Thermostability Improvement of L-Asparaginase from <i>Acinetobacter soli</i> via Consensus-Designed Cysteine Residue Substitution

Thermostability Improvement of L-Asparaginase from <i>Acinetobacter soli</i> via Consensus-Designed Cysteine Residue Substitution

To extend the application range of L-asparaginase in food pre-processing, the thermostability improvement of the enzyme is essential. Herein, two non-conserved cysteine residues with easily oxidized free sulfhydryl groups, Cys8 and Cys283, of <i>Acinetobacter soli</i> L-asparaginase (AsA...

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Bibliographic Details
Main Authors: Linshu Jiao, Huibing Chi, Bingjie Xia, Zhaoxin Lu, Xiaomei Bie, Haizhen Zhao, Fengxia Lu, Meirong Chen
Format: Article
Language:English
Published: MDPI AG 2022-10-01
Series:Molecules
Subjects:
L-asparaginase
<i>Acinetobacter soli</i>
thermostability
consensus design
cysteine substitution
acrylamide inhibition
Online Access:https://www.mdpi.com/1420-3049/27/19/6670

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