Modulation of the thermostability and substrate specificity of Candida rugosa lipase1 by altering the acyl-binding residue Gly414 at the α-helix-connecting bend
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- 作者：Xiaofei Zhanga ; Yong Zhanga ; Guangyu Yanga ; b ; Yuan Xiea ; Lishi Xua ; Jiao Ana ; c ; Li Cuia ; Yan Fenga ; yfeng2009@sjtu.edu.cn" class="auth_mail" title="E-mail the corresponding author
- 关键词：Candida rugosa lipases ; Thermostability ; Substrate specificity ; Saturation mutagenesis ; Bend
- 刊名：Enzyme and Microbial Technology
- 出版年：2016
- 出版时间：January 2016
- 年：2016
- 卷：82
- 期：Complete
- 页码：34-41
- 全文大小：3217 K
文摘
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values of the mutants were increased by 0.5–14 °C compared to that of WT.
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G414W substitution preferred to the short-chain pNP-ester substrates.
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The improved thermostability may be due to the newly formed hydrophobic clusters.
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The additional hydrogen bonds maybe lead to improve thermostability.
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Blocking the tunnel of lipase may limit the hydrolysis of the long-chain substrate.