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Updated: Sep 18, 2025

A New Screening Method for the Directed Evolution of Thermostable Bacteriolytic Enzymes
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A New Screening Method for the Directed Evolution of Thermostable Bacteriolytic Enzymes

Published on: November 7, 2012

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来自Thermococcus sibiricus的高热性L-阿斯巴拉金酶及其双重突变的增加活性:对基质特异性和结构的洞察

Maria V Dumina1, Dmitry D Zhdanov2, Alexander V Veselovsky2

  • 1Federal Research Center "Fundamentals of Biotechnology" of the Russian Academy of Sciences, Moscow 117312, Russia.

International journal of molecular sciences
|June 26, 2025
PubMed
概括

这项研究揭示,来自Thermococcus sibiricus的高热友性L-asparaginase (L-ASNase) 的突变增强了其活性并改变了基质特异性,为改善生物技术应用提供了潜在的潜力.

关键词:
在L-asparaginase的使用中.超热友性酶高热友性酶的使用立体选择性的立体选择性.基质特异性 基质特异性热-L-阿斯巴拉金酶结构

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