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Wang et al., 2019 - Google Patents

Simultaneous enhancement of barley β-amylase thermostability and catalytic activity by R115 and T387 residue sites mutation

Wang 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

External Links

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 …
Continue reading at www.sciencedirect.com (other versions)

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    • C12N9/00Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/14Hydrolases (3)
    • C12N9/24Hydrolases (3) acting on glycosyl compounds (3.2)
    • C12N9/2402Hydrolases (3) acting on glycosyl compounds (3.2) hydrolysing O- and S- glycosyl compounds (3.2.1)
    • C12N9/2405Glucanases
    • C12N9/2408Glucanases acting on alpha -1,4-glucosidic bonds
    • C12N9/2411Amylases
    • C12N9/2414Alpha-amylase (3.2.1.1.)
    • C12N9/2417Alpha-amylase (3.2.1.1.) from microbiological source
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