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Engineering lipases for temperature adaptation: Structure function correlation.
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics ( IF 3.2 ) Pub Date : 2019-08-08 , DOI: 10.1016/j.bbapap.2019.08.001
Rakesh Kumar 1 , Shelly Goomber 2 , Jagdeep Kaur 3
Affiliation  

Bacillus lipases are industrially attractive enzymes due to their broad substrate specificity and optimum alkaline pH. However, narrow temperature range of action and low thermostability restrain their optimal use and thus, necessitate attention. Several laboratories are engaged in protein engineering of Bacillus lipases to generate variants with improved attributes for decades using techniques such as directed evolution or rational design. This review summarizes the effect of mutations on the conformational changes through in silico modeling and their manifestation with respect to various biochemical parameters. Various studies have been put together to develop a perspective on the molecular basis of biocatalysis of lipases holding industrial importance.

中文翻译:

用于温度适应的工程脂肪酶:结构函数相关。

芽孢杆菌脂肪酶由于其广泛的底物特异性和最佳的碱性pH而成为工业上有吸引力的酶。但是,作用温度范围窄和热稳定性差限制了它们的最佳使用,因此需要引起注意。数十年来,使用定向进化或合理设计等技术从事芽孢杆菌脂肪酶蛋白质工程的研究,以产生具有改良属性的变体。这篇综述总结了突变通过计算机模拟及其在各种生化参数方面的表现对构象变化的影响。已经进行了各种研究以开发具有工业重要性的脂肪酶的生物催化的分子基础。
更新日期:2019-11-01
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