L202M+T246V+K320H+S334T、L202M+T246V+Y299W+S334T、L202M+T246V+K320R+S334T、L202M+Y243F+S334T、L202M+T246V+S334T+V474C、L202M+T246V+S334T+G460E、L202M+I235M+T246V+S334T、K108R+L202M+T246V+S334T、A51T+A186D+L202M+N270G+N402Y、A186D+L202M+N270G+S339A+N402Y、A51T+A186D+L202M+N270G、A51T+L202M+T246V+N270G、K37H+A51T+L202M+N270G、A51T+L202M+T246L+N270G、A51T+N174Q+L202M+N270G、A51T+L202M+V238A+N270G、A51T+L202M+A265G、A51T+L202M+M261L+N270G、A51T+L202M+F267Y、A51T+L202M+I275L、A51T+L202M+N270G+S365M、A51T+L202M+N270G+S365C、A51T+L202M+N270G+Q311T、A51T+L202M+N270G+E416L、A51T+L202M+N270G+N402Y、A51T+L202M+N270G+S365C、A51T+L202M+N270G+K383R、A51T+L202M+N270G+V474C、A51T+L202M+N270G+G460E、A51T+Q86L+L202M+N270G、A51T+Q86I+L202M+N270G、A51T+A113E+L202M+N270G、A51T+K93H+L202M+N270G、A51T+K108R+L202M+N270G、A51T+L202M+K269N、A51T+L202M+Y243F+N270G、A51T+F195N+L202M+N270G、A51T+L202M+R247K+N270G、A51T+L202M+R218N+N270G、A51T+L202M+S255K+N270G、A51T+L202M+I257A+N270G、A51T+L202M+V214I+R218N+N270G、A51T+L202M+N270G+Q311H、A51T+L202M+N270G+K320H、A51T+L202M+N270G+Y299W、A51T+L202M+N270G+K320R、A51T+L202M+N270G+K383Q、A51T+K142R+L202M+N270G、A51T+E130Q+L202M+N270G、A51T+K118N+L202M+N270G、A51T+E138Q+L202M+N270G、A51T+K118H+L202M+N270G、A51T+K118Q+L202M+N270G、A51T+Q86H+L202M+N270G、A51T+E121H+L202M+N270G、A51T+K118R+L202M+N270G、K37H+A51T+N174Q+L202M+A265G+Q311R+S334T、A51T+N174Q+L202M+T246I+Q311R+S334T、K37V+A51T+L202M+A265G+F267Y+Q311R+S334T、A51T+N174Q+L202M+A265G+F267Y+Q311R+S334T、A51G+L202M+Q311R+S334T、L202M+T246I+A265G+F267Y+Q311R+S334T、A51T+L202M+F267Y+Q311R+S334T+S365L、A51T+L202M+S365C、A51T+K108R+L202M、A51T+S365C、A51T+K108R、L202M+V238A+S334T、W48F+V238A+S334T、M116F+V238A+S334T、V238A+S334T+W482Y、Y243F+S334T、L202M+V238A+Y299F+S334T、L202M+T246V+N270G+S334T、W48F+K118H+V238A+S334T、W48F+L202M+V238A+S334T、A51T+A186N+L202M+N270G+S365C、W167Y+A186N+H210N+S339A+V366I、W48F+W167Y+A186N+H210N+S339A、W167Y+A186N+H210N+Y299F+S339A+V366I、L202M+T246V+N270G+S334T+S365C、A186N+L202M+T246V+N270G+S334T，及其具有α淀粉酶活性的片段，其中氨基酸位置的编号是根据列于SEQ ID NO:2中的氨基酸序列。
在一个实施例中，当在包含漂白剂的洗涤剂的ADW测定中，并且在40℃进行10min评估多肽时，该多肽展现对应于至少1.2的改进因子(IF)的增强的洗涤性能(例如，参见实例2)。适合的多肽可以是SEQ ID NO:1的变体，该变体在对应于以下位置的一个或多个位置处包含突变：37、51、93、98、108、118、167、186、202、210、235、243、246、247、250、255、259、260、261、270、299、311、319、334、339、365、385、398、和404，其中氨基酸位置的编号是根据列于SEQ ID NO:2中的氨基酸序列。例如，该多肽可以选自下组，该组由以下组成：具有以下突变的SEQ ID NO:1的氨基酸序列的多肽：K37H+L202M、M261L、Y243F、K385H、K385R、K93H、Q98R、K118Q、K118H、S255K、Y404W、Y398W、Q319R、Y299W、N260D、K259N、Y299F、S339A、S334T、A51T+L202M、I235L+T246M+I250L、K37V+A51T+L202M、A51T+L202M+S365C、A51T+L202M+Q311T、A51T+L202M+M261L、A51T+L202M+R247K、A51T+L202M+Y299W、A51T+K108R+L202M、A51T+L202M+Y243F、A51T+A186D+L202M+N270G、A51T+L202M+N270G+S365C、W167Y+A186N+H210N+S339A+V366I、W48F+W167Y+A186N+H210N+S339A、或W167Y+A186N+H210N+Y299F+S339A+V366，及其具有α淀粉酶活性的片段，其中氨基酸位置的编号是根据列于SEQ ID NO:2中的氨基酸序列。
在另一个实施例中，当在包含漂白剂的洗涤剂的ADW测定中，并且在50℃进行20min评估多肽时，该多肽展现对应于至少1.2的IF的增强的洗涤性能(例如，参见实例2)。适合的多肽可以是SEQ ID NO:1的变体，该变体在对应于以下位置的一个或多个位置处包含突变：30、33、37、40、48、51、81、86、93、105、108、116、118、130、138、142、167、174、175、182、186、195、198、202、206、210、235、238、243、246、247、250、255、257、259、260、261、265、266、267、269、270、299、311、319、320、334、339、360、365、366、383、385、402、416、474、和482，其中氨基酸位置的编号是根据列于SEQ ID NO:2中的氨基酸序列。例如，该多肽可以选自下组，该组由以下组成：具有以下突变的SEQ ID NO:1的氨基酸序列的多肽：K37H+L202M、E360F+S365C、M261L、H210N、Y243F、K108R、V474C、T81S、K385H、K385Q、K385R、K93R、K118Q、K118N、E130H、E130Q、E138Q、K37R、D30N、Y243M、K269N、Y198F、Q311T、F195N、I257A、S255K、R247K、Y404W、Y398W、Q319H、Q319R、Q311H、Q311R、Y299W、N260D、K259N、Y299F、V366I、S365M、S339A、I250L、I250V、K37M、S40T、V238T、M105F、M105I、I206L、T182G、M116I、M116L、N174Q、I235L、A265G、K37H、Q311R、N175Q、W48F、M116F、W167Y+H210N+S339A、H210N+S339A、W48F+W167Y+H210N+S339A、W48F+W167Y、W167Y+H210N+V366I、D30N+N33D+K37V+K383R+W482Y、A51T、S334T、T246M、T246L、T246V、T246I、A186G、V238A+S334T、A51T+L202M、A51T+N174Q+L202M+Q311R+S334T、I235L+T246M+I250L、L202M+T246V+S334T+E416L、D30N+L202M+H210N+T246V+S334T、L202M+T246V+N270G+S334T、F195N+L202M+T246V+S334T、L202M+T246V+K320R+S334T、L202M+Y243F+S334T、A51T+A186D+L202M+N270G+N402Y、A186D+L202M+N270G+S339A+N402Y、A51T+A186D+L202M+N270G、A51T+L202M+T246V+N270G、K37H+A51T+L202M+N270G、A51T+L202M+T246L+N270G、A51T+N174Q+L202M+N270G、A51T+L202M+V238A+N270G、A51T+L202M+A265G、A51T+L202M+M261L+N270G、A51T+L202M+F267Y、A51T+L202M+N270G+S365C、A51T+L202M+N270G+S365C、A51T+L202M+N270G+K383R、A51T+Q86I+L202M+N270G、A51T+K93H+L202M+N270G、A51T+K108R+L202M+N270G、A51T+L202M+N270G+K320H、A51T+L202M+N270G+K383Q、A51T+K142R+L202M+N270G、A51T+E130Q+L202M+N270G、A51T+E138Q+L202M+N270G、A51T+L202M+S365C、A51T+S365C、W48F+V238A+S334T、M116F+V238A+S334T、V238A+S334T+W482Y、Y243F+S334T、W48F+K118H+V238A+S334T、A51T+A186N+L202M+N270G+S365C、W167Y+A186N+H210N+S339A+V366I、W48F+W167Y+A186N+H210N+S339A、W167Y+A186N+H210N+Y299F+S339A+V366I、L202M+T246V+N270G+S334T+S365C、或A186N+L202M+T246V+N270G+S334T，及其具有α淀粉酶活性的片段，其中氨基酸位置的编号是根据列于SEQ IDNO:2中的氨基酸序列。
在另外的实施例中，当在没有漂白剂的洗涤剂的ADW测定中，并且在40℃进行10min评估多肽时，该多肽展现对应于至少1.2的改进因子(IF)的增强的洗涤性能(例如，参见实例2)。适合的多肽可以是SEQ ID NO:1的变体，该变体在对应于以下位置的一个或多个位置处包含突变：37、48、51、64、81、108、116、167、174、186、187、189、195、198、202、208、210、235、238、243、246、250、261、265、267、269、270、275、311、319、334、339、365、366、385、460、和474，其中氨基酸位置的编号是根据列于SEQ ID NO:2中的氨基酸序列。例如，该多肽可以选自下组，该组由以下组成：具有以下突变的SEQ ID NO:1的氨基酸序列的多肽：K37H+L202M、M261L、H210N、Y243F、K108R、G460E、T81S、N174Q+L202M、K385R、Y64W、Y243M、K269N、Y198F、S365M、S339A、W48F、M116V、M116F、W187Y+M208L、W167Y、W189H、W167Y+L202M+H210N+Y299F+S339A、W167Y+L202M+H210N+S339A、W167Y+L202M、V238A+S334T、A51T+L202M、L202M+T246L、A51T+N174Q+L202M+T246I+S334T、I235L+T246M+I250L、A186D+F195N+L202M、K37H+A51T+L202M、K37V+A51T+L202M、A51T+L202M+S365C、A51T+L202M+Q311T、A51T+L202M+M261L、A51T+L202M+Q319R、A51T+L202M+Q311H、A51T+K108R+L202M、A51T+L202M+V474C、A51T+A186D+L202M+N270G、K37H+A51T+L202M+N270G、A51T+L202M+A265G、A51T+L202M+M261L+N270G、A51T+L202M+F267Y、A51T+L202M+I275L、A51T+L202M+N270G+S365C、W167Y+A186N+H210N+S339A+V366I、W48F+W167Y+A186N+H210N+S339A、或W167Y+A186N+H210N+Y299F+S339A+V366I，及其具有α淀粉酶活性的片段，其中氨基酸位置的编号是根据列于SEQID NO:2中的氨基酸序列。
在仍另外的实施例中，当在没有漂白剂的洗涤剂的ADW测定中，并且在50℃进行20min评估多肽时，该多肽展现对应于至少1.2的IF的增强的洗涤性能(例如，参见实例2)。适合的多肽可以是SEQ ID NO:1的变体，该变体在对应于以下位置的一个或多个位置处包含突变：30、33、37、40、48、51、86、93、108、109、113、116、118、121、130、138、142、167、174、175、182、186、195、198、202、203、210、218、235、238、243、246、247、250、255、257、259、260、261、265、267、269、270、274、275、299、311、319、320、334、339、365、366、383、385、398、402、416、404、460、474、和482，其中氨基酸位置的编号是根据列于SEQ ID NO:2中的氨基酸序列。例如，该多肽可以选自下组，该组由以下组成：具有以下突变的SEQ ID NO:1的氨基酸序列的多肽：K269S+N270G+A274K、K37V+L202M、N174Q+L202M、K385H、K385R、K93H、K118Q、E130Q、E138Q、K37R、D30N、Y243M、K269N、Y198F、F195N、I257A、S255K、R247K、Y404W、Y398W、Q319H、Q319R、Q311H、Q311R、Y299W、N260D、K259N、Y299F、V366I、S365M、S339A、N174*、K37L、S40T、T182G、A265G、W482Y、M116A、N174Q、I235L、A265G、K37H、Q311R、N175Q、W48F、M116V、M116F、W167Y+L202M+H210N+S339A+V366I、W167Y+L202M+H210N+Y299F+S339A、W167Y+L202M+H210N+S339A、W167Y+L202M+Y299F、W48F+W167Y、W167Y+Y299F、W167Y+L202M、D30N+N33D+K37V+L202M+K383R、D30N+N33D+K37V+W48F+K383R、A51T、S334T、T246M、T246L、T246I、A186G、A51Q+G109M+Y203G、V238A+S334T、A51T+L202M、L202M+T246L、A51T+N174Q+L202M+T246I+S334T、A51T+N174Q+L202M+Q311R+S334T、I235L+T246M+I250L、A186D+L202M、A186D+L202M+N270G+N402Y、A186D+L202M+S339A、A186D+F195N+L202M、K37H+A51T+L202M、K37V+A51T+L202M、A51T+L202M+S365C、A51T+L202M+S339A、A51T+L202M+Q311T、A51T+L202M+M261L、A51T+L202M+H210N、A51T+L202M+N270G、A51T+F195N+L202M、A51T+L202M+Q319H、A51T+L202M+Q319R、A51T+L202M+Q311H、A51T+L202M+R247K、A51T+L202M+Q311R、A51T+L202M+Y398W、A51T+L202M+Y299W、A51T+K108R+L202M、A51T+L202M+Y243F、A51T+L202M+V474C、A51T+L202M+G460E、N174Q+L202M+A265G+Q311R+S334T、A51T+L202M+T246V+A265G+Q311R、K37H+L202M+T246V+S334T、L202M+T246V+S334T+E416L、L202M+T246V+S334T+N402Y、L202M+T246V+S334T+V366I、L202M+T246V+S334T+S365M、L202M+T246V+S334T+S365C、L202M+T246V+M261L+S334T、D30N+L202M+H210N+T246V+S334T、L202M+T246V+N270G+S334T、F195N+L202M+T246V+S334T、L202M+T246V+Q319H+S334T、L202M+T246V+Q319R+S334T、L202M+T246V+Q311H+S334T、L202M+T246V+Q311R+S334T、L202M+T246V+S334T+Y398W、L202M+T246V+K320H+S334T、L202M+T246V+Y299W+S334T、L202M+T246V+K320R+S334T、L202M+Y243F+S334T、L202M+T246V+S334T+V474C、L202M+T246V+S334T+G460E、L202M+I235M+T246V+S334T、K108R+L202M+T246V+S334T、A51T+A186D+L202M+N270G+N402Y、A186D+L202M+N270G+S339A+N402Y、A51T+A186D+L202M+N270G、A51T+L202M+T246V+N270G、K37H+A51T+L202M+N270G、A51T+L202M+T246L+N270G、A51T+N174Q+L202M+N270G、A51T+L202M+V238A+N270G、A51T+L202M+A265G、A51T+L202M+M261L+N270G、A51T+L202M+F267Y、A51T+L202M+I275L、A51T+L202M+N270G+S365M、A51T+L202M+N270G+S365C、A51T+L202M+N270G+Q311T、A51T+L202M+N270G+E416L、A51T+L202M+N270G+N402Y、A51T+L202M+N270G+S365C、A51T+L202M+N270G+K383R、A51T+L202M+N270G+V474C、A51T+L202M+N270G+G460E、A51T+Q86L+L202M+N270G、A51T+Q86I+L202M+N270G、A51T+A113E+L202M+N270G、A51T+K93H+L202M+N270G、A51T+K108R+L202M+N270G、A51T+L202M+K269N、A51T+L202M+Y243F+N270G、A51T+L202M+R247K+N270G、A51T+L202M+R218N+N270G、A51T+L202M+S255K+N270G、A51T+L202M+I257A+N270G、A51T+L202M+V214I+R218N+N270G、A51T+L202M+N270G+Q311H、A51T+L202M+N270G+K320H、A51T+L202M+N270G+Y299W、A51T+L202M+N270G+K320R、A51T+L202M+N270G+K383Q、A51T+K142R+L202M+N270G、A51T+E130Q+L202M+N270G、A51T+K118N+L202M+N270G、A51T+E138Q+L202M+N270G、A51T+K118H+L202M+N270G、A51T+E121H+L202M+N270G、K37H+A51T+N174Q+L202M+A265G+Q311R+S334T、A51T+N174Q+L202M+T246I+Q311R+S334T、K37V+A51T+L202M+A265G+F267Y+Q311R+S334T、A51T+N174Q+L202M+A265G+F267Y+Q311R+S334T、L202M+T246I+A265G+F267Y+Q311R+S334T、A51T+L202M+F267Y+Q311R+S334T+S365L、A51T+L202M+S365C、A51T+K108R+L202M、L202M+V238A+S334T、W48F+V238A+S334T、M116F+V238A+S334T、V238A+S334T+W482Y、Y243F+S334T、L202M+V238A+Y299F+S334T、L202M+T246V+N270G+S334T、W48F+K118H+V238A+S334T、W48F+L202M+V238A+S334T、A51T+A186N+L202M+N270G+S365C、W167Y+A186N+H210N+S339A+V366I、W48F+W167Y+A186N+H210N+S339A、W167Y+A186N+H210N+Y299F+S339A+V366I、L202M+T246V+N270G+S334T+S365C、或A186N+L202M+T246V+N270G+S334T，及其具有α淀粉酶活性的片段，其中氨基酸位置的编号是根据列于SEQ ID NO:2中的氨基酸序列。
在本发明的多肽的一个具体的子集中，该多肽是SEQ ID NO:1的变体，该变体在对应于以下位置的一个或多个位置处包含突变：48、118、167、186、210、235、238、243、246、250、299、334、339、366、和482，其中编号是根据SEQ ID NO:2。因此，该多肽可以由具有一个或多个突变的SEQ ID NO:1的氨基酸序列、或其具有α淀粉酶活性的片段组成，这些突变选自下组，该组由以下组成：W48F、K118H、W167Y、H210N、I235L、V238A、Y243F、T246M、I250L、Y299F、S334T、S339A、V366I、和W482Y，其中氨基酸位置的编号是根据列于SEQ ID NO:2中的氨基酸序列。例如，该多肽可以包含选自以下的氨基酸序列、及其具有α淀粉酶活性的片段或由它们组成：
(a)具有突变W167Y、H210N和S339A的SEQ ID NO:1；
(b)具有突变W167Y、H210N、S339A和V366I的SEQ ID NO:1；
(c)具有突变W167Y、H210N、Y299F、S339A和V366I的SEQ ID NO:1；
(d)具有突变W48F和W167Y的SEQ ID NO:1；
(e)具有突变W48F、W167Y、H210N和S339A的SEQ ID NO:1；
(f)具有突变W48F、W167Y、H210N、Y299F、S339A和V366I的SEQ ID NO:1；
(g)具有突变V238A、S334T、和W482Y的SEQ ID NO:1；
(h)具有突变Y243F和S334T的SEQ ID NO:1；
(i)具有突变W48F的SEQ ID NO:1；
(j)具有突变K118H的SEQ ID NO:1；
(k)具有突变W167Y的SEQ ID NO:1；
(l)具有突变W48F、V238A、和S334T的SEQ ID NO:1；
(m)具有突变I234L、T246M、和I250L的SEQ ID NO:1；
(n)具有突变S339A的SEQ ID NO:1；以及
(o)具有突变S334T的SEQ ID NO:1；
其中氨基酸位置的编号是根据列于SEQ ID NO:2中的氨基酸序列。
本发明的多肽代表亲本α-淀粉酶(SEQ ID NO:1)的氨基酸序列的变体，该变体展现增强的洗涤性能(例如，在40℃或更高的温度下)。本领域技术人员将会理解，本发明多肽的不同实例将与SEQ ID NO:1的序列具有不同程度的氨基酸序列一致性。因此，该多肽可以包含氨基酸序列或由其组成，该氨基酸序列与SEQ ID NO:1具有至少70％序列一致性，例如与SEQ ID NO:1具有至少75％、至少80％、至少85％、至少90％、至少95％、至少96％、至少97％、至少98％、或至少99％序列一致性。在一个实施例中，相对于SEQ ID NO:1的氨基酸序列，在该多肽内的变体的数量是在1个和20个之间，例如，在1个和10个突变之间或在1个和5个突变之间，如1个、2个、3个、4个、5个、6个、7个、8个、9个或10个突变。
本发明的α-淀粉酶多肽的实例显示在表1中(其中表明多肽的氨基酸序列相对于SEQ ID NO:1的亲本α-淀粉酶的序列)。
表1
在具体的实施例中，本发明的变体α-淀粉酶在40℃和50℃的温度下均具有增强的洗涤性能。此类变体α-淀粉酶可以选自
(a)具有突变V238A、S334T、和W482Y的SEQ ID NO:1；
(b)具有突变Y243F和S334T的SEQ ID NO:1；
(c)具有突变W48F、W167Y、H210N、Y299F、S339A、和V366I的SEQ ID NO:1；
(d)具有突变W48F、W167F、H210N、和S339A的SEQ ID NO:1；
(e)具有突变W48F的SEQ ID NO:1；以及
(f)具有突变W167Y、H210N、和S339A的SEQ ID NO:1，
及其具有α淀粉酶活性的片段，其中氨基酸位置的编号是根据列于SEQ ID NO:2中的氨基酸序列。
本发明的多肽的制备
可以使用本领域已知的任何诱变程序来制备本发明的变体α-淀粉酶，如定点诱变、合成基因构建、半合成基因构建、随机诱变、改组等。
定点诱变是在编码该亲本的多核苷酸中的一个或多个限定位点处引入一个或多个(例如，若干个)突变的技术。
通过涉及使用包含所希望的突变的寡核苷酸引物的PCR可以体外实现定点诱变。也可以通过盒式诱变进行体外定点诱变，该盒式诱变涉及由限制酶在包含编码亲本的多核苷酸的质粒中的位点处切割并且随后将包含突变的寡核苷酸连接在多核苷酸中。通常，消化该质粒与该寡核苷酸的限制酶是相同的，从而允许该质粒的粘性末端以及插入片段彼此连接。参见，例如，Scherer和Davis，1979，(Proc.Natl.Acad.Sci.USA[美国科学院院报])76:4949-4955；和Barton等人，1990，Nucleic Acids Res.[核酸研究]18:7349-4966。
还可以通过本领域已知的方法在体内实现定点诱变。参见例如，美国专利申请公开号2004/0171154；Storici等人，2001,Nature Biotechnol.[自然生物技术]19:773-776；Kren等人，1998,Nat.Med.[自然医学]4:285-290；以及Calissano和Macino,1996,FungalGenet.Newslett.[真菌遗传学通讯]43:15-16。
在本发明中可以使用任何定点诱变程序。存在许多可以用于制备变体的可商购的试剂盒。
合成基因构建需要体外合成设计的多核苷酸分子以编码感兴趣的多肽。基因合成可以利用多种技术来进行，如由Tian等人(2004，Nature[自然]432:1050-1054)所述的基于多路微芯片的技术、以及在光可编程的微流芯片上合成并组装寡核苷酸的类似技术。
使用已知的诱变、重组和/或改组方法、随后进行一个相关的筛选程序可以做出单一或多种氨基酸取代、缺失和/或插入并对其进行测试，这些相关的筛选程序例如由Reidhaar-Olson和Sauer，1988，Science[科学]241:53-57；Bowie和Sauer，1989，Proc.Natl.Acad.Sci.USA[美国国家科学院院刊]86：2152-2156；WO 95/17413；或WO 95/22625。其他可以使用的方法包括易错PCR、噬菌体展示(例如Lowman等人，1991，Biochemistry[生物化学]30:10832-10837；美国专利号5,223,409；WO 92/06204)以及区域定向诱变(Derbyshire等人，1986，Gene[基因]46:145；Ner等人，1988，DNA 7:127)。
诱变/改组方法可以与高通量自动化筛选方法组合以检测由宿主细胞表达的克隆的诱变多肽的活性(Ness等人，1999，Nature Biotechnology[自然生物技术]17:893-896)。可以从宿主细胞回收编码活性多肽的诱变的DNA分子，并且使用本领域的标准方法快速测序。这些方法允许迅速确定多肽中个体氨基酸残基的重要性。
通过组合合成基因构建、和/或定点诱变、和/或随机诱变、和/或改组的多方面来实现半合成基因的构建。半合成构建典型地是利用合成的多核苷酸片段的过程结合PCR技术。因此，基因的限定区域可以从头合成，而其他区域可以使用位点特异性诱变引物来扩增，然而还有其他区域可以进行易错PCR或非易错PCR扩增。然后可以对多核苷酸子序列进行改组。
多核苷酸
本发明还涉及编码本发明的变体的多核苷酸。因此，本发明涉及编码变体多肽的多核苷酸，该变体多肽具有α-淀粉酶活性并与SEQ ID NO:1的多肽相比展现增强的洗涤性能。具体而言，本发明涉及编码变体多肽的多核苷酸，该变体多肽在对应于以下位置的一个或多个位置处包含突变：10、25、30、37、40、48、51、54、64、81、86、93、98、105、108、109、113、116、118、121、130、135、138、142、167、174、175、178、182、186、187、189、195、198、202、203、206、208、210、214、218、235、238、242、243、246、247、250、255、257、259、260、261、265、267、269、270、274、275、276、281、295、298、299、311、319、320、334、339、360、365、366、383、384、385、394、398、402、404、416、434、460、469、474、和482，其中编号是根据列于SEQ ID NO:2中的氨基酸序列。
核酸构建体
本发明还涉及包含编码本发明的变体多肽的、可操作地连接至一个或多个控制序列上的多核苷酸的核酸构建体，该一个或多个控制序列在与控制序列相容的条件下指导编码序列在适合的宿主细胞中的表达。因此，本发明涉及包含多核苷酸的核酸构建体，该多核苷酸编码具有α-淀粉酶活性并与SEQ ID NO:1的多肽相比展现增强的洗涤性能的变体多肽，该多核苷酸可操作地连接到一个或多个控制序列上，该一个或多个控制序列在与这些控制序列相容的条件下指导编码序列在适合的宿主细胞中的表达。具体而言，本发明涉及编码变体多肽的核酸构建体，该变体多肽在对应于以下位置的一个或多个位置处包含突变：10、25、30、37、40、48、51、54、64、81、86、93、98、105、108、109、113、116、118、121、130、135、138、142、167、174、175、178、182、186、187、189、195、198、202、203、206、208、210、214、218、235、238、242、243、246、247、250、255、257、259、260、261、265、267、269、270、274、275、276、281、295、298、299、311、319、320、334、339、360、365、366、383、384、385、394、398、402、404、416、434、460、469、474、和482，其中编号是根据列于SEQ ID NO:2中的氨基酸序列，这些核酸构建体可操作地连接到一个或多个控制序列上，该一个或多个控制序列在与这些控制序列相容的条件下指导编码序列在适合的宿主细胞中的表达。
可以按多种方式来操纵多核苷酸以提供变体的表达。取决于表达载体，在其插入载体以前操纵多核苷酸可以是令人希望的或必需的。用于利用重组DNA方法修饰多核苷酸的技术是本领域熟知的。
控制序列可以是启动子，即由宿主细胞识别用于表达该多核苷酸的多核苷酸。启动子包含介导变体的表达的转录控制序列。启动子可以是在宿主细胞中显示出转录活性的任何多核苷酸，包括突变型、截短型和杂合型启动子，并且可以是从编码与宿主细胞同源或异源的细胞外或细胞内多肽的基因获得。
用于在细菌宿主细胞中指导本发明核酸构建体的转录的适合启动子的实例是从以下基因中获得的启动子：解淀粉芽孢杆菌α-淀粉酶基因(amyQ)、地衣芽孢杆菌α-淀粉酶基因(amyL)、地衣芽孢杆菌青霉素酶基因(penP)、嗜热脂肪芽孢杆菌产麦芽糖淀粉酶基因(amyM)、枯草芽孢杆菌果聚糖蔗糖酶基因(sacB)、枯草芽孢杆菌xylA和xylB基因、苏云金芽孢杆菌cryIIIA基因(Agaisse和Lereclus,1994,Molecular Microbiology[分子微生物学]13:97-107)、大肠杆菌lac操纵子、大肠杆菌trc启动子(Egon等人，1988,Gene[基因]69:301-315)、天蓝链霉菌琼脂水解酶基因(dagA)和原核β-内酰胺酶基因(Villa-Kamaroff等人，1978,Proc.Natl.Acad.Sci.USA[美国国家科学院院刊]75:3727-3731)以及tac启动子(DeBoer等人，1983,Proc.Natl.Acad.Sci.USA[美国国家科学院院刊]80:21-25)。其他启动子描述于Gilbert等人，1980，Scientific American[科学美国人]242:74-94的“Usefulproteins from recombinant bacteria[来自重组细菌的有用蛋白质]”中；和在Sambrook等人，1989，见上文。串联启动子的实例披露于WO 99/43835中。
用于指导本发明的核酸构建体在丝状真菌宿主细胞中的转录的适合启动子的实例是从以下各项的基因获得的启动子：构巢曲霉乙酰胺酶、黑曲霉中性α-淀粉酶、黑曲霉酸稳定性α-淀粉酶、黑曲霉或泡盛曲霉葡糖淀粉酶(glaA)、米曲霉TAKA淀粉酶、米曲霉碱性蛋白酶、米曲霉丙糖磷酸异构酶、尖镰孢胰蛋白酶样蛋白酶(WO 96/00787)、镶片镰孢淀粉葡糖苷酶(WO 00/56900)、镶片镰孢Daria(WO 00/56900)、镶片镰孢Quinn(WO 00/56900)、米黑根毛霉脂肪酶、米黑根毛霉天冬氨酸蛋白酶、里氏木霉β-葡糖苷酶、里氏木霉纤维二糖水解酶I、里氏木霉纤维二糖水解酶II、里氏木霉内切葡聚糖酶I、里氏木霉内切葡聚糖酶II、里氏木霉内切葡聚糖酶III、里氏木霉内切葡聚糖酶IV、里氏木霉内切葡聚糖酶V、里氏木霉木聚糖酶I、里氏木霉木聚糖酶II、里氏木霉β-木糖苷酶，以及NA2-tpi启动子(一种修饰的启动子，其来自曲霉属中性α-淀粉酶基因，其中未翻译的前导子由曲霉属丙糖磷酸异构酶基因的未翻译的前导子替代；非限制性实例包括来自编码中性α-淀粉酶的黑曲霉基因的修饰的启动子，其中已经用来自编码丙糖磷酸异构酶的构巢曲霉或米曲霉基因的未翻译的前导子替换未翻译的前导子)；及其突变型、截短型及杂合型启动子。
在酵母宿主中，有用的启动子从以下各项的基因获得：酿酒酵母烯醇酶(ENO-1)、酿酒酵母半乳糖激酶(GAL1)、酿酒酵母醇脱氢酶/甘油醛-3磷酸脱氢酶(ADH1、ADH2/GAP)、酿酒酵母丙糖磷酸异构酶(TPI)、酿酒酵母金属硫蛋白(CUP1)、以及酿酒酵母3磷酸甘油酸激酶。Romanos等人，1992，Yeast[酵母]8:423-488描述了酵母宿主细胞的其他有用的启动子。
控制序列也可为由宿主细胞识别以终止转录的转录终止子。该终止子序列被可操作地连接至编码该变体的多核苷酸的3’-末端。可以使用在宿主细胞中具有功能的任何终止子。
细菌宿主细胞的优选终止子从以下各项的基因获得：克劳氏芽孢杆菌碱性蛋白酶(aprH)、地衣芽孢杆菌α-淀粉酶(amyL)和大肠杆菌核糖体RNA(rrnB)。
丝状真菌宿主细胞的优选终止子是从以下各项的基因中获得的：构巢曲霉邻氨基苯甲酸合酶、黑曲霉葡糖淀粉酶、黑曲霉α-葡糖苷酶、米曲霉TAKA淀粉酶以及尖镰孢胰蛋白酶样蛋白酶。
用于酵母宿主细胞的优选终止子从以下各项的基因获得：酿酒酵母烯醇酶、酿酒酵母细胞色素C(CYC1)、以及酿酒酵母甘油醛-3磷酸脱氢酶。酵母宿主细胞的其他有用终止子在Romanos等人，1992，见上文描述。
控制序列还可为启动子下游和基因的编码序列上游的mRNA稳定子区域，其增加该基因的表达。
适合的mRNA稳定子区域的实例是从以下基因获得：苏云金芽孢杆菌cryIIIA基因(WO 94/25612)和枯草芽孢杆菌SP82基因(Hue等人，1995,Journal of Bacteriology[细菌学杂志]177:3465-3471)。
该控制序列也可以是前导序列，一种对宿主细胞翻译很重要的非翻译mRNA区域。前导子序列可操作地连接至编码该变体的多核苷酸的5’端。在宿主细胞中起作用的任何前导子都可以使用。
用于丝状真菌宿主细胞的优选前导序列是从米曲霉TAKA淀粉酶和构巢曲霉丙糖磷酸异构酶的基因获得的。
对于酵母宿主细胞适合的前导序列从以下酶的基因获得：酿酒酵母烯醇化酶(ENO-1)、酿酒酵母3-磷酸甘油酸激酶、酿酒酵母α因子、和酿酒酵母醇脱氢酶/甘油醛-3-磷酸脱氢酶(ADH2/GAP)。
该控制序列还可以是一种多腺苷酸化序列，即被可操作地连接至该变体编码序列的3’-末端并且当转录时由宿主细胞识别成将多腺苷酸残基添加到所转录的mRNA上的一个信号的一种序列。可以使用在宿主细胞中起作用的任何多腺苷酸化序列。
丝状真菌宿主细胞的优选多聚腺苷酸化从针对以下各项的基因获得：构巢曲霉邻氨基苯甲酸酯合酶、黑曲霉葡糖淀粉酶、黑曲霉-α葡糖苷酶、米曲霉TAKA淀粉酶、和尖孢镰刀菌胰蛋白酶样蛋白酶。
对于酵母宿主细胞有用的多聚腺苷酸化序列由Guo和Sherman，1995，Mol.Cellular Biol.[分子细胞生物学]15:5983-5990描述。
该控制序列还可以是信号肽编码区，编码与变体的N-末端连接的信号肽，并且指导该变体进入细胞的分泌通路。该多核苷酸的编码序列的5’-末端可以固有地包含信号肽编码序列，该信号肽编码序列在翻译阅读框中与编码该变体的编码序列的区段天然地连接在一起。可替代地，该编码序列的5’-末端可以包含对于该编码序列来说是外来的信号肽编码序列。在编码序列不天然地包含信号肽编码序列的情况下，可需要外来的信号肽编码序列。可替代地，外源信号肽编码序列可以简单地替换天然信号肽编码序列，以便增强变体的分泌。然而，可以使用指导表达的变体进入宿主细胞的分泌通路的任何信号肽编码序列。
用于细菌宿主细胞的有效信号肽编码序列是从以下各项的基因获得的信号肽编码序列：芽孢杆菌属NCIB 11837产麦芽糖淀粉酶、地衣芽孢杆菌枯草杆菌蛋白酶、地衣芽孢杆菌β-内酰胺酶、嗜热脂肪芽孢杆菌α-淀粉酶、嗜热脂肪芽孢杆菌中性蛋白酶(nprT、nprS、nprM)和枯草芽孢杆菌prsA。另外的信号肽由Simonen和Palva,1993,MicrobiologicalReviews[微生物评论]57:109-137描述。
用于丝状真菌宿主细胞的有效的信号肽编码序列是从以下酶的基因获得的信号肽编码序列：黑曲霉中性淀粉酶、黑曲霉葡糖淀粉酶、米曲霉TAKA淀粉酶、特异腐质霉(Humicola insolens)纤维素酶、特异腐质霉内切葡聚糖酶V、疏棉状腐质霉(Humicolalanuginosa)脂肪酶和米黑根毛霉天冬氨酸蛋白酶。
用于酵母宿主细胞的有用的信号肽从酿酒酵母α-因子和酿酒酵母转化酶的基因获得。Romanos等人(1992，见上文)描述了其他有用的信号肽编码序列。
该控制序列还可以是编码位于变体的N-末端处的前肽的前肽编码序列。生成的多肽被称为前体酶(proenzyme)或多肽原(或在一些情况下被称为酶原(zymogen))。多肽原通常是无活性的并且可以通过催化切割或自身催化切割来自多肽原的前肽而转化为活性多肽。可以从枯草芽孢杆菌碱性蛋白酶(aprE)、枯草芽孢杆菌中性蛋白酶(nprT)、嗜热毁丝霉漆酶(WO95/33836)、米黑根毛霉天冬氨酸蛋白酶和酿酒酵母α-因子的基因获得前肽编码序列。
在信号肽序列和前肽序列二者都存在的情况下，该前肽序列定位成紧邻该变体的N-末端并且该信号肽序列定位成紧邻该前肽序列的N-末端。
还令人希望的可以是添加相对于宿主细胞的生长来调节该变体的表达的调节序列。调节系统的实例是响应于化学或物理刺激而引起基因的表达开启或关闭的那些，包括调控化合物的存在。原核系统中的调节系统包括lac、tac和trp操纵子系统。在酵母中，可以使用ADH2系统或GAL1系统。在丝状真菌中，可以使用黑曲霉葡糖淀粉酶启动子、米曲霉TAKAα-淀粉酶启动子、以及米曲霉葡糖淀粉酶启动子。调控序列的其他实例是允许基因扩增的那些。在真核系统中，这些调控序列包括在甲氨蝶呤存在下被扩增的二氢叶酸还原酶基因以及用重金属扩增的金属硫蛋白基因。在这些情况下，编码该变体的多核苷酸将与该调节序列可操作地连接。
表达载体
本发明还涉及包含编码本发明的变体多肽的多核苷酸、启动子以及转录和翻译终止信号的重组表达载体。因此，本发明涉及包含多核苷酸、启动子、以及转录和翻译终止信号的重组表达载体，该多核苷酸编码具有α-淀粉酶活性并与SEQ ID NO:1的多肽相比展现增强的洗涤性能的变体多肽。具体而言，本发明涉及包含多核苷酸、启动子、以及转录和翻译终止密码子的重组表达载体，该多核苷酸编码在对应于以下位置的一个或多个位置处包含突变的变体多肽：10、25、30、37、40、48、51、54、64、81、86、93、98、105、108、109、113、116、118、121、130、135、138、142、167、174、175、178、182、186、187、189、195、198、202、203、206、208、210、214、218、235、238、242、243、246、247、250、255、257、259、260、261、265、267、269、270、274、275、276、281、295、298、299、311、319、320、334、339、360、365、366、383、384、385、394、398、402、404、416、434、460、469、474、和482，其中编号是根据列于SEQ ID NO:2中的氨基酸序列。
各种核苷酸和控制序列可以连接在一起以产生重组表达载体，该重组表达载体可以包括一个或多个合宜的限制位点以允许在这样的位点处插入或取代编码变体的多核苷酸。可替代地，可以通过将多核苷酸或包含该多核苷酸的核酸构建体插入用于表达的适当载体中来表达该多核苷酸。在产生表达载体时，编码序列位于载体中，这样使得编码序列与用于表达的适当控制序列可操作地连接。
重组表达载体可以是可方便地经受重组DNA程序并且可引起多核苷酸表达的任何载体(例如，质粒或病毒)。载体的选择将典型地取决于载体与待引入载体的宿主细胞的相容性。载体可以是线状或闭合的环状质粒。
载体可以是自主复制载体，即作为染色体外实体存在的载体，其复制独立于染色体复制，例如质粒、染色体外元件、微染色体或人工染色体。载体可以包含用于确保自我复制的任何装置。可替代地，载体可以是这样的载体，当它引入宿主细胞中时整合入基因组中并与其中已整合了它的染色体一起复制。此外，可使用单一载体或质粒或两个或更多个载体或质粒(这些载体或质粒一起包含待引入到宿主细胞的基因组中的总DNA)或转座子。
载体优选包含允许方便地选择转化细胞、转染细胞、转导细胞等细胞的一个或多个选择性标记。选择性标记是一种基因，其产物提供了杀生物剂抗性或病毒抗性、对重金属抗性、对营养缺陷型的原养性等。
细菌选择性标记的实例是地衣芽孢杆菌或枯草芽孢杆菌dal基因，或赋予抗生素抗性(如氨苄青霉素、氯霉素、卡那霉素、新霉素、大观霉素或四环素抗性)的标记。用于酵母宿主细胞的适合的标记包括但不限于ADE2、HIS3、LEU2、LYS2、MET3、TRP1和URA3。用于在丝状真菌宿主细胞中使用的选择性标记包括但不限于amdS(乙酰胺酶)、argB(鸟氨酸氨甲酰基转移酶)、bar(草胺膦乙酰转移酶)、hph(潮霉素磷酸转移酶)、niaD(硝酸还原酶)、pyrG(乳清苷-5’磷酸脱羧酶)、sC(硫酸腺苷基转移酶)、以及trpC(邻氨基苯甲酸合酶)，连同其等效物。优选在曲霉属细胞中使用的是构巢曲霉或米曲霉amdS和pyrG基因以及吸水链霉菌bar基因。
载体优选包含允许载体整合到宿主细胞的基因组中或载体在细胞中独立于基因组自主复制的一个或多个元件。
对于整合到该宿主细胞基因组中，该载体可以依靠编码该变体的多核苷酸序列或用于通过同源或非同源重组整合到该基因组中的该载体的任何其他元件。可替代地，该载体可以包含用于指导通过同源重组而整合到宿主细胞基因组中的染色体中的精确位置的另外的多核苷酸。为了增加在精确位置整合的可能性，这些整合的元件应包含足够数量的核酸，如100至10,000个碱基对、400至10,000个碱基对、以及800至10,000个碱基对，这些碱基对与相应的靶序列具有高度的序列一致性以提高同源重组的可能性。整合元件可以是与宿主细胞基因组内的靶序列同源的任何序列。此外，整合元件可以是非编码多核苷酸或编码多核苷酸。另一方面，载体可以通过非同源重组整合入宿主细胞的基因组中。
对于自主复制，载体可以进一步包含使载体能够在所讨论的宿主细胞中自主地进行复制的复制起点。复制起点可为在细胞中有功能的介导自主复制的任何质粒复制子。术语“复制起点(origin of replication)”或“质粒复制子(plasmid replicator)”意指使得质粒或载体能够在体内复制的多核苷酸。
细菌复制起点的实例是允许在大肠杆菌中复制的质粒pBR322、pUC19、pACYC177、以及pACYC184的复制起点，以及允许在芽孢杆菌属中复制的质粒pUB110、pE194、pTA1060、以及pAMβ1的复制起点。
用于酵母宿主细胞中的复制起点的实例是2微米复制起点、ARS1、ARS4、ARS1与CEN3的组合、及ARS4与CEN6的组合。
用于丝状真菌细胞中的复制起点的实例是AMA1和ANS1(Gems等人，1991，Gene[基因]98:61-67；Cullen等人，1987，Nucleic Acids Res.[核酸研究]15:9163-9175；WO 00/24883)。可根据WO 00/24883中公开的方法完成AMA1基因的分离和包含该基因的质粒或载体的构建。
可以将多于一个拷贝的本发明的多核苷酸插入宿主细胞中以增加变体的产生。可以通过将序列的至少一个另外的拷贝整合入宿主细胞基因组中或通过包括与该多核苷酸一起的可扩增的选择性标记基因来获得多核苷酸的增加的拷贝数目，其中通过在适当的选择性试剂的存在下培养细胞可以选择包含选择性标记基因的经扩增的拷贝的细胞、以及由此该多核苷酸的另外的拷贝。
用于连接以上所述的元件以构建本发明的重组表达载体的程序是本领域的普通技术人员熟知的(参见例如，Sambrook等人，1989，同上)。
宿主细胞
本发明还涉及重组宿主细胞，这些重组宿主细胞包含编码本发明的变体多肽的、可操作地连接至一个或多个控制序列的多核苷酸，该一个或多个控制序列指导本发明的变体多肽的产生。因此，本发明涉及包含多核苷酸的重组宿主细胞，该多核苷酸编码具有α-淀粉酶活性并与SEQ ID NO:1的多肽相比展现增强的洗涤性能的变体多肽，该多核苷酸可操作地连接至指导变体多肽的产生的一个或多个控制序列上。具体而言，本发明涉及包含多核苷酸的重组宿主细胞，该多核苷酸编码在对应于以下位置的一个或多个位置处包含突变的变体多肽：10、25、30、37、40、48、51、54、64、81、86、93、98、105、108、109、113、116、118、121、130、135、138、142、167、174、175、178、182、186、187、189、195、198、202、203、206、208、210、214、218、235、238、242、243、246、247、250、255、257、259、260、261、265、267、269、270、274、275、276、281、295、298、299、311、319、320、334、339、360、365、366、383、384、385、394、398、402、404、416、434、460、469、474、和482，其中编号是根据列于SEQ ID NO:2中的氨基酸序列，该多核苷酸可操作地连接至指导变体多肽的产生的一个或多个控制序列上。
将包含多核苷酸的构建体或载体引入宿主细胞中，这样使得该构建体或载体作为染色体整合体或作为自主复制的染色体外载体维持，如较早前所述。术语“宿主细胞”涵盖由于复制过程中发生的突变而与亲本细胞不同的亲本细胞的任何后代。宿主细胞的选择在很大程度上将取决于编码变体的基因及其来源。
宿主细胞可以是在变体的重组产生中有用的任何细胞，例如原核细胞或真核细胞。
原核宿主细胞可以是任何革兰氏阳性或革兰氏阴性细菌。革兰氏阳性细菌包括但不限于芽孢杆菌属、梭菌属、肠球菌属、土芽孢杆菌属、乳杆菌属、乳球菌属、海洋芽孢杆菌属、葡萄球菌属、链球菌属和链霉菌属。革兰氏阴性细菌包括但不限于：弯曲杆菌属、大肠杆菌、黄杆菌属、梭杆菌属、螺杆菌属、泥杆菌属、奈瑟氏菌属、假单胞菌属、沙门氏菌属、以及脲原体属。
细菌宿主细胞可以是任何芽孢杆菌属细胞，包括但不限于嗜碱芽孢杆菌、解淀粉芽孢杆菌、短芽孢杆菌、环状芽孢杆菌、克劳氏芽孢杆菌、凝结芽孢杆菌、坚硬芽孢杆菌、灿烂芽孢杆菌、迟缓芽孢杆菌、地衣芽孢杆菌、巨大芽孢杆菌、短小芽孢杆菌、嗜热脂肪芽孢杆菌、枯草芽孢杆菌以及苏云金芽孢杆菌细胞。
细菌宿主细胞还可为任何链球菌属细胞，包括但不限于：似马链球菌、酿脓链球菌、乳房链球菌和马链球菌兽瘟亚种细胞。
细菌宿主细胞还可以是任何链霉菌属细胞，包括但不限于：不产色链霉菌、除虫链霉菌、天蓝色链霉菌、灰色链霉菌、以及变铅青链霉菌细胞。
将DNA引入芽孢杆菌属细胞中可以通过以下来实现：原生质体转化(参见例如，Chang和Cohen,1979,Mol.Gen.Genet.[分子遗传学与基因组学]168:111-115)、感受态细胞转化(参见例如，Young和Spizizen,1961,J.Bacteriol.[细菌学杂志]81:823-829，或Dubnau和Davidoff-Abelson,1971,J.Mol.Biol.[分子生物学杂志]56:209-221)、电穿孔(参见例如，Shigekawa和Dower,1988,Biotechniques[生物技术]6:742-751)或接合(参见例如，Koehler和Thorne,1987,J.Bacteriol.[细菌学杂志]169:5271-5278)。将DNA引入大肠杆菌细胞中可以通过以下来实现：原生质体转化(参见例如，Hanahan,1983,J.Mol.Biol.[分子生物学杂志]166:557-580)或电穿孔(参见例如，Dower等人,1988,Nucleic AcidsRes.[核酸研究]16:6127-6145)。将DNA引入链霉菌属细胞中可以通过以下来实现：原生质体转化、电穿孔(参见例如，Gong等人，2004,Folia Microbiol.(Praha)[叶线形微生物学(布拉格)]49:399-405)、接合(参见例如，Mazodier等人，1989，J.Bacteriol.[细菌学杂志]171:3583-3585)或转导(参见例如，Burke等人，2001，Proc.Natl.Acad.Sci.USA[美国国家科学院院刊]98:6289-6294)。将DNA引入假单孢菌属细胞中可以通过以下来实现：电穿孔(参见例如，Choi等人，2006,J.Microbiol.Methods[微生物学方法杂志]64:391-397)或接合(参见例如，Pinedo和Smets,2005,Appl.Environ.Microbiol.[应用与环境微生物学]71:51-57)。将DNA引入链球菌属细胞中可以通过以下来实现：天然感受态(参见例如，Perry和Kuramitsu,1981,Infect.Immun.[感染与免疫]32:1295-1297)、原生质体转化(参见例如，Catt和Jollick,1991,Microbios[微生物学]68:189-207)、电穿孔(参见例如，Buckley等人,1999,Appl.Environ.Microbiol.[应用与环境微生物学]65:3800-3804)或接合(参见例如，Clewell,1981,Microbiol.Rev.[微生物学评论]45:409-436)。然而，可以使用本领域已知的将DNA引入宿主细胞中的任何方法。
宿主细胞还可以是真核生物，如植物、或真菌细胞。
宿主细胞可为真菌细胞。如在此使用的“真菌”包括子囊菌门(Ascomycota)、担子菌门(Basidiomycota)、壶菌门(Chytridiomycota)和接合菌门(Zygomycota)以及卵菌门(Oomycota)和所有有丝分裂孢子真菌(如由Hawksworth等人所定义的，在：Ainsworth andBisby’s Dictionary of The Fungi[Ainsworth和Bisby的真菌大词典]，第8版，1995，国际CAB，大学出版社，剑桥，英国)。
真菌宿主细胞可为酵母细胞。如在此所使用的“酵母”包括产子囊酵母(酵母目)、产担子酵母及属于不完全真菌的酵母(芽生菌目)。由于酵母的分类可能在将来变化，出于本发明的目的，酵母应当如酵母的生物学与活性(Skinner、Passmore和Davenport编辑，Soc.App.Bacteriol.Symposium Series No.9[应用细菌学学会专题论文集系列9]，1980)所描述那样定义。
酵母宿主细胞可以是假丝酵母属细胞、汉逊酵母属细胞、克鲁维酵母属细胞、毕赤酵母属细胞、酵母菌属细胞、裂殖酵母或耶罗维亚酵母属细胞、如乳酸克鲁维酵母细胞、卡氏酵母细胞、酿酒酵母细胞、糖化酵母细胞、道格拉斯酵母(Saccharomyces douglasii)细胞、克鲁弗酵母细胞、诺地酵母细胞、卵形酵母细胞或解脂耶罗维亚酵母细胞。
真菌宿主细胞可为丝状真菌细胞。“丝状真菌”包括真菌门(Eumycota)和卵菌门(Oomycota)的亚门的所有丝状形式(如由Hawksworth等人所定义的，1995，见上文)。丝状真菌通常的特征在于由几丁质、纤维素、葡聚糖、壳多糖、甘露聚糖、以及其他复杂多糖构成的菌丝体壁。营养生长是通过菌丝延长，而碳分解代谢是专性需氧的。相反，酵母(如酿酒酵母)的营养生长是通过单细胞菌体的出芽(budding)，而碳分解代谢可以是发酵性的。
丝状真菌宿主细胞可以是枝顶孢属、曲霉属、短梗霉属、烟管霉属(Bjerkandera)、拟腊菌属、金孢子菌属、鬼伞属、革盖菌属(Coriolus)、隐球菌属、线黑粉菌科(Filibasidium)、镰孢属、腐质霉属、梨孢菌属、毛霉属、毁丝霉属、新美鞭菌属、链孢菌属、拟青霉属、青霉属、平革菌属、射脉菌属(Phlebia)、瘤胃壶菌属、侧耳属(Pleurotus)、裂褶菌属、篮状菌属、嗜热子囊菌属、梭孢壳属、弯颈霉属、栓菌属(Trametes)或木霉属细胞。
例如，丝状真菌宿主细胞可以是泡盛曲霉、臭曲霉、烟曲霉、日本曲霉、构巢曲霉、黑曲霉、米曲霉、黑刺烟管菌(Bjerkandera adusta)、干拟蜡菌(Ceriporiopsisaneirina)、卡内基拟蜡菌(Ceriporiopsis caregiea)、浅黄拟蜡孔菌(Ceriporiopsisgilvescens)、潘诺希塔拟蜡菌(Ceriporiopsis pannocinta)、环带拟蜡菌(Ceriporiopsisrivulosa)、微红拟蜡菌(Ceriporiopsis subrufa)、虫拟蜡菌(Ceriporiopsissubvermispora)、狭边金孢子菌(Chrysosporium inops)、嗜角质金孢子菌、卢克诺文思金孢子菌(Chrysosporium lucknowense)、粪状金孢子菌(Chrysosporium merdarium)、租金孢子菌、女王杜香金孢子菌(Chrysosporium queenslandicum)、热带金孢子菌、褐薄金孢子菌(Chrysosporium zonatum)、灰盖鬼伞(Coprinus cinereus)、毛革盖菌(Coriolushirsutus)、杆孢状镰孢、谷类镰孢、库威镰孢、大刀镰孢、禾谷镰孢、禾赤镰孢、异孢镰孢、合欢木镰孢、尖镰孢、多枝镰孢、粉红镰孢、接骨木镰孢、肤色镰孢、拟分枝孢镰孢、硫色镰孢、圆镰孢、拟丝孢镰孢、镶片镰孢、特异腐质霉、柔毛腐质霉、米黑毛霉、嗜热毁丝霉、粗糙链孢菌、产紫青霉、黄孢平革菌(Phanerochaete chrysosporium)、射脉菌(Phlebia radiata)、刺芹侧耳(Pleurotus eryngii)、土生梭孢壳霉、长域毛栓菌(Trametes villosa)、变色栓菌(Trametes versicolor)、哈茨木霉、康宁木霉、长枝木霉、里氏木霉、或绿色木霉细胞。
真菌细胞可以通过下述过程转化，该过程涉及原生质体形成、原生质体的转化、以及以本身已知的方式的细胞壁的再生。用于转化曲霉属和木霉属宿主细胞的适合程序描述于以下文献中：EP 238023，Yelton等人，1984，Proc.Natl.Acad.Sci.USA[美国国家科学院院刊]81:1470-1474以及Christensen等人，1988，Bio/Technology[生物/技术]6:1419-1422。用于转化镰孢菌属物种的适合方法由Malardier等人1989，Gene[基因]78:147-156和WO 96/00787描述。可使用由如以下文献描述的方法转化酵母：Becker和Guarente，于Abelson，J.N.和Simon，M.I.编，Guide to Yeast Genetics and Molecular Biology[酵母遗传学与分子生物学指南]，Methods in Enzymology[酶学方法]，第194卷，第182-187页，学术出版社有限公司(Academic Press,Inc.)，纽约；Ito等人，1983，J.Bacteriol.[细菌学杂志]153:163；以及Hinnen等人，1978，Proc.Natl.Acad.Sci.USA[美国科学院院刊]75:1920。
生产方法
本发明还涉及产生变体α-淀粉酶的方法，这些方法包括：(a)在适合于变体多肽的表达的条件下，培养本发明的宿主细胞；和(b)回收该变体多肽。
使用本领域已知的方法在适合于产生变体的营养培养基中培养宿主细胞。例如，可以通过摇瓶培养，或者在适合的培养基中并在允许变体表达和/或分离的条件下在实验室或工业发酵罐中进行小规模或大规模发酵(包括连续发酵、分批发酵、分批给料发酵或固态发酵)来培养细胞。培养是使用本领域已知的程序，在适合营养培养基中发生，该培养基包含碳和氮来源及无机盐。适合的培养基可以从商业供应商获得或可以根据公开的组成(例如，在美国典型培养物保藏中心(American Type Culture Collection)的目录中)制备。如果变体被分泌到营养培养基中，则变体可以直接从培养基中回收。如果变体没有分泌，则它可以从细胞裂解液中回收。
变体可以使用本领域已知的方法检测。适合的检测方法包括但不限于：特异性抗体的使用、酶产物的形成或酶底物的消失。例如，可以使用酶测定来确定变体的α-淀粉酶活性(参见实例)。
变体可以使用本领域已知的方法回收。例如，可以通过多种常规程序从营养培养基中回收变体，所述常规程序包括但不限于收集、离心、过滤、提取、喷雾干燥、蒸发或沉淀。
可以通过本领域中已知的多种程序来纯化变体以获得基本上纯的变体，这些程序包括但不限于色谱法(例如，离子交换色谱、亲和色谱、疏水作用色谱、色谱聚焦、以及尺寸排阻色谱)、电泳程序(例如，制备型等电点聚焦)、差别溶解度(例如，硫酸铵沉淀)、SDS-PAGE、或萃取(参见，例如，Protein Purification[蛋白质纯化]，Janson和Ryden编辑，VCH出版社(VCH Publishers)，纽约，1989)。
在可替代的方面，没有回收变体，而是将表达变体的本发明的宿主细胞用作变体的来源。
组合物
可以将本发明的α-淀粉酶多肽添加至洗涤剂组合物中并且因此使其成为洗涤剂组合物的组分。因此，本发明涉及包含变体多肽的组合物，该变体多肽具有α-淀粉酶活性并与SEQ ID NO:1的多肽相比展现增强的洗涤性能。具体而言，本发明涉及包含变体多肽的组合物，该变体多肽在对应于以下位置的一个或多个位置处包含突变：10、25、30、37、40、48、51、54、64、81、86、93、98、105、108、109、113、116、118、121、130、135、138、142、167、174、175、178、182、186、187、189、195、198、202、203、206、208、210、214、218、235、238、242、243、246、247、250、255、257、259、260、261、265、267、269、270、274、275、276、281、295、298、299、311、319、320、334、339、360、365、366、383、384、385、394、398、402、404、416、434、460、469、474、和482，其中编号是根据列于SEQ ID NO:2中的氨基酸序列。
因此，本发明的另外的方面提供洗涤剂组合物，该洗涤剂组合物包含本发明的多肽和表面活性剂(如阴离子表面活性剂、阳离子表面活性剂、非离子表面活性剂和/或两性离子表面活性剂)。还提供了用于制备此类洗涤剂组合物的浓缩物或添加剂，该浓缩物或添加剂包含本发明的多肽以及任选地表面活性剂。
如以下详细讨论的，该洗涤剂组合物可进一步包含选自下组的一种或多种另外的组分，该组由以下组成：氧化剂、漂白活化剂、填充剂、助洗剂、缓冲剂、结构剂、螯合剂、荧光增白剂、消泡剂、酶、香料、抗再沉积剂、皮肤调理剂、柔软剂、乳化剂、和着色剂。
在一个实施例中，该组合物是液体或粉末衣物洗涤剂组合物。
在另外的实施例中，该组合物是液体或粉末自动餐具洗涤(ADW)洗涤剂组合物。
例如，可以将本发明的洗涤剂组合物配制成手洗或机洗清洁剂组合物，包括适于预处理带有污渍的织物的洗衣用添加剂组合物和漂洗中添加的织物软化剂组合物，或配制成用于在一般性的家居硬表面的清洁操作中使用的洗涤剂组合物，或配制成在手或机洗碗操作中使用的洗涤剂组合物。
在具体的方面，本发明提供包含本发明的α-淀粉酶多肽的洗涤剂浓缩物/添加剂。该洗涤剂浓缩物/添加剂、连同洗涤剂组合物可以包含一种或多种其他酶，如蛋白酶、脂肪酶、过氧化物酶、另一种淀粉分解酶，例如另一种α-淀粉酶、葡糖淀粉酶、麦芽糖淀粉酶、CGT酶和/或纤维素酶、甘露聚糖酶(如MANNAWAYTM，来自诺维信公司(Novozymes)，丹麦)、果胶酶、果胶裂合酶、角质酶和/或漆酶。
一般而言，选择的一种或多种酶的特性应与所选的洗涤剂兼容(即，最适pH、与其他酶和非酶成分的兼容性等)，并且该一种或多种酶应以有效量存在。
蛋白酶：适合的蛋白酶包括动物、植物或微生物来源的那些。优选的是微生物来源。包括化学修饰的突变体或蛋白质工程化的突变体。该蛋白酶可以是丝氨酸蛋白酶或金属蛋白酶，优选碱性微生物蛋白酶或胰蛋白酶样蛋白酶。碱性蛋白酶的实例为枯草杆菌蛋白酶，特别是源自芽孢杆菌属的那些，例如枯草杆菌蛋白酶Novo、枯草杆菌蛋白酶Carlsberg、枯草杆菌蛋白酶309、枯草杆菌蛋白酶147以及枯草杆菌蛋白酶168(在WO 89/06279中描述)。胰蛋白酶样蛋白酶的实例是胰蛋白酶(例如，猪或牛来源的)以及在WO 89/06270和WO 94/25583中描述的镰孢属蛋白酶。
有用的蛋白酶的实例是如WO 92/19729、WO 98/20115、WO 98/20116和WO 98/34946所描述的变体，特别是在下述位置中的一个或多个处发生取代的变体：27、36、57、76、87、97、101、104、120、123、167、170、194、206、218、222、224、235、以及274。优选的可商购的蛋白酶包括
(SEQ ID NO:3)、
和
(来自(诺维信公司(Novozymes A/S))、
MAXACAL、
(杰能科国际公司(Genencor International Inc.))。
脂肪酶：适合的脂肪酶包括细菌或真菌来源的那些脂肪酶。包括化学修饰的突变体或蛋白质工程化的突变体。有用脂肪酶的实例包括来自腐质霉属(Humicola)(与嗜热丝孢菌属(Thermomyces)同义)，例如来自如EP 258 068和EP 305 216描述的疏棉状腐质霉(H.lanuginosa)(细毛嗜热霉(T.lanuginosus))或来自如WO 96/13580中描述的特异腐质霉(H.insolens)的脂肪酶；假单胞菌属(Pseudomonas)脂肪酶，例如来自产碱假单胞菌(P.alcaligenes)或类产碱假单胞菌(P.pseudoalcaligenes)(EP 218 272)、洋葱假单胞菌(P.cepacia)(EP 331 376)、施氏假单胞菌(P.stutzeri)(GB 1,372,034)、萤光假单胞菌(P.fluorescens)、假单胞菌属物种株系SD 705(Pseudomonas sp.strain SD 705)(WO 95/06720和WO 96/27002)、威斯康星假单胞菌(P.wisconsinensis)(WO 96/12012)；芽孢杆菌属(Bacillus)脂肪酶，例如来自枯草芽孢杆菌(B.subtilis)(达图瓦(Dartois)等人，1993，生物化学与生物物理学报(Biochemica et Biophysica Acta)，1131:253-360)，嗜热脂肪芽抱杆菌(B.stearothermophilus)(JP 64/744992)或短小芽孢杆菌(B.pumilus)(WO 91/16422)。脂肪酶变体的其他实例如在WO 92/05249、WO 94/01541、EP 407 225、EP 260 105、WO 95/35381、WO 96/00292、WO 95/30744、WO 94/25578、WO 95/14783、WO 95/22615、WO97/04079以及WO 97/07202中描述的那些。
优选的可商购的脂肪酶包括LIPOLASE<TM>和LIPOLASE ULTRA<TM>(诺维信公司(Novozymes A/S)，本文的SEQ ID NO:4)。
淀粉酶：适合的淀粉酶(α-和/或β-淀粉酶)包含来源于细菌或真菌的淀粉酶。包括化学修饰的突变体或蛋白质工程化的突变体。淀粉酶包括例如从芽孢杆菌属，例如地衣芽孢杆菌的特定菌株(更详细地描述于GB 1,296,839中)获得的α-淀粉酶。有用的α-淀粉酶的实例是在WO 94/02597、WO 94/18314、WO 96/23873、以及WO 97/43424中描述的变体，尤其是在一个或多个以下位置上具有取代的变体：15、23、105、106、124、128、133、154、156、181、188、190、197、202、208、209、243、264、304、305、391、408、和444。可商购的α-淀粉酶是DURAMYL<TM>、LIQUEZYMETM、TERMAMYL<TM>、NATALASE<TM>、FUNGAMYL<TM>and BAN<TM>(诺维信公司(Novozymes A/S))、Preferenz S100、Preferenz S110、Preferenz S1000、ExcellenzS110、Excellenz S1000、Excellenz S2000、RAPIDASE<TM>和PURASTAR<TM>(来自杰能科国际公司(Genencor International Inc.))。因此，适合的淀粉酶可以是本文列为SEQ ID NO:5、6、7、8、9、10、和11的那些中的任一种，及其变体。
纤维素酶：适合的纤维素酶包括细菌或真菌来源的那些。包括化学修饰的突变体或蛋白质工程化的突变体。适合的纤维素酶包括来自芽孢杆菌属、假单胞菌属、腐质霉属、镰孢属、梭孢壳属、枝顶孢霉属的纤维素酶，例如，从在US 4,435,307、US 5,648,263、US 5,691,178、US 5,776,757以及WO 89/09259中披露的特异腐质霉、嗜热毁丝霉和尖镰孢产生的真菌纤维素酶。特别适合的纤维素酶是具有颜色护理益的碱性或中性纤维素酶。此类纤维素酶的实例是在EP 0 495 257、EP 0 531 372、WO 96/11262、WO 96/29397、WO 98/08940中描述的纤维素酶。其他实例为纤维素酶变体，例如在WO 94/07998、EP 0 531 315、US 5,457,046、US 5,686,593、US 5,763,254、WO 95/24471、WO 98/12307以及PCT/DK 98/00299中描述的那些。
可商购的纤维素酶包括
和
(诺维信公司(Novozymes A/S))、
和PURADAX
(杰能科国际公司(GenencorInternational Inc.))和
(花王株式会社(Kao Corporation))。
过氧化物酵/氧化酶：适合的过氧化物酶/氧化酶包括植物、细菌或真菌来源的那些。包括化学修饰的突变体或蛋白质工程化的突变体。有用的过氧化物酶的实例包括来自鬼伞属(例如来自灰盖鬼伞)的过氧化物酶、及其变体，如在WO 93/24618、WO 95/10602、以及WO 98/15257中描述的那些。可商购的过氧化物酶包括
(诺维信公司(Novozymes A/S))。
Lechinase：适合的Lechinase包括细菌来源或真菌来源的那些。它们可以被化学修饰或蛋白质工程化。有用的lechinase的实例包括SEQ ID NO:3、4、和5中(诺维信公司(Novozymes A/S))以及WO 99/06516(德国汉高公司(Henkel KGAA))提出的那些。可以被化学修饰或蛋白质工程改造的其他适合的lichinase的实例是如本文SEQ ID NO:12、13、14、和15中所示的那些。
可以通过添加包含一种或多种酶的单独添加剂、或通过添加包含所有这些酶的组合添加剂而将洗涤剂酶包括在洗涤剂组合物中。本发明的洗涤剂添加剂(即单独添加剂或组合添加剂)可配制为例如颗粒、液体、浆液等。优选的洗涤剂添加剂配制品是颗粒，尤其是非尘颗粒；液体，尤其是稳定的液体；或浆液。
非尘化的颗粒可以例如如在US 4,106,991和4,661,452中所披露而产生，并且可以任选地通过本领域已知的方法进行包衣。蜡状包衣材料的实例是具有平均分子量为1000至20000的聚(环氧乙烷)产品(聚乙二醇，PEG)；具有从16个到50个环氧乙烷单位的乙氧基化壬基酚；具有从12个至20个碳原子并且存在15个至80个环氧乙烷单位的乙氧基化脂肪族醇；脂肪醇；脂肪酸；以及脂肪酸的甘油单酯、甘油二酯、和甘油三酯。适用于通过流化床技术应用的成膜包衣材料的实例在GB 1483591中给出。液体酶制剂可以例如通过根据已确立的方法添加多元醇(例如丙二醇)、糖或糖醇、乳酸或硼酸而稳定化。受保护的酶可以根据EP238 216中披露的方法制备。
本发明的洗涤剂组合物可以呈任何便利的形式，如棒状、片剂、粉、颗粒、糊状或液体。液体洗涤剂可以是水性的，典型地包含至多70％的水和0-30％的有机溶剂，或可以是非水性的。
所述洗涤剂组合物包括一种或多种表面活性剂，表面活性剂可以是非离子型(包括半极性)和/或阴离子型和/或阳离子型和/或两性离子型。表面活性剂典型地以按重量计0.1％至60％的水平存在。
当包含在其中时，洗涤剂通常将包含约1％至约40％的阴离子表面活性剂，例如线性烷基苯磺酸盐、a-烯烃磺酸盐、烷基硫酸盐(脂肪醇硫酸盐)、醇乙氧基硫酸盐、仲烷基磺酸盐、α-磺基脂肪酸甲酯、烷基或烯基琥珀酸或肥皂。
当包含在所述洗涤剂中时，洗涤剂通常包含从约0.2％到约40％的非离子表面活性剂，例如醇乙氧基化物、壬基酚乙氧基化物、烷基多苷、烷基二甲基胺氧化物、乙氧基化脂肪酸单乙醇酰胺、脂肪酸单乙醇酰胺、多羟基烷基脂肪酰胺、或葡糖胺的N-酰基N-烷基衍生物(“葡糖酰胺”)。
该洗涤剂可以包含0-65％的洗涤剂助洗剂或络合剂，如沸石、二磷酸盐、三磷酸盐、膦酸盐、碳酸盐、柠檬酸盐、次氮基三乙酸、乙二胺四乙酸、二乙二胺三氨基五乙酸、烷基或烯基琥珀酸、可溶性硅酸盐、或层状硅酸盐(例如，来自赫斯特(Hoechst)的SKS-6)。其他络合剂可以是甲基甘氨酸二乙酸(MGDA)和谷氨酸二乙酸(GLDA)，其可特别用于不含磷酸盐的自动餐具洗涤剂中。
该洗涤剂可以包含一种或多种聚合物。实例为磺化的聚合物、羧甲基纤维素、聚(乙烯基-吡咯烷酮)、聚(乙二醇)、聚(乙烯醇)、聚(乙烯基吡啶-N-氧化物)、聚(乙烯基咪唑)、聚羧酸酯(如聚丙烯酸酯)、马来酸/丙烯酸共聚物、以及甲基丙烯酸月桂酯/丙烯酸共聚物。
洗涤剂可以包含漂白系统，其可以包含H2O2源，如过硼酸或过碳酸，其可以与形成过酸的漂白活化剂(如四乙酰基乙二胺或壬酰氧基苯磺酸盐)组合。此外，漂白催化剂可以是基于Mn和/或Co的组分。可替代地，漂白系统可以包含过酸，例如酰胺、亚胺或砜类型的过酸。
可以使用常规稳定剂稳定本发明的洗涤剂组合物的一种或多种酶，这些常规稳定剂例如是多元醇，例如丙二醇或甘油、糖或糖醇、乳酸、硼酸或硼酸衍生物，例如芳香族硼酸酯，或苯基硼酸衍生物，例如4-甲酰苯基硼酸，并且可以如在例如WO 92/19709和WO 92/19708中所描述配制该组合物。
该洗涤剂还可以包含其他的常规洗涤剂成分，像例如织物调理剂，这些织物调理剂包括粘土、泡沫促进剂、泡沫抑制剂、防腐蚀剂、污垢悬浮剂、抗污物再沉淀剂、染料、杀菌剂、光学增亮剂、水溶助长剂、晦暗抑制剂、或香料。
目前期望在洗涤剂组合物中加入任何酶，特别是本发明的α淀粉酶多肽，添加量相当于每升洗涤液添加0.01mg-100mg酶蛋白，优选每升洗涤液加0.05mg-5mg酶蛋白，特别优选每升洗涤液加0.1mg-1mg酶蛋白。
另外，本发明的α淀粉酶多肽可以掺入WO 2006/002643(将其通过引用结合在此)中所披露的洗涤剂配制品中。
本发明的餐具洗涤剂组合物的实例
可以将本发明的α-淀粉酶多肽用于包括以下的餐具洗涤剂组合物中：
(a)粉末自动餐具洗涤组合物
(b)粉末自动餐具洗涤组合物
(c)粉末自动餐具洗涤组合物
(d)粉末自动餐具洗涤组合物
(e)粉末自动餐具洗涤组合物
(f)具有清洗表面活性剂系统的粉末和液体餐具洗涤组合物
(p)非水性液体自动餐具洗涤组合物
(q)非水性液体餐具洗涤组合物
(r)触变的液体自动餐具洗涤组合物
(s)液体自动餐具洗涤组合物
(t)包含保护的漂白剂颗粒的液体自动餐具洗涤剂组合物
(u)如在(a)、(b)、(c)、(d)、(f)和(j)中描述的自动餐具洗涤组合物，其中用过碳酸盐替换过硼酸盐。
(v)如在(a)至(f)中描述的自动餐具洗涤组合物，其另外地包含锰催化剂。锰催化剂可以例如是以下中描述的化合物之一：“Efficient manganese catalysts for low-temperature bleaching[用于低温漂白的高效锰催化剂]”，Nature[自然]369，1994，第637-639页。
用途
本发明还针对将本发明的α-淀粉酶多肽用于洗涤剂(特别是衣物洗涤剂组合物和餐具洗涤剂组合物)中的方法。
因此，本发明提供本发明的α-淀粉酶多肽或组合物在家庭或工业清洗过程中的用途。
在一个实施例中，该用途是织物的清洗，例如衣物洗涤。
在另一个实施例中，该用途是陶瓷、塑料或玻璃材料的清洗，例如餐具洗涤。
因此，本发明的α-淀粉酶多肽可用作洗涤、餐具洗涤和硬表面清洁洗涤剂组合物(在家庭或工业环境中)的组分。
本发明的α-淀粉酶变体具有允许各种其他工业应用的宝贵特性。例如，本发明的α-淀粉酶多肽可以用于淀粉过程，特别是淀粉转化，尤其是淀粉的液化(参见，例如US 3,912,590、欧洲专利申请号252 730和63 909、WO 99/19467、和WO 96/28567，所有参考文献通过引用结合在此)。还涵盖用于淀粉转化目的组合物，除了本发明的变体以外，这些组合物还可包括葡糖淀粉酶、支链淀粉酶以及其他α-淀粉酶。
此外，本发明α-淀粉酶变体也特别适用于从淀粉或全谷粒中生产甜味剂以及乙醇(参见，例如，美国专利号5,231,017，通过引用结合在此)，如燃料乙醇、饮用乙醇以及工业乙醇。
本发明的α-淀粉酶变体还用于纺织品、织物和服装的退浆(参见，例如WO 95/21247、美国专利4,643,736、EP 119,920，通过引用结合在此)、啤酒制造或酿造、纸浆和纸张生产。
淀粉转化
常规的淀粉转化过程(如液化和糖化过程)例如在美国专利3,912,590和欧洲专利公开号252,730和63,909中进行了描述，通过引用结合在此。
在一个实施例中，淀粉转化方法将淀粉降解为较低分子量的碳水化合物成分，如糖或脂肪替代物，该方法包括一个脱支步骤。
当将淀粉转化为糖时，淀粉被解聚。这类解聚过程可以由例如预处理步骤以及两个或三个连续过程步骤组成，即，液化过程、糖化过程并且取决于所需最终产物，任选地异构化过程。
(i)天然淀粉的预处理
天然淀粉由室温下不溶于水的微观颗粒组成。加热水性淀粉浆料时，颗粒膨胀并且最后破裂，将淀粉分子分散至溶液中。在此“糊化(gelatinization)”过程中，粘度有显著地增加。由于典型工业方法中的固体水平为30％-40％，因此不得不稀释或“液化”淀粉以使其能够被操作。如今主要是通过酶降解而获得粘度的降低。
(ii)液化
在液化步骤中，α-淀粉酶将长链淀粉降解为支链以及直链的较短单元(麦芽糊精)。液化过程在105℃-110℃下进行5至10分钟，随后在95℃下进行1-2小时。pH值在5.5和6.2之间。为了确保在这些条件下最佳的酶稳定性，添加1mM钙(40ppm游离的钙离子)。在这个处理之后，液化的淀粉将具有10-15的“右旋糖当量”(DE)。
(iii)糖化
在液化过程之后，通过添加葡糖淀粉酶(例如AMG)和脱支酶(如异淀粉酶(美国专利号4,335,208)或支链淀粉酶(例如PromozymeTM)美国专利号4,560,651)将麦芽糖糊精转化为右旋糖。在该步骤之前，将pH降低至低于4.5的值，维持高温(高于95℃)以使液化α-淀粉酶失活以减少称为“潘糖前体”的短寡糖的形成，所述短寡糖不能被脱支酶适当地水解酶。
将温度降至60℃，并添加葡糖淀粉酶和脱支酶。糖化过程进行24-72小时。
通常，在液化步骤后使α-淀粉酶变性时，约0.2％-0.5％的糖化产物是不能被支链淀粉酶降解的支化三糖6<2>-α-葡糖基麦芽糖(潘糖)。如果在糖化过程中存在来自液化步骤的活性淀粉酶(即未变性)，则该水平可以高达1％-2％，这是高度不希望的，因为它显著降低了糖化产率。
(iv)异构化
当所需的最终糖产物是例如高果糖糖浆时，右旋糖糖浆可被转化为果糖。糖化过程之后，将pH值增加至6-8范围内的值，优选地pH 7.5，并且通过离子交换去除钙。然后，使用例如固定化葡糖异构酶(如Sweetzyme<TM>IT)将右旋糖糖浆转化成高果糖糖浆。
乙醇生产
总体上，从全谷粒来生产醇(乙醇)可分成4个主要步骤
-研磨
-液化
-糖化
-发酵
(i)研磨
谷粒经过研磨以便打开结构并且允许进一步处理。所使用的两个过程是湿式或干式研磨。在干式研磨中，将完整谷粒研磨并且用于该过程的其余部分中。湿式研磨可很好地分离胚芽(germ)和粗粉(淀粉颗粒和蛋白质)，除少数情况外湿式研磨在平行生产糖浆时的多个位置使用。
(ii)液化
在液化过程中，淀粉颗粒通过水解来溶解成DP大部分高于4的麦芽糊精。水解可通过酸处理来执行或由α-淀粉酶来酶法执行。酸水解有限地使用。原材料可以是研磨的全谷粒或来自淀粉处理的侧流。
酶法液化典型地以三步热浆液方法进行。浆液加热至60℃-95℃(优选地，80℃-85℃)之间，并且添加一种或多种酶。然后将浆液在95℃-140℃(优选地，105℃-125℃)之间喷射蒸煮、冷却至60℃-95℃并且添加更多酶以获得最终水解。液化方法在pH 4.5-6.5、典型地在5与6之间的pH进行。研磨并且液化的谷粒又称为醪液(mash)。
(iii)糖化
为了生产可被酵母代谢的低分子糖DP1-3，液化过程中的麦芽糖糊精必须进一步水解。典型地通过葡糖淀粉酶进行酶水解，可替代地，可以使用α-葡糖苷酶或酸性α-淀粉酶。全糖化步骤可以持续72小时，然而，通常只进行典型的40-90分钟的预糖化，并且然后在发酵期间完成糖化(SSF)。糖化典型地在从30℃-65℃、典型地约60℃的温度下并在pH 4.5下进行。
(iv)发酵
将典型地来自酵母属的酵母添加至醪液中并且发酵持续24-96小时，如典型地35-60小时。温度在26℃-34℃之间，典型地在约32℃，并且pH是从pH 3-6，优选地，约pH 4-5。
请注意，最广泛使用的过程是同步糖化和发酵(SSF)过程，其中没有糖化的持续阶段，这意味着酵母和酶添加在一起。在进行SSF时，通常在发酵之前在高于50℃的温度下引入预糖化步骤。
(v)蒸馏
发酵后，将醪液蒸馏以提取乙醇。
根据本发明的方法获得的乙醇可用作例如燃料乙醇、饮用乙醇，即可饮用的中性酒精饮料，或工业乙醇。
(vi)副产品
来自发酵的剩余物是酒糟，它典型地用于液体或干燥形式的动物饲料。
关于如何完成液化、糖化、发酵、蒸馏以及回收乙醇的进一步细节是本领域技术人员熟知的。
根据本发明的方法，糖化以及发酵可同时或单独地执行。
纸浆以及纸张生产
本发明的碱性α-淀粉酶多肽还可用于从淀粉增强废纸以及纸板来生产木质纤维素材料如纸浆、纸张以及纸板，尤其当再浆化在高于7的pH下发生以及当淀粉酶经由增强淀粉的降解来促进废弃材料的分解时。本发明的α-淀粉酶尤其适用于从淀粉涂布的印刷纸来生产造纸纸浆的过程。该工艺可如WO 95/14807描述来执行，包括以下步骤：
a)使纸张分解以产生纸浆，
b)在步骤a)之前、期间或之后用淀粉降解酶进行处理，并且
c)在步骤a)和b)之后，从纸浆中分离油墨颗粒。
本发明的α-淀粉酶还可非常适用于对淀粉进行改性，其中酶改性的淀粉与碱性填充剂如碳酸钙、高岭土以及粘土一起用于造纸。用本发明的碱性α-淀粉酶有可能在填充剂存在下将淀粉改性，从而允许一种更简单的整合过程。
纺织品、织物以及服饰的退浆
本发明的α-淀粉酶在纺织品，织物或衣服脱浆中也非常有用。在纺织加工工业中，传统上使用α-淀粉酶作为脱浆过程中的助剂，以促进在织造过程中作为纬纱上的保护涂层的含淀粉胶料的去除。织造之后彻底去除胶料涂层对于确保后续过程(其中所述织物被擦洗、漂白和染色)中的最佳效果是至关重要的。酶法淀粉分解是优选的，因为它不对纤维材料产生任何有害的作用。为了减少加工成本并增加研磨机处理量，有时将脱浆过程与擦洗和漂白步骤结合。在这类情况下，非酶助剂如碱或氧化剂典型用于分解淀粉，因为传统α-淀粉酶并不与高pH水平以及漂白剂非常相容。由于使用具有相当腐蚀性的化学品，因此淀粉胶料的非酶分解导致一些纤维损伤。因此，希望使用本发明的α-淀粉酶，因为它们在碱性溶液中具有改进的性能。在使含纤维素的织物或纺织品脱浆时，α-淀粉酶可单独或与纤维素酶组合使用。
退浆以及漂白过程在本领域中是熟知的。例如，这类工艺描述于例如WO 95/21247、美国专利4,643,736、EP 119,920(通过引用结合在此)中。
用于退浆的可商购的产品包括
和
ULTRA(来自诺维信公司(Novozymes A/S))。
啤酒制造
本发明的α-淀粉酶在啤酒制造工艺中也可以是非常有用的；在醪液形成(mashing)工艺期间，典型地添加α-淀粉酶。
通过以下实例进一步描述本发明，所述实例不应理解为对本发明的范围进行限制。
本申请中描述并且要求保护的本发明不限于在此披露的特定方面的范围，因为这些方面旨在说明本发明的若干方面。任何等同方面意欲在本发明的范围之内。实际上，除了本文所示和描述的那些之外，对于本领域的技术人员而言本发明的各种修改将从前述的说明书变得显而易见。这样的修改也旨在落入所附权利要求书的范围内。在有冲突的情况下，以包括定义的本披露为准。
实例
实例1：α-淀粉酶活性的测定
1.Phadebas测定
通过采用
片剂作为底物的方法可以确定α-淀粉酶活性。Phadebas片剂(
淀粉酶测试物(
Amylase Test)，由法玛西亚诊断公司(Pharmacia Diagnostic)提供)包含交联的不溶性蓝色淀粉聚合物，它已与牛血清白蛋白和缓冲物质混合并压片。
对于每一单次测量，将一片悬浮于包含5ml 50mM伯瑞坦-罗宾森(Britton-Robinson)缓冲液(50mM乙酸，50mM磷酸，50mM硼酸，0.1mM CaCl2，用NaOH调节pH至感兴趣的值)的管中。于感兴趣的温度下在水浴中进行该测试。在x ml的50mM伯瑞坦-罗宾森缓冲液中稀释待测试的α-淀粉酶。将1ml此α-淀粉酶溶液添加至5ml 50mM伯瑞坦-罗宾森缓冲液中。通过α-淀粉酶水解淀粉，从而给出可溶性蓝色片段。在620nm处用分光光度计测量所得到的蓝色溶液的吸光度，其是α-淀粉活性的函数。
重要的是在10或15分钟的孵育(测试时间)后测量的620nm吸光度在620nm的0.2-2.0的吸光度单位的范围内。在此吸光度范围内，在活性和吸光度之间存在线性关系(朗伯-比尔(Lambert-Beer)定律)。因此，必须调节酶的稀释以适合该标准。在一组指定的条件(温度、pH、反应时间、缓冲液条件)下，1mg给定的α-淀粉酶将水解某一量的底物并将产生蓝色。在620nm测量颜色强度。在给定组的条件下，所测量的吸光度与α-淀粉酶的比活性(纯的α-淀粉酶蛋白的每毫克活性)成正比。
2.替代方法
α-淀粉酶活性通过采用PNP-G7底物的方法来确定。PNP-G7是对硝基苯基-α,D-麦芽七糖苷的缩写，它是可以由内切淀粉酶切割的嵌段寡糖。切割之后，试剂盒中所包括的α-葡糖苷酶消化底物以释放自由PNP分子，该分子具有黄色并且因而可以通过可见分光光度法在λ＝405nm(400nm-420nm)下测量。包含PNP-G7底物和α-葡糖苷酶的试剂盒由勃林格-曼海姆公司(Bohringer-Mannheim)制造(目录号1054635)。
为了制备试剂溶液，将10ml底物/缓冲溶液添加至由制造商推荐的50ml酶/缓冲溶液中。通过将20μL样品转移至96孔微量滴定板并在25℃下孵育来进行测定。添加预平衡至25℃的200μL试剂溶液。将溶液混合并预孵育1分钟，并在ELISA读取器中在OD 405nm处每隔30秒经4分钟测量吸光度。
在一组给定条件下，时间相关吸收曲线的斜率与所讨论的α-淀粉酶的活性成正比例。
LAS敏感性的确定
将该变体与不同浓度的LAS(直链烷基苯磺酸酯；Nansa 1169/P)在40℃下孵育10分钟。
使用
测定法或使用PNP-G7底物的可替代方法确定残余活性。
将LAS稀释进0.1M磷酸盐缓冲液(pH7.5)中。
使用以下浓度：无LAS时，为500ppm、250ppm、100ppm、50ppm、25ppm、和10ppm。将变体在不同的LAS缓冲液中稀释至浓度为0.01mg/l-5mg/l，总体积为10ml，并在温度控制的水浴中孵育10分钟。通过将小等分试样转移至冷测定缓冲液中来停止孵育。在活动测量期间，LAS浓度低于1ppm是非常重要的，以免影响活性测量。
然后使用上述
测定或可替代方法一式二确定残余活性。活性是在减去空白后测量的。没有LAS的活性是100％。
实例2：使用全规模自动餐具洗涤(ADW)评估本发明的α-淀粉酶多肽的洗涤性能
为了评估本发明的多肽在洗涤剂基础组合物中的洗涤性能，可以使用全规模自动餐具洗涤(ADW)进行洗涤实验。全规模ADW装备用于测试模拟常规消费者装备的测试条件下多肽的洗涤性能。
在本研究中，测试条件是使用Miele Dishwasher Miele G4300SCU机器的常规50℃洗涤程序和短40℃程序。
洗涤性能总体描述。
按照如下说明，将用例如淀粉玷污的三聚氰胺瓷砖(DM-77/DM-177/DM-277/DM-377，来自测试材料中心BV(邮箱120，3133KT，弗拉尔丁恩，荷兰))用作测试材料，并使用19°dH-20°dH的自来水在40℃和50℃下在设定程序下进行洗涤(参见表2、3和4)。当洗涤剂分配器盖在餐具洗涤机中打开时，对于40℃洗涤以1.5mg多肽/洗涤或3mg多肽/洗涤的浓度添加洗涤剂和α-淀粉酶，对于50℃洗涤以0.5mg多肽/洗涤或1mg多肽/洗涤的浓度添加洗涤剂和α-淀粉酶。具有0mg多肽/L的测试用作空白并且对应于来自洗涤剂的贡献。全规模洗涤性能实验在下面指定的实验条件下进行：
表2
实验条件
表3
具有漂白剂的ADW标准洗涤剂
表4
没有漂白剂的ADW标准洗涤剂
洗涤后，将三聚氰胺瓷砖干燥。
洗涤性能测量为洗涤的瓷砖和未洗涤的瓷砖之间的反射的差异。使用用于获取光谱和进行反射差计算的Color-Eye 7000(CE7000)进行反射值测量。在460nm处(发光体中没有UV光)测量反射值。
如果改进因子(IF)在以上所列的一个或多个条件下至少为1.0，优选至少为1.2，则认为洗涤性能得到改进，即在40℃或50℃下，其中在40℃洗涤中变体浓度为1.5mg多肽/洗涤或3mg多肽/洗涤，以及0.5mg多肽/洗涤或1mg多肽/洗涤。
从全规模洗涤中获得的本发明的示例性多肽的洗涤性能显示在表5a(40℃)和表5b(50℃)(其中洗涤性能评分相对于SEQ ID NO:1的亲本α-淀粉酶的洗涤性能)中。
表5a
本发明的示例性多肽的ADW洗涤性能
表5b
本发明的示例性多肽的ADW洗涤性能
实例3：使用全规模自动机械应力测定(AMSA)评估本发明的α-淀粉酶多肽的洗涤性能
为了评估本发明的多肽在洗涤剂基础组合物中的洗涤性能，也可以使用自动机械应力测定(AMSA)进行洗涤实验。使用AMSA测试，可以检查大量小体积酶洗涤剂溶液的洗涤性能。AMSA板具有许多用于测试溶液的缝和盖子，盖子将待洗涤的纺织品小块布样对所有缝开口强力挤压。在洗涤时间期间，将平板、测试溶液、纺织品和盖子剧烈振动从而使测试溶液与纺织品接触并以规则、周期性振荡方式施加机械应力。关于进一步描述，参见WO02/42740(尤其是第23-24页的“定方法实施例”段落，其披露通过引用结合在此)。
洗涤性能总体描述
制备测试溶液，该测试溶液包含水(21°dH)、3.94g/L具有漂白剂的ADW标准洗涤剂或3.45g/L不具有漂白剂的ADW标准洗涤剂(如下规定的)(参见表6、7和8)、和本发明的多肽，该多肽的浓度为0.03mg、0.06mg、0.12mg和0.24mg多肽蛋白/L(40℃)或0.01mg、0.03mg、0.06mg和0.12mg酶蛋白/L(50℃)。添加带有淀粉污渍的织物(来自测试材料中心BV的CS-28，邮政信箱120，3133KT，弗拉尔丁恩，荷兰)并且将它们在40℃和50℃洗涤10或20分钟，如在下文中详细说明的那样。在流动自来水下彻底漂洗并且在黑暗中干燥之后，随后测量带有污渍的织物的光强度值作为洗涤性能的量度。具有0mg酶蛋白/L的测试用作空白并且对应于来自洗涤剂的贡献。优选地，在洗涤步骤期间施加机械作用，例如以将洗涤溶液与织物和瓷砖一起振摇、转动或搅拌的形式施加。AMSA洗涤性能实验在以下详细说明的实验条件下进行：
表6
实验条件
表7
具有漂白剂的ADW标准洗涤剂
表8
没有漂白剂的ADW标准洗涤剂
通过向测试系统添加CaCl2、MgCl2和NaHCO3(Ca2+:Mg2+:HCO3-＝4:1:10)，将水硬度调节至21°dH。在洗涤之后，将纺织品用自来水冲洗并干燥。
洗涤性能可以被测量为亮度，表达为当用白光照亮时从样品反射的光的强度。当样品被沾污时，其反射光的强度低于干净样品的反射光强度。因此，反射光的强度可以用来衡量洗涤性能。
使用专业平板扫描仪(EPSON Expression 10000XL,EPSON)进行颜色测量，该扫描仪用于捕获所洗涤纺织品的图像。
为了从扫描图像中提取光强度的值，将来自图像的48
24位彩色像素值转化为红色、绿色和蓝色(RGB)的值。通过将RGB值作为向量进行加和并且然后取所得向量的长度来计算强度值(Int)：
通过AMSA获得的根据本发明的变体的洗涤性能如下；
表9
本发明的示例性多肽的AMSA洗涤性能
序列表
<110> 诺维信公司(Novozymes A/S)
<120> 酶变体以及编码它们的多核苷酸
<130> 13193-WO-PCT
<160> 15
<170> PatentIn版本3.5
<210> 1
<211> 483
<212> PRT
<213> 芽孢杆菌属物种
<400> 1
His His Asn Gly Thr Asn Gly Thr Leu Met Gln Tyr Phe Glu Trp Tyr
1 5 10 15
Leu Pro Asn Asp Gly Asn His Trp Asn Arg Leu Arg Ser Asp Ala Ser
20 25 30
Asn Leu Lys Asp Lys Gly Ile Ser Ala Val Trp Ile Pro Pro Ala Trp
35 40 45
Lys Gly Ala Ser Gln Asn Asp Val Gly Tyr Gly Ala Tyr Asp Leu Tyr
50 55 60
Asp Leu Gly Glu Phe Asn Gln Lys Gly Thr Ile Arg Thr Lys Tyr Gly
65 70 75 80
Thr Arg Asn Gln Leu Gln Ala Ala Val Asn Ala Leu Lys Ser Asn Gly
85 90 95
Ile Gln Val Tyr Gly Asp Val Val Met Asn His Lys Gly Gly Ala Asp
100 105 110
Ala Thr Glu Met Val Lys Ala Val Glu Val Asn Pro Asn Asn Arg Asn
115 120 125
Gln Glu Val Ser Gly Glu Tyr Thr Ile Glu Ala Trp Thr Lys Phe Asp
130 135 140
Phe Pro Gly Arg Ala Asn Thr His Ser Asn Phe Lys Trp Arg Trp Tyr
145 150 155 160
His Phe Asp Gly Val Asp Trp Asp Gln Ser Arg Lys Leu Asn Asn Arg
165 170 175
Ile Tyr Lys Phe Arg Thr Lys Ala Trp Asp Trp Glu Val Asp Thr Glu
180 185 190
Phe Gly Asn Tyr Asp Tyr Leu Leu Tyr Ala Asp Ile Asp Met Asp His
195 200 205
Pro Glu Val Val Asn Glu Leu Arg Asn Trp Gly Val Trp Tyr Thr Asn
210 215 220
Thr Leu Gly Leu Asp Gly Phe Arg Ile Asp Ala Val Lys His Ile Lys
225 230 235 240
Tyr Ser Phe Thr Arg Asp Trp Ile Asn His Val Arg Ser Ala Ile Gly
245 250 255
Lys Asn Met Phe Ala Val Ala Glu Phe Trp Lys Asn Asp Leu Gly Ala
260 265 270
Ile Glu Asn Tyr Leu Asn Lys Thr Asn Trp Asn His Ser Val Phe Asp
275 280 285
Val Pro Leu His Phe Asn Leu Tyr Tyr Ala Ser Lys Ser Gly Gly Asn
290 295 300
Tyr Asp Met Arg Gln Ile Phe Asn Gly Thr Val Val Gln Lys His Pro
305 310 315 320
Thr His Ala Val Thr Phe Val Asp Asn His Asp Ser Gln Pro Glu Glu
325 330 335
Ser Leu Glu Ser Phe Val Arg Glu Trp Phe Lys Pro Leu Ala Tyr Ala
340 345 350
Leu Thr Leu Thr Arg Glu Gln Gly Tyr Pro Ser Val Phe Tyr Gly Asp
355 360 365
Tyr Tyr Gly Ile Pro Thr His Gly Val Pro Ala Met Lys Ser Lys Ile
370 375 380
Asp Pro Ile Leu Glu Ala Arg Gln Lys Tyr Ala Tyr Gly Arg Gln Asn
385 390 395 400
Asp Tyr Leu Asp His His Asn Ile Ile Gly Trp Thr Arg Glu Gly Asn
405 410 415
Thr Ala His Pro Asn Ser Gly Leu Ala Thr Ile Met Ser Asp Gly Ala
420 425 430
Gly Gly Asn Lys Trp Met Phe Val Gly Arg Asn Lys Ala Gly Gln Val
435 440 445
Trp Thr Asp Ile Thr Gly Asn Lys Ala Gly Thr Val Thr Ile Asn Ala
450 455 460
Asp Gly Trp Gly Asn Phe Ser Val Asn Gly Gly Ser Val Ser Ile Trp
465 470 475 480
Val Asn Lys
<210> 2
<211> 485
<212> PRT
<213> 枯草芽孢杆菌
<400> 2
His His Asn Gly Thr Asn Gly Thr Met Met Gln Tyr Phe Glu Trp Tyr
1 5 10 15
Leu Pro Asn Asp Gly Asn His Trp Asn Arg Leu Arg Ser Asp Ala Ser
20 25 30
Asn Leu Lys Asp Lys Gly Ile Ser Ala Val Trp Ile Pro Pro Ala Trp
35 40 45
Lys Gly Ala Ser Gln Asn Asp Val Gly Tyr Gly Ala Tyr Asp Leu Tyr
50 55 60
Asp Leu Gly Glu Phe Asn Gln Lys Gly Thr Ile Arg Thr Lys Tyr Gly
65 70 75 80
Thr Arg Asn Gln Leu Gln Ala Ala Val Asn Ala Leu Lys Ser Asn Gly
85 90 95
Ile Gln Val Tyr Gly Asp Val Val Met Asn His Lys Gly Gly Ala Asp
100 105 110
Ala Thr Glu Met Val Arg Ala Val Glu Val Asn Pro Asn Asn Arg Asn
115 120 125
Gln Glu Val Ser Gly Glu Tyr Thr Ile Glu Ala Trp Thr Lys Phe Asp
130 135 140
Phe Pro Gly Arg Gly Asn Thr His Ser Asn Phe Lys Trp Arg Trp Tyr
145 150 155 160
His Phe Asp Gly Val Asp Trp Asp Gln Ser Arg Lys Leu Asn Asn Arg
165 170 175
Ile Tyr Lys Phe Arg Gly Asp Gly Lys Gly Trp Asp Trp Glu Val Asp
180 185 190
Thr Glu Asn Gly Asn Tyr Asp Tyr Leu Met Tyr Ala Asp Ile Asp Met
195 200 205
Asp His Pro Glu Val Val Asn Glu Leu Arg Asn Trp Gly Val Trp Tyr
210 215 220
Thr Asn Thr Leu Gly Leu Asp Gly Phe Arg Ile Asp Ala Val Lys His
225 230 235 240
Ile Lys Tyr Ser Phe Thr Arg Asp Trp Ile Asn His Val Arg Ser Ala
245 250 255
Thr Gly Lys Asn Met Phe Ala Val Ala Glu Phe Trp Lys Asn Asp Leu
260 265 270
Gly Ala Ile Glu Asn Tyr Leu Asn Lys Thr Asn Trp Asn His Ser Val
275 280 285
Phe Asp Val Pro Leu His Tyr Asn Leu Tyr Asn Ala Ser Lys Ser Gly
290 295 300
Gly Asn Tyr Asp Met Arg Gln Ile Phe Asn Gly Thr Val Val Gln Arg
305 310 315 320
His Pro Met His Ala Val Thr Phe Val Asp Asn His Asp Ser Gln Pro
325 330 335
Glu Glu Ala Leu Glu Ser Phe Val Glu Glu Trp Phe Lys Pro Leu Ala
340 345 350
Tyr Ala Leu Thr Leu Thr Arg Glu Gln Gly Tyr Pro Ser Val Phe Tyr
355 360 365
Gly Asp Tyr Tyr Gly Ile Pro Thr His Gly Val Pro Ala Met Lys Ser
370 375 380
Lys Ile Asp Pro Ile Leu Glu Ala Arg Gln Lys Tyr Ala Tyr Gly Arg
385 390 395 400
Gln Asn Asp Tyr Leu Asp His His Asn Ile Ile Gly Trp Thr Arg Glu
405 410 415
Gly Asn Thr Ala His Pro Asn Ser Gly Leu Ala Thr Ile Met Ser Asp
420 425 430
Gly Ala Gly Gly Asn Lys Trp Met Phe Val Gly Arg Asn Lys Ala Gly
435 440 445
Gln Val Trp Thr Asp Ile Thr Gly Asn Arg Ala Gly Thr Val Thr Ile
450 455 460
Asn Ala Asp Gly Trp Gly Asn Phe Ser Val Asn Gly Gly Ser Val Ser
465 470 475 480
Ile Trp Val Asn Lys
485
<210> 3
<211> 269
<212> PRT
<213> 迟缓芽孢杆菌
<400> 3
Ala Gln Ser Val Pro Trp Gly Ile Ser Arg Val Gln Ala Pro Ala Ala
1 5 10 15
His Asn Arg Gly Leu Thr Gly Ser Gly Val Lys Val Ala Val Leu Asp
20 25 30
Thr Gly Ile Ser Thr His Pro Asp Leu Asn Ile Arg Gly Gly Ala Ser
35 40 45
Phe Val Pro Gly Glu Pro Ser Thr Gln Asp Gly Asn Gly His Gly Thr
50 55 60
His Val Ala Gly Thr Ile Ala Ala Leu Asn Asn Ser Ile Gly Val Leu
65 70 75 80
Gly Val Ala Pro Ser Ala Glu Leu Tyr Ala Val Lys Val Leu Gly Ala
85 90 95
Ser Gly Ser Gly Ser Val Ser Ser Ile Ala Gln Gly Leu Glu Trp Ala
100 105 110
Gly Asn Asn Gly Met His Val Ala Asn Leu Ser Leu Gly Ser Pro Ser
115 120 125
Pro Ser Ala Thr Leu Glu Gln Ala Val Asn Ser Ala Thr Ser Arg Gly
130 135 140
Val Leu Val Val Ala Ala Ser Gly Asn Ser Gly Ala Gly Ser Ile Ser
145 150 155 160
Tyr Pro Ala Arg Tyr Ala Asn Ala Met Ala Val Gly Ala Thr Asp Gln
165 170 175
Asn Asn Asn Arg Ala Ser Phe Ser Gln Tyr Gly Ala Gly Leu Asp Ile
180 185 190
Val Ala Pro Gly Val Asn Val Gln Ser Thr Tyr Pro Gly Ser Thr Tyr
195 200 205
Ala Ser Leu Asn Gly Thr Ser Met Ala Thr Pro His Val Ala Gly Ala
210 215 220
Ala Ala Leu Val Lys Gln Lys Asn Pro Ser Trp Ser Asn Val Gln Ile
225 230 235 240
Arg Asn His Leu Lys Asn Thr Ala Thr Ser Leu Gly Ser Thr Asn Leu
245 250 255
Tyr Gly Ser Gly Leu Val Asn Ala Glu Ala Ala Thr Arg
260 265
<210> 4
<211> 269
<212> PRT
<213> 疏棉状嗜热丝孢菌
<400> 4
Glu Val Ser Gln Asp Leu Phe Asn Gln Phe Asn Leu Phe Ala Gln Tyr
1 5 10 15
Ser Ala Ala Ala Tyr Cys Gly Lys Asn Asn Asp Ala Pro Ala Gly Thr
20 25 30
Asn Ile Thr Cys Thr Gly Asn Ala Cys Pro Glu Val Glu Lys Ala Asp
35 40 45
Ala Thr Phe Leu Tyr Ser Phe Glu Asp Ser Gly Val Gly Asp Val Thr
50 55 60
Gly Phe Leu Ala Leu Asp Asn Thr Asn Lys Leu Ile Val Leu Ser Phe
65 70 75 80
Arg Gly Ser Arg Ser Ile Glu Asn Trp Ile Gly Asn Leu Asn Phe Asp
85 90 95
Leu Lys Glu Ile Asn Asp Ile Cys Ser Gly Cys Arg Gly His Asp Gly
100 105 110
Phe Thr Ser Ser Trp Arg Ser Val Ala Asp Thr Leu Arg Gln Lys Val
115 120 125
Glu Asp Ala Val Arg Glu His Pro Asp Tyr Arg Val Val Phe Thr Gly
130 135 140
His Ser Leu Gly Gly Ala Leu Ala Thr Val Ala Gly Ala Asp Leu Arg
145 150 155 160
Gly Asn Gly Tyr Asp Ile Asp Val Phe Ser Tyr Gly Ala Pro Arg Val
165 170 175
Gly Asn Arg Ala Phe Ala Glu Phe Leu Thr Val Gln Thr Gly Gly Thr
180 185 190
Leu Tyr Arg Ile Thr His Thr Asn Asp Ile Val Pro Arg Leu Pro Pro
195 200 205
Arg Glu Phe Gly Tyr Ser His Ser Ser Pro Glu Tyr Trp Ile Lys Ser
210 215 220
Gly Thr Leu Val Pro Val Thr Arg Asn Asp Ile Val Lys Ile Glu Gly
225 230 235 240
Ile Asp Ala Thr Gly Gly Asn Asn Gln Pro Asn Ile Pro Asp Ile Pro
245 250 255
Ala His Leu Trp Tyr Phe Gly Leu Ile Gly Thr Cys Leu
260 265
<210> 5
<211> 485
<212> PRT
<213> 盐敏芽孢杆菌
<400> 5
His His Asn Gly Thr Asn Gly Thr Met Met Gln Tyr Phe Glu Trp His
1 5 10 15
Leu Pro Asn Asp Gly Asn His Trp Asn Arg Leu Arg Asp Asp Ala Ser
20 25 30
Asn Leu Arg Asn Arg Gly Ile Thr Ala Ile Trp Ile Pro Pro Ala Trp
35 40 45
Lys Gly Thr Ser Gln Asn Asp Val Gly Tyr Gly Ala Tyr Asp Leu Tyr
50 55 60
Asp Leu Gly Glu Phe Asn Gln Lys Gly Thr Val Arg Thr Lys Tyr Gly
65 70 75 80
Thr Arg Ser Gln Leu Glu Ser Ala Ile His Ala Leu Lys Asn Asn Gly
85 90 95
Val Gln Val Tyr Gly Asp Val Val Met Asn His Lys Gly Gly Ala Asp
100 105 110
Ala Thr Glu Asn Val Leu Ala Val Glu Val Asn Pro Asn Asn Arg Asn
115 120 125
Gln Glu Ile Ser Gly Asp Tyr Thr Ile Glu Ala Trp Thr Lys Phe Asp
130 135 140
Phe Pro Gly Arg Gly Asn Thr Tyr Ser Asp Phe Lys Trp Arg Trp Tyr
145 150 155 160
His Phe Asp Gly Val Asp Trp Asp Gln Ser Arg Gln Phe Gln Asn Arg
165 170 175
Ile Tyr Lys Phe Arg Gly Asp Gly Lys Ala Trp Asp Trp Glu Val Asp
180 185 190
Ser Glu Asn Gly Asn Tyr Asp Tyr Leu Met Tyr Ala Asp Val Asp Met
195 200 205
Asp His Pro Glu Val Val Asn Glu Leu Arg Arg Trp Gly Glu Trp Tyr
210 215 220
Thr Asn Thr Leu Asn Leu Asp Gly Phe Arg Ile Asp Ala Val Lys His
225 230 235 240
Ile Lys Tyr Ser Phe Thr Arg Asp Trp Leu Thr His Val Arg Asn Ala
245 250 255
Thr Gly Lys Glu Met Phe Ala Val Ala Glu Phe Trp Lys Asn Asp Leu
260 265 270
Gly Ala Leu Glu Asn Tyr Leu Asn Lys Thr Asn Trp Asn His Ser Val
275 280 285
Phe Asp Val Pro Leu His Tyr Asn Leu Tyr Asn Ala Ser Asn Ser Gly
290 295 300
Gly Asn Tyr Asp Met Ala Lys Leu Leu Asn Gly Thr Val Val Gln Lys
305 310 315 320
His Pro Met His Ala Val Thr Phe Val Asp Asn His Asp Ser Gln Pro
325 330 335
Gly Glu Ser Leu Glu Ser Phe Val Gln Glu Trp Phe Lys Pro Leu Ala
340 345 350
Tyr Ala Leu Ile Leu Thr Arg Glu Gln Gly Tyr Pro Ser Val Phe Tyr
355 360 365
Gly Asp Tyr Tyr Gly Ile Pro Thr His Ser Val Pro Ala Met Lys Ala
370 375 380
Lys Ile Asp Pro Ile Leu Glu Ala Arg Gln Asn Phe Ala Tyr Gly Thr
385 390 395 400
Gln His Asp Tyr Phe Asp His His Asn Ile Ile Gly Trp Thr Arg Glu
405 410 415
Gly Asn Thr Thr His Pro Asn Ser Gly Leu Ala Thr Ile Met Ser Asp
420 425 430
Gly Pro Gly Gly Glu Lys Trp Met Tyr Val Gly Gln Asn Lys Ala Gly
435 440 445
Gln Val Trp His Asp Ile Thr Gly Asn Lys Pro Gly Thr Val Thr Ile
450 455 460
Asn Ala Asp Gly Trp Ala Asn Phe Ser Val Asn Gly Gly Ser Val Ser
465 470 475 480
Ile Trp Val Lys Arg
485
<210> 6
<211> 484
<212> PRT
<213> 芽孢杆菌属物种
<400> 6
Asn Thr Ala Pro Ile Asn Glu Thr Met Met Gln Tyr Phe Glu Trp Asp
1 5 10 15
Leu Pro Asn Asp Gly Thr Leu Trp Thr Lys Val Lys Asn Glu Ala Ala
20 25 30
Asn Leu Ser Ser Leu Gly Ile Thr Ala Leu Trp Leu Pro Pro Ala Tyr
35 40 45
Lys Gly Thr Ser Gln Ser Asp Val Gly Tyr Gly Val Tyr Asp Leu Tyr
50 55 60
Asp Leu Gly Glu Phe Asn Gln Lys Gly Thr Ile Arg Thr Lys Tyr Gly
65 70 75 80
Thr Lys Thr Gln Tyr Ile Gln Ala Ile Gln Ala Ala Lys Ala Ala Gly
85 90 95
Met Gln Val Tyr Ala Asp Val Val Phe Asn His Lys Ala Gly Ala Asp
100 105 110
Gly Thr Glu Phe Val Asp Ala Val Glu Val Asp Pro Ser Asn Arg Asn
115 120 125
Gln Glu Thr Ser Gly Thr Tyr Gln Ile Gln Ala Trp Thr Lys Phe Asp
130 135 140
Phe Pro Gly Arg Gly Asn Thr Tyr Ser Ser Phe Lys Trp Arg Trp Tyr
145 150 155 160
His Phe Asp Gly Thr Asp Trp Asp Glu Ser Arg Lys Leu Asn Arg Ile
165 170 175
Tyr Lys Phe Arg Ser Thr Gly Lys Ala Trp Asp Trp Glu Val Asp Thr
180 185 190
Glu Asn Gly Asn Tyr Asp Tyr Leu Met Phe Ala Asp Leu Asp Met Asp
195 200 205
His Pro Glu Val Val Thr Glu Leu Lys Asn Trp Gly Thr Trp Tyr Val
210 215 220
Asn Thr Thr Asn Ile Asp Gly Phe Arg Leu Asp Ala Val Lys His Ile
225 230 235 240
Lys Tyr Thr Phe Phe Pro Asp Trp Leu Thr Tyr Val Arg Asn Gln Thr
245 250 255
Gly Lys Asn Leu Phe Ala Val Gly Glu Phe Trp Ser Tyr Asp Val Asn
260 265 270
Lys Leu His Asn Tyr Ile Thr Lys Thr Asn Gly Ser Met Ser Leu Phe
275 280 285
Asp Ala Pro Leu His Asn Asn Phe Tyr Thr Ala Ser Lys Ser Ser Gly
290 295 300
Tyr Phe Asp Met Arg Tyr Leu Leu Asn Asn Thr Leu Met Lys Asp Gln
305 310 315 320
Pro Ser Leu Ala Val Thr Leu Val Asp Asn His Asp Thr Gln Pro Gly
325 330 335
Gln Ser Leu Gln Ser Trp Val Glu Pro Trp Phe Lys Pro Leu Ala Tyr
340 345 350
Ala Phe Ile Leu Thr Arg Gln Glu Gly Tyr Pro Cys Val Phe Tyr Gly
355 360 365
Asp Tyr Tyr Gly Ile Pro Lys Tyr Asn Ile Pro Gly Leu Lys Ser Lys
370 375 380
Ile Asp Pro Leu Leu Ile Ala Arg Arg Asp Tyr Ala Tyr Gly Thr Gln
385 390 395 400
Arg Asp Tyr Ile Asp His Gln Asp Ile Ile Gly Trp Thr Arg Glu Gly
405 410 415
Ile Asp Thr Lys Pro Asn Ser Gly Leu Ala Ala Leu Ile Thr Asp Gly
420 425 430
Pro Gly Gly Ser Lys Trp Met Tyr Val Gly Lys Lys His Ala Gly Lys
435 440 445
Val Phe Tyr Asp Leu Thr Gly Asn Arg Ser Asp Thr Val Thr Ile Asn
450 455 460
Ala Asp Gly Trp Gly Glu Phe Lys Val Asn Gly Gly Ser Val Ser Ile
465 470 475 480
Trp Val Ala Lys
<210> 7
<211> 485
<212> PRT
<213> 噬细胞菌属物种
<400> 7
Ala Ala Thr Asn Gly Thr Met Met Gln Tyr Phe Glu Trp Tyr Val Pro
1 5 10 15
Asn Asp Gly Gln Gln Trp Asn Arg Leu Arg Thr Asp Ala Pro Tyr Leu
20 25 30
Ser Ser Val Gly Ile Thr Ala Val Trp Thr Pro Pro Ala Tyr Lys Gly
35 40 45
Thr Ser Gln Ala Asp Val Gly Tyr Gly Pro Tyr Asp Leu Tyr Asp Leu
50 55 60
Gly Glu Phe Asn Gln Lys Gly Thr Val Arg Thr Lys Tyr Gly Thr Lys
65 70 75 80
Gly Glu Leu Lys Ser Ala Val Asn Thr Leu His Ser Asn Gly Ile Gln
85 90 95
Val Tyr Gly Asp Val Val Met Asn His Lys Ala Gly Ala Asp Tyr Thr
100 105 110
Glu Asn Val Thr Ala Val Glu Val Asn Pro Ser Asn Arg Asn Gln Glu
115 120 125
Thr Ser Gly Glu Tyr Asn Ile Gln Ala Trp Thr Gly Phe Asn Phe Pro
130 135 140
Gly Arg Gly Thr Thr Tyr Ser Asn Phe Lys Trp Gln Trp Phe His Phe
145 150 155 160
Asp Gly Thr Asp Trp Asp Gln Ser Arg Ser Leu Ser Arg Ile Phe Lys
165 170 175
Phe Arg Gly Thr Gly Lys Ala Trp Asp Trp Glu Val Ser Ser Glu Asn
180 185 190
Gly Asn Tyr Asp Tyr Leu Met Tyr Ala Asp Ile Asp Tyr Asp His Pro
195 200 205
Asp Val Val Asn Glu Met Lys Lys Trp Gly Val Trp Tyr Ala Asn Glu
210 215 220
Val Gly Leu Asp Gly Tyr Arg Leu Asp Ala Val Lys His Ile Lys Phe
225 230 235 240
Ser Phe Leu Lys Asp Trp Val Asp Asn Ala Arg Ala Ala Thr Gly Lys
245 250 255
Glu Met Phe Thr Val Gly Glu Tyr Trp Gln Asn Asp Leu Gly Ala Leu
260 265 270
Asn Asn Tyr Leu Ala Lys Val Asn Tyr Asn Gln Ser Leu Phe Asp Ala
275 280 285
Pro Leu His Tyr Asn Phe Tyr Ala Ala Ser Thr Gly Gly Gly Tyr Tyr
290 295 300
Asp Met Arg Asn Ile Leu Asn Asn Thr Leu Val Ala Ser Asn Pro Thr
305 310 315 320
Lys Ala Val Thr Leu Val Glu Asn His Asp Thr Gln Pro Gly Gln Ser
325 330 335
Leu Glu Ser Thr Val Gln Pro Trp Phe Lys Pro Leu Ala Tyr Ala Phe
340 345 350
Ile Leu Thr Arg Ser Gly Gly Tyr Pro Ser Val Phe Tyr Gly Asp Met
355 360 365
Tyr Gly Thr Lys Gly Thr Thr Thr Arg Glu Ile Pro Ala Leu Lys Ser
370 375 380
Lys Ile Glu Pro Leu Leu Lys Ala Arg Lys Asp Tyr Ala Tyr Gly Thr
385 390 395 400
Gln Arg Asp Tyr Ile Asp Asn Pro Asp Val Ile Gly Trp Thr Arg Glu
405 410 415
Gly Asp Ser Thr Lys Ala Lys Ser Gly Leu Ala Thr Val Ile Thr Asp
420 425 430
Gly Pro Gly Gly Ser Lys Arg Met Tyr Val Gly Thr Ser Asn Ala Gly
435 440 445
Glu Ile Trp Tyr Asp Leu Thr Gly Asn Arg Thr Asp Lys Ile Thr Ile
450 455 460
Gly Ser Asp Gly Tyr Ala Thr Phe Pro Val Asn Gly Gly Ser Val Ser
465 470 475 480
Val Trp Val Gln Gln
485
<210> 8
<211> 485
<212> PRT
<213> 芽孢杆菌属物种
<400> 8
His His Asn Gly Thr Asn Gly Thr Met Met Gln Tyr Phe Glu Trp Tyr
1 5 10 15
Leu Pro Asn Asp Gly Asn His Trp Asn Arg Leu Asn Ser Asp Ala Ser
20 25 30
Asn Leu Lys Ser Lys Gly Ile Thr Ala Val Trp Ile Pro Pro Ala Trp
35 40 45
Lys Gly Ala Ser Gln Asn Asp Val Gly Tyr Gly Ala Tyr Asp Leu Tyr
50 55 60
Asp Leu Gly Glu Phe Asn Gln Lys Gly Thr Val Arg Thr Lys Tyr Gly
65 70 75 80
Thr Arg Ser Gln Leu Gln Ala Ala Val Thr Ser Leu Lys Asn Asn Gly
85 90 95
Ile Gln Val Tyr Gly Asp Val Val Met Asn His Lys Gly Gly Ala Asp
100 105 110
Ala Thr Glu Met Val Arg Ala Val Glu Val Asn Pro Asn Asn Arg Asn
115 120 125
Gln Glu Val Thr Gly Glu Tyr Thr Ile Glu Ala Trp Thr Arg Phe Asp
130 135 140
Phe Pro Gly Arg Gly Asn Thr His Ser Ser Phe Lys Trp Arg Trp Tyr
145 150 155 160
His Phe Asp Gly Val Asp Trp Asp Gln Ser Arg Arg Leu Asn Asn Arg
165 170 175
Ile Tyr Lys Phe Arg Gly His Gly Lys Ala Trp Asp Trp Glu Val Asp
180 185 190
Thr Glu Asn Gly Asn Tyr Asp Tyr Leu Met Tyr Ala Asp Ile Asp Met
195 200 205
Asp His Pro Glu Val Val Asn Glu Leu Arg Asn Trp Gly Val Trp Tyr
210 215 220
Thr Asn Thr Leu Gly Leu Asp Gly Phe Arg Ile Asp Ala Val Lys His
225 230 235 240
Ile Lys Tyr Ser Phe Thr Arg Asp Trp Ile Asn His Val Arg Ser Ala
245 250 255
Thr Gly Lys Asn Met Phe Ala Val Ala Glu Phe Trp Lys Asn Asp Leu
260 265 270
Gly Ala Ile Glu Asn Tyr Leu Gln Lys Thr Asn Trp Asn His Ser Val
275 280 285
Phe Asp Val Pro Leu His Tyr Asn Leu Tyr Asn Ala Ser Lys Ser Gly
290 295 300
Gly Asn Tyr Asp Met Arg Asn Ile Phe Asn Gly Thr Val Val Gln Arg
305 310 315 320
His Pro Ser His Ala Val Thr Phe Val Asp Asn His Asp Ser Gln Pro
325 330 335
Glu Glu Ala Leu Glu Ser Phe Val Glu Glu Trp Phe Lys Pro Leu Ala
340 345 350
Tyr Ala Leu Thr Leu Thr Arg Glu Gln Gly Tyr Pro Ser Val Phe Tyr
355 360 365
Gly Asp Tyr Tyr Gly Ile Pro Thr His Gly Val Pro Ala Met Arg Ser
370 375 380
Lys Ile Asp Pro Ile Leu Glu Ala Arg Gln Lys Tyr Ala Tyr Gly Lys
385 390 395 400
Gln Asn Asp Tyr Leu Asp His His Asn Ile Ile Gly Trp Thr Arg Glu
405 410 415
Gly Asn Thr Ala His Pro Asn Ser Gly Leu Ala Thr Ile Met Ser Asp
420 425 430
Gly Ala Gly Gly Ser Lys Trp Met Phe Val Gly Arg Asn Lys Ala Gly
435 440 445
Gln Val Trp Ser Asp Ile Thr Gly Asn Arg Thr Gly Thr Val Thr Ile
450 455 460
Asn Ala Asp Gly Trp Gly Asn Phe Ser Val Asn Gly Gly Ser Val Ser
465 470 475 480
Ile Trp Val Asn Lys
485
<210> 9
<211> 483
<212> PRT
<213> 芽孢杆菌属物种
<400> 9
His His Asn Gly Thr Asn Gly Thr Met Met Gln Tyr Phe Glu Trp Tyr
1 5 10 15
Leu Pro Asn Asp Gly Asn His Trp Asn Arg Leu Asn Ser Asp Ala Ser
20 25 30
Asn Leu Lys Ser Lys Gly Ile Thr Ala Val Trp Ile Pro Pro Ala Trp
35 40 45
Lys Gly Ala Ser Gln Asn Asp Val Gly Tyr Gly Ala Tyr Asp Leu Tyr
50 55 60
Asp Leu Gly Glu Phe Asn Gln Lys Gly Thr Val Arg Thr Lys Tyr Gly
65 70 75 80
Thr Arg Ser Gln Leu Gln Ala Ala Val Thr Ser Leu Lys Asn Asn Gly
85 90 95
Ile Gln Val Tyr Gly Asp Val Val Met Asn His Lys Gly Gly Ala Asp
100 105 110
Ala Thr Glu Met Val Arg Ala Val Glu Val Asn Pro Asn Asn Arg Asn
115 120 125
Gln Glu Val Thr Gly Glu Tyr Thr Ile Glu Ala Trp Thr Arg Phe Asp
130 135 140
Phe Pro Gly Arg Gly Asn Thr His Ser Ser Phe Lys Trp Arg Trp Tyr
145 150 155 160
His Phe Asp Gly Val Asp Trp Asp Gln Ser Arg Arg Leu Asn Asn Arg
165 170 175
Ile Tyr Lys Phe Arg Gly Lys Ala Trp Asp Trp Glu Val Asp Thr Glu
180 185 190
Asn Gly Asn Tyr Asp Tyr Leu Met Tyr Ala Asp Ile Asp Met Asp His
195 200 205
Pro Glu Val Val Asn Glu Leu Arg Asn Trp Gly Val Trp Tyr Thr Asn
210 215 220
Thr Leu Gly Leu Asp Gly Phe Arg Ile Asp Ala Val Lys His Ile Lys
225 230 235 240
Tyr Ser Phe Thr Arg Asp Trp Ile Asn His Val Arg Ser Ala Thr Gly
245 250 255
Lys Asn Met Phe Ala Val Ala Glu Phe Trp Lys Asn Asp Leu Gly Ala
260 265 270
Ile Glu Asn Tyr Leu Gln Lys Thr Asn Trp Asn His Ser Val Phe Asp
275 280 285
Val Pro Leu His Tyr Asn Leu Tyr Asn Ala Ser Lys Ser Gly Gly Asn
290 295 300
Tyr Asp Met Arg Asn Ile Phe Asn Gly Thr Val Val Gln Arg His Pro
305 310 315 320
Ser His Ala Val Thr Phe Val Asp Asn His Asp Ser Gln Pro Glu Glu
325 330 335
Ala Leu Glu Ser Phe Val Glu Glu Trp Phe Lys Pro Leu Ala Tyr Ala
340 345 350
Leu Thr Leu Thr Arg Glu Gln Gly Tyr Pro Ser Val Phe Tyr Gly Asp
355 360 365
Tyr Tyr Gly Ile Pro Thr His Gly Val Pro Ala Met Arg Ser Lys Ile
370 375 380
Asp Pro Ile Leu Glu Ala Arg Gln Lys Tyr Ala Tyr Gly Pro Gln His
385 390 395 400
Asp Tyr Leu Asp His Pro Asp Val Ile Gly Trp Thr Arg Glu Gly Asp
405 410 415
Ser Ser His Pro Lys Ser Gly Leu Ala Thr Leu Ile Thr Asp Gly Pro
420 425 430
Gly Gly Ser Lys Arg Met Tyr Ala Gly Leu Lys Asn Ala Gly Glu Thr
435 440 445
Trp Tyr Asp Ile Thr Gly Asn Arg Ser Asp Thr Val Lys Ile Gly Ser
450 455 460
Asp Gly Trp Gly Glu Phe His Val Asn Asp Gly Ser Val Ser Ile Tyr
465 470 475 480
Val Gln Lys
<210> 10
<211> 485
<212> PRT
<213> 芽孢杆菌属物种
<400> 10
His His Asn Gly Thr Asn Gly Thr Met Met Gln Tyr Phe Glu Trp Tyr
1 5 10 15
Leu Pro Asn Asp Gly Asn His Trp Asn Arg Leu Arg Ser Asp Ala Ser
20 25 30
Asn Leu Lys Asp Lys Gly Ile Thr Ala Val Trp Ile Pro Pro Ala Trp
35 40 45
Lys Gly Ala Ser Gln Asn Asp Val Gly Tyr Gly Ala Tyr Asp Leu Tyr
50 55 60
Asp Leu Gly Glu Phe Asn Gln Lys Gly Thr Val Arg Thr Lys Tyr Gly
65 70 75 80
Thr Arg Asn Gln Leu Gln Ala Ala Val Thr Ala Leu Lys Ser Asn Gly
85 90 95
Ile Gln Val Tyr Gly Asp Val Val Met Asn His Lys Gly Gly Ala Asp
100 105 110
Ala Thr Glu Trp Val Arg Ala Val Glu Val Asn Pro Ser Asn Arg Asn
115 120 125
Gln Glu Val Ser Gly Asp Tyr Thr Ile Glu Ala Trp Thr Lys Phe Asp
130 135 140
Phe Pro Gly Arg Gly Asn Thr His Ser Asn Phe Lys Trp Arg Trp Tyr
145 150 155 160
His Phe Asp Gly Val Asp Trp Asp Gln Ser Arg Gln Leu Gln Asn Arg
165 170 175
Ile Tyr Lys Phe Arg Gly Asp Gly Lys Gly Trp Asp Trp Glu Val Asp
180 185 190
Thr Glu Asn Gly Asn Tyr Asp Tyr Leu Met Tyr Ala Asp Ile Asp Met
195 200 205
Asp His Pro Glu Val Val Asn Glu Leu Arg Asn Trp Gly Val Trp Tyr
210 215 220
Thr Asn Thr Leu Gly Leu Asp Gly Phe Arg Ile Asp Ala Val Lys His
225 230 235 240
Ile Lys Tyr Ser Phe Thr Arg Asp Trp Leu Thr His Val Arg Asn Thr
245 250 255
Thr Gly Lys Asn Met Phe Ala Val Ala Glu Phe Trp Lys Asn Asp Ile
260 265 270
Gly Ala Ile Glu Asn Tyr Leu Ser Lys Thr Asn Trp Asn His Ser Val
275 280 285
Phe Asp Val Pro Leu His Tyr Asn Leu Tyr Asn Ala Ser Arg Ser Gly
290 295 300
Gly Asn Tyr Asp Met Arg Gln Ile Phe Asn Gly Thr Val Val Gln Arg
305 310 315 320
His Pro Thr His Ala Val Thr Phe Val Asp Asn His Asp Ser Gln Pro
325 330 335
Glu Glu Ala Leu Glu Ser Phe Val Glu Glu Trp Phe Lys Pro Leu Ala
340 345 350
Cys Ala Leu Thr Leu Thr Arg Asp Gln Gly Tyr Pro Ser Val Phe Tyr
355 360 365
Gly Asp Tyr Tyr Gly Ile Pro Thr His Gly Val Pro Ala Met Lys Ser
370 375 380
Lys Ile Asp Pro Ile Leu Glu Ala Arg Gln Lys Tyr Ala Tyr Gly Lys
385 390 395 400
Gln Asn Asp Tyr Leu Asp His His Asn Met Ile Gly Trp Thr Arg Glu
405 410 415
Gly Asn Thr Ala His Pro Asn Ser Gly Leu Ala Thr Ile Met Ser Asp
420 425 430
Gly Pro Gly Gly Asn Lys Trp Met Tyr Val Gly Arg Asn Lys Ala Gly
435 440 445
Gln Val Trp Arg Asp Ile Thr Gly Asn Arg Ser Gly Thr Val Thr Ile
450 455 460
Asn Ala Asp Gly Trp Gly Asn Phe Ser Val Asn Gly Gly Ser Val Ser
465 470 475 480
Ile Trp Val Asn Asn
485
<210> 11
<211> 485
<212> PRT
<213> 芽孢杆菌属物种
<400> 11
His His Asn Gly Thr Asn Gly Thr Met Met Gln Tyr Phe Glu Trp Tyr
1 5 10 15
Leu Pro Asn Asp Gly Asn His Trp Asn Arg Leu Asn Ser Asp Ala Ser
20 25 30
Asn Leu Lys Ser Lys Gly Ile Thr Ala Val Trp Ile Pro Pro Ala Trp
35 40 45
Lys Gly Ala Ser Gln Asn Asp Val Gly Tyr Gly Ala Tyr Asp Leu Tyr
50 55 60
Asp Leu Gly Glu Phe Asn Gln Lys Gly Thr Val Arg Thr Lys Tyr Gly
65 70 75 80
Thr Arg Ser Gln Leu Gln Ala Ala Val Thr Ser Leu Lys Asn Asn Gly
85 90 95
Ile Gln Val Tyr Gly Asp Val Val Met Asn His Lys Gly Gly Ala Asp
100 105 110
Ala Thr Glu Met Val Arg Ala Val Glu Val Asn Pro Asn Asn Arg Asn
115 120 125
Gln Glu Val Thr Gly Glu Tyr Thr Ile Glu Ala Trp Thr Arg Phe Asp
130 135 140
Phe Pro Gly Arg Gly Asn Thr His Ser Ser Phe Lys Trp Arg Trp Tyr
145 150 155 160
His Phe Asp Gly Val Asp Trp Asp Gln Ser Arg Arg Leu Asn Asn Arg
165 170 175
Ile Tyr Lys Phe Arg Gly His Gly Lys Ala Trp Asp Trp Glu Val Asp
180 185 190
Thr Glu Asn Gly Asn Tyr Asp Tyr Leu Leu Tyr Ala Asp Ile Asp Met
195 200 205
Asp His Pro Glu Val Val Asn Glu Leu Arg Asn Trp Gly Val Trp Tyr
210 215 220
Thr Asn Thr Leu Gly Leu Asp Gly Phe Arg Ile Asp Ala Val Lys His
225 230 235 240
Ile Lys Tyr Ser Phe Thr Arg Asp Trp Ile Asn His Val Arg Ser Ala
245 250 255
Thr Gly Lys Asn Met Phe Ala Val Ala Glu Phe Trp Lys Asn Asp Leu
260 265 270
Gly Ala Ile Glu Asn Tyr Leu Gln Lys Thr Asn Trp Asn His Ser Val
275 280 285
Phe Asp Val Pro Leu His Tyr Asn Leu Tyr Asn Ala Ser Lys Ser Gly
290 295 300
Gly Asn Tyr Asp Met Arg Asn Ile Phe Asn Gly Thr Val Val Gln Arg
305 310 315 320
His Pro Ser His Ala Val Thr Phe Val Asp Asn His Asp Ser Gln Pro
325 330 335
Glu Glu Ala Leu Glu Ser Phe Val Glu Glu Trp Phe Lys Pro Leu Ala
340 345 350
Tyr Ala Leu Thr Leu Thr Arg Glu Gln Gly Tyr Pro Ser Val Phe Tyr
355 360 365
Gly Asp Tyr Tyr Gly Ile Pro Thr His Gly Val Pro Ala Met Arg Ser
370 375 380
Lys Ile Asp Pro Ile Leu Glu Ala Arg Gln Lys Tyr Ala Tyr Gly Lys
385 390 395 400
Gln Asn Asp Tyr Leu Asp His His Asn Ile Ile Gly Trp Thr Arg Glu
405 410 415
Gly Asn Thr Ala His Pro Asn Ser Gly Leu Ala Thr Ile Met Ser Asp
420 425 430
Gly Ala Gly Gly Ser Lys Trp Met Phe Val Gly Arg Asn Lys Ala Gly
435 440 445
Gln Val Trp Ser Asp Ile Thr Gly Asn Arg Thr Gly Thr Val Thr Ile
450 455 460
Asn Ala Asp Gly Trp Gly Asn Phe Ser Val Asn Gly Gly Ser Val Ser
465 470 475 480
Ile Trp Val Asn Lys
485
<210> 12
<211> 351
<212> PRT
<213> 芽孢杆菌属物种
<400> 12
Tyr Asn Pro Val Thr Glu Asp Glu Leu Tyr His Ser Phe Asp Ser His
1 5 10 15
Asp Ala Arg Asn Trp Gln Ile Ser Asp Gly Trp Arg Asn Gly Asp Asp
20 25 30
Phe Phe Gly Cys His Trp Ser Gln Asn Arg Val Asn Phe Asn Arg Gly
35 40 45
Glu Met Glu Leu Ser Leu Arg Thr Asn Tyr Ser Tyr Ser Ala Pro Tyr
50 55 60
Asn Tyr Glu Cys Ala Glu Tyr Ala Thr Ser Asn Phe Tyr Gly Tyr Gly
65 70 75 80
Leu Tyr Glu Val Ser Met Lys Pro Ala Asn Val Ser Gly Val Ile Ser
85 90 95
Ser Phe Phe Thr Tyr Thr Gly Pro Ser Tyr Asn Gly Ala Pro Trp Asp
100 105 110
Glu Ile Asp Ile Glu Phe Leu Gly Asn Asp Thr Thr Lys Val Gln Phe
115 120 125
Asn Tyr Tyr Thr Asn Gly Val Gly Gly Asn Glu Ile Ile Tyr Asp Leu
130 135 140
Gly Phe Asp Ala Ala Asn Ser Phe Asn Thr Tyr Ala Phe Asp Trp Gln
145 150 155 160
Glu Asn Tyr Ile Ser Trp Tyr Val Asn Gly Asn Leu Val Ala Thr Ala
165 170 175
Thr Glu Asn Ile Pro Ser Asn Pro Ser Lys Ile Met Met Asn Val Trp
180 185 190
Asn Thr Tyr Gly Ile Asp Glu Trp Ala Gly Ala Tyr Gly Gly Glu Ala
195 200 205
Ala Asn Ala Thr Tyr Glu Trp Val Arg Tyr Thr Pro Asn Asn Gly Asn
210 215 220
Thr Thr Pro Ser Thr Ala Pro Asp Phe Gln Leu Gln Ala Cys Asp Tyr
225 230 235 240
Ser Asp Ser Ser Gly Ile Thr Ser Trp Ser Cys Gly Val Gly Thr Phe
245 250 255
His Ser Ser Asn Trp Ile Lys Phe Asp Ser Val Asp Leu Ser Thr Gly
260 265 270
Tyr Asn Ala Phe Ala Val Ser Tyr Thr Ser Pro Gly Ser Gly Ser Phe
275 280 285
Asp Ile Arg Leu Gly Ser Pro His Gly Gln Arg Ile Gly Thr Val Asn
290 295 300
Tyr Gly Ala Thr Gly Gly Trp Ser Asn Tyr Glu Trp Ser Gly Thr Pro
305 310 315 320
Ser Leu Asp Val Thr Val Arg Gly Ala His Asp Ile Tyr Ile Val Ala
325 330 335
Thr Ser Gly Ala Ala Asn Leu Arg Glu Phe Trp Phe Lys Asn Glu
340 345 350
<210> 13
<211> 245
<212> PRT
<213> 秋叶氏芽孢杆菌（Bacillus akibai）
<400> 13
Ala Glu Arg Pro Ile Gly Thr Thr Phe Val Glu Thr Phe Glu Ser Tyr
1 5 10 15
Asp Ser Glu Arg Trp Ser Lys Ala Gly Val Trp Thr Asn Gly Gln Met
20 25 30
Phe Asn Ala Thr Trp Tyr Pro Glu Gln Val Thr Phe Ser Asp Gly Lys
35 40 45
Met Lys Leu Gln Ile Asp Lys Glu Asp Asn Glu Thr Ala Ser Pro Pro
50 55 60
Tyr Lys Ala Gly Glu Leu Arg Thr Asn Asp Phe Tyr His Tyr Gly Leu
65 70 75 80
Phe Glu Val Ser Met Lys Pro Ala Lys Ser Thr Gly Thr Val Ser Ser
85 90 95
Phe Phe Thr Tyr Thr Gly Pro Trp Asp Trp Asp Asn Asp Pro Trp Asp
100 105 110
Glu Ile Asp Ile Glu Phe Leu Gly Lys Asp Thr Thr Lys Ile Gln Phe
115 120 125
Asn Tyr Phe Thr Asn Gly Val Gly Gly Asn Glu His Tyr His Glu Leu
130 135 140
Gly Phe Asp Ala Ala Asp Asp Phe Asn Thr Tyr Ala Phe Glu Trp Arg
145 150 155 160
Pro Glu Ser Ile Arg Trp Phe Val Asn Gly Glu Leu Val His Thr Ala
165 170 175
Thr Glu Asn Ile Pro Gln Thr Pro Gln Lys Ile Met Met Asn Leu Trp
180 185 190
Pro Gly Ile Gly Val Asp Gly Trp Thr Gly Arg Phe Asn Gly Glu Asp
195 200 205
Thr Pro Val Val Thr Gln Tyr Asp Trp Val Lys Tyr Thr Pro Leu Glu
210 215 220
Glu Leu Gly Cys Tyr Asn Glu Lys Asn Asn Lys Tyr Lys Lys Cys Lys
225 230 235 240
Lys Thr Lys Val Lys
245
<210> 14
<211> 222
<212> PRT
<213> 黏琼脂芽孢杆菌
<400> 14
His Asn Pro Val Thr Asp Glu Glu Val Tyr His Ser Phe Asn Ser His
1 5 10 15
Asp Trp Gln Asn Trp Asn Met Ser Asp Gly Trp Lys Asn Asp Asp Tyr
20 25 30
Phe Phe Gly Cys His Trp Ser Gln Asn Arg Val Asn Phe Tyr Gly Gly
35 40 45
Gln Met Glu Leu Ser Leu Arg Thr Asn Tyr Ser Tyr Ala Pro Pro Tyr
50 55 60
Asn Tyr Glu Cys Ala Glu Tyr Thr Thr Asn Asn Phe Tyr Gly Tyr Gly
65 70 75 80
Leu Tyr Glu Val Ser Met Lys Pro Ala Lys Val Ser Gly Val Ile Ser
85 90 95
Ser Phe Phe Thr Tyr Thr Gly Pro Ser Tyr Asn Gly Ala Pro Trp Asp
100 105 110
Glu Ile Asp Ile Glu Phe Leu Gly Asn Asp Thr Thr Lys Val Gln Phe
115 120 125
Asn Tyr Tyr Thr Asp Gly Val Gly Gly Asn Glu Ile Leu Tyr Asp Leu
130 135 140
Gly Phe Asp Ala Ala Asp Ser Tyr Asn Thr Tyr Ala Phe Asp Trp Gln
145 150 155 160
Glu Asn Tyr Ile Asn Trp Tyr Val Asn Gly Gln Leu Val Ala Thr Ala
165 170 175
Thr Glu Asn Ile Pro Ser Asn Pro Ser Lys Ile Met Met Asn Ile Trp
180 185 190
Asn Thr Tyr Gly Ile Asp Glu Trp Ala Gly Arg Tyr Tyr Gly Glu Asp
195 200 205
Ala Asn Ala Ser Tyr Asn Trp Val Arg Tyr Thr Pro Asn Arg
210 215 220
<210> 15
<211> 214
<212> PRT
<213> 莫海威芽孢杆菌（Bacillus mojavensis）
<400> 15
Gln Thr Gly Gly Ser Phe Phe Asp Pro Phe Asn Gly Tyr Asn Ser Gly
1 5 10 15
Phe Trp Gln Lys Ala Asn Gly Tyr Ser Asn Gly Asn Met Phe Asn Cys
20 25 30
Thr Trp Arg Ala Asn Asn Val Ser Met Thr Ser Leu Gly Glu Met Arg
35 40 45
Leu Ala Leu Thr Ser Pro Ser Tyr Asn Lys Phe Asp Cys Gly Glu Asn
50 55 60
Arg Ser Val Gln Thr Tyr Gly Tyr Gly Leu Tyr Glu Val Arg Met Lys
65 70 75 80
Pro Ala Lys Asn Val Gly Ile Val Ser Ser Phe Phe Thr Tyr Thr Gly
85 90 95
Pro Thr Asp Gly Thr Pro Trp Asp Glu Ile Asp Ile Glu Phe Leu Gly
100 105 110
Lys Asp Thr Thr Lys Val Gln Phe Asn Tyr Tyr Thr Asn Gly Val Gly
115 120 125
Asn His Glu Lys Leu Val Asp Leu Gly Phe Asp Ala Ala Asn Ala Tyr
130 135 140
His Thr Tyr Ala Phe Asp Trp Gln Pro Asn Ser Ile Lys Trp Tyr Val
145 150 155 160
Asp Gly Gln Leu Lys His Thr Ala Thr Ser Gln Ile Pro Thr Thr Pro
165 170 175
Gly Lys Ile Met Met Asn Leu Trp Asn Gly Thr Gly Val Asp Glu Trp
180 185 190
Leu Gly Ser Tyr Asn Gly Val Thr Pro Leu Tyr Ala His Tyr Asp Trp
195 200 205
Val Arg Tyr Thr Lys Lys
210
Claims (16)
1.一种包含SEQ ID NO:1的变体氨基酸序列的多肽，其中与SEQ ID NO:1的多肽相比，该多肽具有α-淀粉酶活性并展现增强的洗涤性能,其中变体氨基酸序列与SEQ ID NO:1至少95％相同，和包含W167Y取代，其中编号是根据SEQ ID NO:2所示氨基酸序列进行编号，和其中所述多肽由具有突变的SEQ ID NO:1的氨基酸序列组成，所述突变选自以下组成的组：
W167Y+H210N+S339A
W48F+W167Y+H210N+S339A
W48F+W167Y+H210N+S339A+V366I
W167Y+H210N+S339A+S365C
W167Y+H210N+S339A+S365C+V366I
W48F+W167Y+H210N+S339A+S365C
W167Y+H210N+Y299F+S339A+S365C+V366I
W167Y+A186N+H210N+S339A+V366I
W48F+W167Y+A186N+H210N+S339A
W167Y+A186N+H210N+Y299F+S339A+V366I
和其中当在包含漂白剂的洗涤剂的ADW测定中，并且在40℃进行10min评估多肽时，所述增强的洗涤性能对应于至少1.2的改进因子(IF)。
2.一种编码根据权利要求1中所述的多肽的多核苷酸。
3.一种包含根据权利要求2所述的多核苷酸的核酸构建体。
4.一种包含根据权利要求2所述的多核苷酸的表达载体。
5.一种包含根据权利要求2所述的多核苷酸的宿主细胞。
6.一种产生α-淀粉酶多肽的方法，该方法包括：
(a)在适合于表达所述多肽的条件下培养根据权利要求5所述的宿主细胞；以及
(b)回收所述多肽。
7.一种洗涤剂组合物，该洗涤剂组合物包含根据权利要求1中所述的多肽和表面活性剂、或浓缩物或添加剂用于制备该洗涤剂组合物。
8.根据权利要求7所述的组合物，其中该表面活性剂选自下组，该组由以下组成：阴离子表面活性剂、阳离子表面活性剂、非离子表面活性剂和两性离子表面活性剂。
9.根据权利要求7或8所述的组合物，该组合物进一步包含选自下组的一种或多种另外的组分，该组由以下组成：氧化剂、漂白活化剂、螯合剂、填充剂、助洗剂、缓冲剂、结构剂、螯合剂、荧光增白剂、消泡剂、酶、香料、抗再沉积剂、皮肤调理剂、柔软剂、乳化剂、和着色剂。
10.根据权利要求7至9中任一项所述的组合物，其中所述组合物是液体或粉末衣物洗涤剂组合物。
11.根据权利要求7至9中任一项所述的组合物，其中所述组合物是液体或粉末自动餐具洗涤(ADW)洗涤剂组合物。
12.根据权利要求7至9中任一项所述的组合物，其中所述组合物是液体手动餐具洗涤剂组合物。
13.根据权利要求1中所述的变体、或根据权利要求7至12中任一项所述的组合物在家庭或工业清洗过程中的用途。
14.根据权利要求13所述的用途，用于清洗织物，例如衣物洗涤。
15.根据权利要求13所述的用途，用于陶瓷、塑料或玻璃材料的清洗，例如餐具洗涤。
16.一种用于从表面去除污渍的方法，该方法包括使所述表面与根据权利要求7至12中任一项所述的组合物接触。
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| PCT/EP2016/082828 WO2017114891A1 (en) | 2015-12-30 | 2016-12-29 | Enzyme variants and polynucleotides encoding the same |
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| CN108603185B (zh) | 2015-12-30 | 2022-05-17 | 诺维信公司 | 酶变体以及编码它们的多核苷酸 |
| EP3241890B1 (en) * | 2016-05-03 | 2019-06-26 | The Procter and Gamble Company | Automatic dishwashing detergent composition |
| US11441139B2 (en) | 2017-08-18 | 2022-09-13 | Danisco Us Inc (157111) | α-Amylase variants |
| KR101991684B1 (ko) * | 2017-09-29 | 2019-09-30 | 오스템임플란트 주식회사 | 상아세관 침투력 및 코팅 유지력이 향상된 치아 도포제 및 이의 제조방법 |
| WO2020028443A1 (en) * | 2018-07-31 | 2020-02-06 | Danisco Us Inc | Variant alpha-amylases having amino acid substitutions that lower the pka of the general acid |
| MX2021011287A (es) * | 2019-03-21 | 2021-10-13 | Novozymes As | Variantes de alfa-amilasa y polinucleotidos que codifican las mismas. |
| EP4022019A1 (en) * | 2019-08-27 | 2022-07-06 | Novozymes A/S | Detergent composition |
| US20210122998A1 (en) * | 2019-10-24 | 2021-04-29 | The Procter & Gamble Company | Automatic dishwashing detergent composition comprising an amylase |
| JP2023506927A (ja) * | 2019-12-19 | 2023-02-20 | ノボザイムス アクティーゼルスカブ | α－アミラーゼ変異体 |
| US20230159861A1 (en) * | 2020-01-23 | 2023-05-25 | Novozymes A/S | Enzyme compositions and uses thereof |
| WO2023225459A2 (en) | 2022-05-14 | 2023-11-23 | Novozymes A/S | Compositions and methods for preventing, treating, supressing and/or eliminating phytopathogenic infestations and infections |
| WO2022175435A1 (en) * | 2021-02-22 | 2022-08-25 | Basf Se | Amylase variants |
| EP4047088A1 (en) * | 2021-02-22 | 2022-08-24 | Basf Se | Amylase variants |
| CN113151329B (zh) * | 2021-03-30 | 2023-09-08 | 云南师范大学 | 中性蛋白酶突变体及其构造方法和应用 |
| CN114381448B (zh) * | 2022-01-10 | 2024-02-20 | 鑫缘茧丝绸集团股份有限公司 | 一种葡聚糖酶突变体及其应用 |
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| Publication number | Publication date |
|---|---|
| WO2017114891A1 (en) | 2017-07-06 |
| CN114921442A (zh) | 2022-08-19 |
| US11407986B2 (en) | 2022-08-09 |
| EP4219702A3 (en) | 2023-11-01 |
| JP2019505204A (ja) | 2019-02-28 |
| EP3397761B1 (en) | 2022-11-09 |
| ZA201803706B (en) | 2019-03-27 |
| US11859221B2 (en) | 2024-01-02 |
| CN119120430A (zh) | 2024-12-13 |
| CN108603185A (zh) | 2018-09-28 |
| JP2025013842A (ja) | 2025-01-28 |
| US20220364068A1 (en) | 2022-11-17 |
| MX2023001119A (es) | 2023-02-22 |
| EP4219702A2 (en) | 2023-08-02 |
| US20180371441A1 (en) | 2018-12-27 |
| EP3397761A1 (en) | 2018-11-07 |
| CN114921442B (zh) | 2024-10-01 |
| MX2018007485A (es) | 2018-08-01 |
| CA3006607A1 (en) | 2017-07-06 |
| JP7626576B2 (ja) | 2025-02-07 |
| US20240093170A1 (en) | 2024-03-21 |
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