Wang et al., 2019 - Google Patents
Simultaneous enhancement of barley β-amylase thermostability and catalytic activity by R115 and T387 residue sites mutationWang et al., 2019
- Document ID
- 2677555171930982423
- Author
- Wang X
- Niu C
- Bao M
- Li Y
- Liu C
- Yun Z
- Li Q
- Wang J
- Publication year
- Publication venue
- Biochemical and Biophysical Research Communications
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Snippet
Objective To simultaneously increase the thermostability and catalytic activity of barley β- amylase. Methods The amino acid sequences of various barley β-amylases with different enzyme properties were aligned, two amino acid residues R115 and T387 were identified to …
- 108010019077 beta-Amylase 0 title abstract description 54
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- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/24—Hydrolases (3) acting on glycosyl compounds (3.2)
- C12N9/2402—Hydrolases (3) acting on glycosyl compounds (3.2) hydrolysing O- and S- glycosyl compounds (3.2.1)
- C12N9/2405—Glucanases
- C12N9/2408—Glucanases acting on alpha -1,4-glucosidic bonds
- C12N9/2411—Amylases
- C12N9/2414—Alpha-amylase (3.2.1.1.)
- C12N9/2417—Alpha-amylase (3.2.1.1.) from microbiological source
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- C12N9/14—Hydrolases (3)
- C12N9/16—Hydrolases (3) acting on ester bonds (3.1)
- C12N9/18—Carboxylic ester hydrolases (3.1.1)
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