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CN118421723B - Method for synthesizing R-type vitronectin by enzyme catalysis and application thereof - Google Patents

Method for synthesizing R-type vitronectin by enzyme catalysis and application thereof Download PDF

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CN118421723B
CN118421723B CN202410896630.5A CN202410896630A CN118421723B CN 118421723 B CN118421723 B CN 118421723B CN 202410896630 A CN202410896630 A CN 202410896630A CN 118421723 B CN118421723 B CN 118421723B
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carbonyl reductase
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glucose dehydrogenase
vitronectin
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CN118421723A (en
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袁强
郭帅印
随宝东
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Shandong Juntai Pharmaceutical Co ltd
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    • C12Y101/01184—Carbonyl reductase (NADPH) (1.1.1.184)
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Abstract

The invention belongs to the technical fields of enzyme engineering and biological medicine, and particularly relates to a method for synthesizing R-type vitronectin by enzyme catalysis and application thereof. Specifically, the method for synthesizing the R-type vitronectin by enzyme catalysis comprises the following steps: carbonyl reductase is used as catalytic enzyme, and a substrate and oxidized coenzyme are added to perform enzyme catalytic reaction on the substrate, so that R-type vitronectin is obtained. Researches show that the carbonyl reductase source slow rooting tumor bacteria can efficiently catalyze and synthesize a glass color factor product with a single R configuration, has the advantages of mild reaction conditions, short reaction time, high yield and the like, is very suitable for industrial scale production, and has good practical application value.

Description

Method for synthesizing R-type vitronectin by enzyme catalysis and application thereof
Technical Field
The invention belongs to the technical fields of enzyme engineering and biological medicine, and particularly relates to a method for synthesizing R-type vitronectin by enzyme catalysis and application thereof.
Background
At present, the method for synthesizing the glass color factor is mainly synthesized by a chemical method, but the glass color factor synthesized by the chemical method is difficult to obtain a specific R configuration, in addition, the chemical method synthesis process often needs to use dangerous reagents such as sodium borohydride, lithium aluminum hydride, catalytic hydrogenation and the like and complex processes, so that the cost is greatly improved, and no patent report for synthesizing the single R-type glass color factor by the chemical method exists. Therefore, the high-efficiency and specificity synthesis of the R-type vitriol by utilizing the enzyme protein catalysis has the advantages of mild catalysis conditions and simple process, and accords with the concept of green chemical industry.
The Chinese patent publication No. CN 116904543B discloses a method for preparing R-type vitronectin by using dehydrogenase. In addition, patent publication numbers CN 113717997A and CN 115896199A and the like both refer to methods for synthesizing S-type vitriol by a chemical enzyme method, but the inventor researches have found that the methods still have the defects of overlong reaction time, still to improve the conversion rate and the like.
Disclosure of Invention
Aiming at the defects of the prior art, the invention aims to provide a method for synthesizing R-type vitronectin by enzyme catalysis and application thereof. Specifically, the carbonyl reductase BsKRED from the bradyrhizobium is researched, and experiments prove that the carbonyl reductase BsKRED can be used for efficiently catalyzing and synthesizing the vitronectin product with a single R configuration, has the advantages of short reaction time, few byproducts, high purity and the like, and is suitable for large-scale industrial production. Based on the above results, the present invention has been completed.
In order to achieve the technical purpose, the technical scheme provided by the invention is as follows:
in a first aspect of the present invention, there is provided a method for the enzymatic synthesis of R-type vitronectin, said method comprising: carbonyl reductase is used as catalytic enzyme, and substrate beta-acetonylxyloside and oxidized coenzyme are added to perform enzyme catalytic reaction on the substrate, so that R-type vitronectin is obtained.
The reaction system also contains glucose dehydrogenase, and further, the carbonyl reductase and the glucose dehydrogenase can be obtained by fermenting and culturing the same engineering bacteria; the specific method comprises the following steps: the carbonyl reductase encoding gene and the glucose dehydrogenase encoding gene are inserted into the same plasmid vector, and the plasmid vector is introduced into host bacteria.
In a second aspect of the invention, there is provided the use of the above method for the industrial production of R-type vitreous color factor.
The beneficial technical effects of one or more of the technical schemes are as follows:
The carbonyl reductase can be obtained by first screening, can be used for efficiently catalyzing and synthesizing the vitronectin product with a single R configuration, has the advantages of mild reaction conditions, short reaction time, high yield and the like, and is very suitable for industrial scale production, so that the carbonyl reductase has good practical application value.
Drawings
FIG. 1 is a diagram of a recombinant vector according to an embodiment of the present invention.
FIG. 2 is a chromatogram of an enzyme-catalyzed preparation of R-type vitreogene in an embodiment of the invention.
Detailed Description
It is noted that the terminology used herein is for the purpose of describing particular embodiments only and is not intended to be limiting of exemplary embodiments according to the present invention. As used herein, the singular is also intended to include the plural unless the context clearly indicates otherwise, and furthermore, it is to be understood that the terms "comprises" and/or "comprising" when used in this specification are taken to specify the presence of stated features, steps, operations, devices, components, and/or combinations thereof.
The invention will now be further illustrated with reference to specific examples, which are given for the purpose of illustration only and are not intended to be limiting in any way. If experimental details are not specified in the examples, it is usually the case that the conditions are conventional or recommended by the reagent company; reagents, consumables, etc. used in the examples described below are commercially available unless otherwise specified.
In an exemplary embodiment of the present invention, there is provided a method for enzymatically synthesizing R-type vitronectin, the method comprising: carbonyl reductase is used as catalytic enzyme, and substrate beta-acetonylxyloside and oxidized coenzyme are added to perform enzyme catalytic reaction on the substrate, so that R-type vitronectin is obtained.
Wherein the concentration of the substrate beta-acetonylxyloside is 180 g/L-210 g/L, and more preferably 195g/L;
The oxidized coenzyme II can be oxidized coenzyme II, namely NADP +, and in the reaction system, the concentration of the oxidized coenzyme II is controlled to be 1-2 g/L, and more preferably 1.5g/L;
The carbonyl reductase is specifically carbonyl reductase BsKRED, and NCBI accession number of the carbonyl reductase is ABQ37878.1; specifically, the carbonyl reductase can be obtained by fermenting and culturing engineering bacteria containing the carbonyl reductase coding gene.
Wherein, the carbonyl reductase coding gene is shown in SEQ ID NO. 2.
More specifically, the reaction conditions are: the reaction is carried out at 25-35 ℃ for 4-6 hours, more preferably at 30 ℃ for 5 hours.
Further, the reaction system further comprises Mg 2+, wherein the concentration of Mg 2+ is controlled to be 10-40 mM, preferably 20mM.
Furthermore, the reaction system also contains glucose dehydrogenase, wherein the glucose dehydrogenase is BmGDH-M6, and the amino acid sequence and the nucleotide sequence of the glucose dehydrogenase are respectively shown as SEQ ID NO.3 and SEQ ID NO. 4. The glucose dehydrogenase may be obtained by fermentation culture of an engineering bacterium containing a gene encoding the glucose dehydrogenase.
Furthermore, the carbonyl reductase and the glucose dehydrogenase can be obtained by fermenting and culturing the same engineering bacteria; the specific method comprises the following steps: the carbonyl reductase encoding gene and the glucose dehydrogenase encoding gene are inserted into the same plasmid vector, and the plasmid vector is introduced into host bacteria.
The plasmid vector can be pETduent-1, and the host bacterium can be escherichia coli BL21 (DE 3);
Further, the carbonyl reductase-encoding gene was inserted between NcoI and NotI in the multiple cloning site MCS1 of plasmid vector pETduent-1, and the glucose dehydrogenase-encoding gene was inserted between NdeI and XhoI in the multiple cloning site MCS2 of plasmid vector pETduent-1.
In yet another embodiment of the present invention, there is provided the use of the above method for the industrial production of R-vitronectin.
The invention is further illustrated by the following examples, which are not to be construed as limiting the invention. It is to be understood that these examples are illustrative of the present invention and are not intended to limit the scope of the present invention. The following examples are test methods in which specific conditions are noted, and are generally conducted under conventional conditions.
Examples
1. Recombinant vector construction
The carbonyl reductase is derived from a slow rooting tumor bacterium, NCBI accession number is ABQ37878.1, the enzyme protein sequence is named BsKRED, the nucleotide sequence of the enzyme protein is subjected to codon optimization by Shanghai bioengineering (the optimized nucleotide sequence is shown as SEQ ID NO. 2), the enzyme protein is constructed to enter between NcoI and NotI in a multiple cloning site MCS1 of a vector pETduent-1, meanwhile, a glucose dehydrogenase gene BmGDH-M6 (the amino acid sequence and the nucleotide sequence of the enzyme protein are respectively shown as SEQ ID NO.3 and SEQ ID NO. 4) is also synthesized by Shanghai bioengineering and inserted between NdeI and XhoI in a multiple cloning site MCS2 of the vector pETduent-1, and the map of the final recombinant vector is shown as figure 1.
2. Preparation of crude enzyme solution
The recombinant vector is transferred into escherichia coli BL21 (DE 3) to be competent by a chemical conversion method, the escherichia coli BL21 (DE 3) is purchased from Shanghai Weidi organism, the product number is EC1002, the chemical conversion is carried out according to the specification requirements provided by a official network, finally, a solid LB plate containing ampicillin resistance is coated, and the solid LB plate is cultured at 37 ℃ overnight in a constant temperature incubator. The monoclonal was picked up into 50mL small shake flasks with 20mL LB medium and incubated at 37℃on a shaker at 220r for 12h. Transferring the small shake flask culture according to the inoculation amount of 1% to a shake flask with 100mL TB medium, culturing for 4h at 37 ℃ under 220r, monitoring OD 600,OD600 to 0.6-0.8 in the culturing process, adding IPTG to induce the culture to the final concentration of 1mM, and culturing for 12h at 220r under 25 ℃ of a shaking table. The cells were collected by centrifugation and weighed to obtain the wet weight of E.coli cells, which were resuspended by adding 10mL of phosphate buffer according to 1g of wet weight of cells, followed by sonication. Ultrasonic crushing parameters with power of 300W, ultrasonic treatment for 10s and interval of 10s, total ultrasonic treatment time of 15min, ultrasonic crushing process all operation on ice, and final centrifugal degerming of residues at 4deg.C and 12000r to obtain crude enzyme solution.
3. Establishing a reaction system
In this reaction system, 3g of wet cells were crushed and all put into a 100mL reaction system to participate in the reaction, the substrate beta-acetoxyloside concentration was 195g/L, the NADP + concentration was 1.5g/L, the MgCl 2 concentration was 20mM, the reaction time was 5 hours, and the conversion was 97.6%, as shown in FIG. 2.
Amino acid and nucleotide sequence information presented in the examples:
carbonyl reductase BsKRED amino acid sequence:
MLPVVACAAMLELRLPPVIAPIQDSAHCRAVIQRAVDELGGIDILVNNAAHQATFSEIGDISDDEWEMTFRTNIHAMFYLTKAAVPHMKPGSAIVNTASVNSDMPNPSLLAYATTKGAIQNFTGGLAQMLADKGIRANAVAPGPIWTPLIPSTMPEEKVTSFGQQVPMKRAGQPAELATAYVMLADPLSSYTSGTTVAVTGGKPFI（SEQ ID NO.1）
Carbonyl reductase BsKRED coding gene sequence:
ATGCTGCCTGTCGTTGCTTGCGCCGCAATGCTGGAACTGCGCCTGCCGCCAGTGATTGCCCCAATCCAGGACTCTGCGCACTGCCGTGCAGTTATCCAGCGTGCAGTGGATGAACTGGGCGGTATCGACATTCTGGTGAACAACGCAGCCCACCAGGCAACCTTCTCTGAAATCGGCGATATCTCCGACGATGAATGGGAAATGACCTTCCGTACCAACATCCACGCTATGTTCTACCTGACTAAAGCCGCTGTGCCGCACATGAAACCGGGCAGCGCCATCGTTAACACTGCGAGCGTTAACTCTGATATGCCAAACCCGTCCCTGCTGGCTTATGCAACTACGAAAGGTGCCATCCAGAACTTCACCGGTGGCCTGGCACAGATGCTGGCTGACAAAGGCATCCGTGCTAACGCAGTAGCTCCGGGTCCGATCTGGACTCCGCTGATCCCTAGCACCATGCCTGAGGAAAAAGTAACCAGCTTCGGTCAGCAGGTCCCGATGAAACGCGCTGGTCAGCCTGCTGAACTGGCTACGGCGTACGTCATGCTGGCTGACCCGCTGAGCTCTTACACTTCTGGTACTACCGTCGCAGTGACGGGTGGTAAACCGTTCATC（SEQ ID NO.2）
glucose dehydrogenase BmGDH-M6 amino acid sequence:
MAHHHHHHMYKDLEGKVVVITGSSTGLGKSMAIRFATEKAKVVVNYRSKEDEANSVLEEIKKVGGEAIAVKGDVTVESDIINLVQSAIKEFGKLDVMINNAGLENPVPSHEMSLSDWNKVIDTNLTGAFLGSREAIKYFVENDIRGTVINMSSVHEKIPWPLFVHYAASKGGMRLMTKTLALEYAPKGIRVNNIGPGAINTPINAEKFADPEQRADVESMIPMGYIGEPEEIAAVAAWLASSEASYVTGITLFADGGMTLYPSFQAGRG（SEQ ID NO.3）
glucose dehydrogenase BmGDH-M6 coding gene sequence:
ATGGCGCATCACCACCACCACCACATGTATAAAGATCTGGAAGGTAAAGTTGTTGTTATCACCGGCTCTTCTACCGGCCTGGGTAAATCTATGGCGATCCGTTTCGCGACCGAAAAAGCGAAAGTTGTTGTGAACTACCGTAGCAAAGAAGATGAAGCGAACAGCGTTCTGGAAGAAATCAAAAAAGTTGGTGGTGAAGCGATCGCGGTTAAAGGCGATGTTACCGTTGAATCTGATATCATCAACCTGGTTCAGAGCGCGATCAAAGAATTCGGTAAACTGGATGTTATGATCAACAACGCAGGCCTGGAAAACCCGGTTCCGTCCCACGAAATGTCTCTGTCTGATTGGAACAAAGTTATCGATACCAACCTGACCGGTGCATTCCTGGGTTCTCGTGAAGCTATCAAATATTTCGTTGAAAACGATATCCGTGGTACCGTTATCAACATGAGCAGCGTTCATGAAAAAATTCCGTGGCCGCTGTTCGTTCACTATGCGGCGTCTAAAGGCGGCATGCGTCTGATGACCAAAACCCTGGCGCTGGAATATGCGCCGAAAGGTATCCGTGTTAACAACATCGGTCCGGGCGCGATTAACACCCCGATCAACGCTGAAAAATTCGCTGATCCGGAACAGCGTGCTGATGTTGAAAGCATGATCCCGATGGGCTACATTGGCGAACCGGAAGAAATCGCGGCGGTTGCAGCGTGGCTGGCGAGCTCTGAAGCTTCTTACGTTACCGGTATCACCCTGTTCGCTGATGGTGGTATGACCCTGTACCCGTCTTTCCAGGCGGGCCGTGGTTAA（SEQ ID NO.4）
the invention is not a matter of the known technology.
Finally, it should be noted that: the foregoing description is only a preferred embodiment of the present invention, and is not intended to limit the present invention, but although the present invention has been described in detail with reference to the foregoing embodiment, it will be apparent to those skilled in the art that modifications may be made to the technical solution described in the foregoing embodiment, or equivalents may be substituted for some of the technical features thereof. Any modification, equivalent replacement, improvement, etc. made within the spirit and principle of the present invention should be included in the protection scope of the present invention.

Claims (9)

1. A method for synthesizing R-type vitronectin by enzyme catalysis, which is characterized by comprising the following steps: taking carbonyl reductase as catalytic enzyme, adding substrate beta-acetonylxyloside and oxidized coenzyme to perform enzyme catalytic reaction on the substrate to obtain R-type vitronectin;
The carbonyl reductase is carbonyl reductase BsKRED, and NCBI accession number of the carbonyl reductase is ABQ37878.1;
the oxidized coenzyme is oxidized coenzyme II;
The reaction system also contains Mg 2+.
2. The method of claim 1, wherein the substrate β -acetonylxyloside is present at a concentration of 180g/L to 210g/L.
3. The method according to claim 1, wherein the concentration of oxidized coenzyme II is controlled to 1 to 2g/L.
4. The method according to claim 1, wherein the carbonyl reductase is obtained by fermentation culture of an engineering bacterium containing a gene encoding the carbonyl reductase; wherein, the carbonyl reductase coding gene is shown in SEQ ID NO. 2.
5. The method of claim 1, wherein the conditions of the enzyme-catalyzed reaction are: reacting for 4-6 hours at the temperature of 25-35 ℃.
6. The method of claim 1, wherein the Mg 2+ concentration is controlled to be 10-40 mm.
7. The method of claim 1, wherein the reaction system further comprises glucose dehydrogenase, wherein the glucose dehydrogenase is BmGDH-M6, and the amino acid sequence and the nucleotide sequence of the glucose dehydrogenase are shown as SEQ ID NO.3 and SEQ ID NO.4 respectively; the glucose dehydrogenase is obtained by fermenting and culturing engineering bacteria containing a glucose dehydrogenase encoding gene.
8. The method of claim 7, wherein the carbonyl reductase and glucose dehydrogenase are obtained by fermentation culture of the same engineering bacterium;
the method comprises the following steps: inserting the carbonyl reductase encoding gene and the glucose dehydrogenase encoding gene into the same plasmid vector, and introducing the plasmid vector into host bacteria;
Wherein the plasmid vector is pETduent-1, and the host bacterium is escherichia coli BL21 (DE 3);
The carbonyl reductase encoding gene is inserted between NcoI and NotI in the multiple cloning site MCS1 of the plasmid vector pETduent-1, and the glucose dehydrogenase encoding gene is inserted between NdeI and XhoI in the multiple cloning site MCS2 of the plasmid vector pETduent-1.
9. Use of the method according to any one of claims 1-8 for the industrial production of R-type vitronectin.
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CN118109431A (en) * 2024-03-24 2024-05-31 上海微理智成生物技术有限公司 Carbonyl reductase for synthesizing R-vitronectin, and preparation method and application thereof

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WO2008013996A2 (en) * 2006-07-27 2008-01-31 Gevo Inc. Engineered microorganisms for increasing product yield in biotransformations, related methods and systems
CN113717997B (en) * 2021-11-04 2022-02-08 深圳瑞德林生物技术有限公司 Enzyme composition and method for synthesizing vitronectin by chemical enzyme method
CN116904543B (en) * 2023-09-07 2023-11-21 云合(天津)生物技术有限公司 Application of dehydrogenase in synthesis of R-configuration vitronectin and synthesis method
CN117535256A (en) * 2023-11-16 2024-02-09 上海微理智成生物技术有限公司 Carbonyl reductase and application thereof in synthesis of vitronectin
CN118028257A (en) * 2024-02-08 2024-05-14 杭州海普沃辉生物医药有限公司 Mutant carbonyl reductase and application thereof in synthesis of (R) -configuration vitronectin

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CN118109431A (en) * 2024-03-24 2024-05-31 上海微理智成生物技术有限公司 Carbonyl reductase for synthesizing R-vitronectin, and preparation method and application thereof

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