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Recent advances in the improvement of enzyme thermostability by structure modification
Critical Reviews in Biotechnology ( IF 9 ) Pub Date : 2019-11-05 , DOI: 10.1080/07388551.2019.1682963
Zhe Xu 1, 2 , Yu-Ke Cen 1, 2 , Shu-Ping Zou 1, 2 , Ya-Ping Xue 1, 2 , Yu-Guo Zheng 1, 2
Affiliation  

Thermostability is considered to be an important parameter to measure the feasibility of enzymes for industrial applications. Generally, higher thermostability makes an enzyme more competitive and desirable in industry. However, most natural enzymes show poor thermostability, which restricts their application. Protein structure modification is a desirable method to improve enzyme properties. In recent years, tremendous progress has been achieved in protein thermostability engineering. In this review, we provide a systemic overview on the approaches of protein structure modification for the improvement of enzyme thermostability during the last decade. Structure modification approaches, including the introduction of non-covalent interactions and covalent bonds, increase of proline and/or decrease in glycine, reinforcement of subunit–subunit interactions, introduction of glycosylation sites, truncation and cyclization have been highlighted.



中文翻译:

通过结构修饰改善酶热稳定性的最新进展

热稳定性被认为是衡量酶在工业应用中可行性的重要参数。通常,较高的热稳定性使酶在工业中更具竞争力和理想性。然而,大多数天然酶显示出差的热稳定性,这限制了它们的应用。蛋白质结构修饰是改善酶性质的理想方法。近年来,蛋白质热稳定性工程学已经取得了巨大的进步。在这篇综述中,我们提供了有关蛋白质结构修饰方法的系统综述,以改善过去十年中酶的热稳定性。结构修饰方法,包括引入非共价相互作用和共价键,脯氨酸增加和/或甘氨酸减少,

更新日期:2019-11-06
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