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提高脂肪酶的溶剂耐受性以增强其应用:最新进展。

Solvent Tolerance Improvement of Lipases Enhanced Their Applications: State of the Art.

机构信息

State Key Laboratory of Materials-Oriented Chemical Engineering, School of Pharmaceutical Sciences, Nanjing Tech University, Nanjing 210009, China.

出版信息

Molecules. 2024 May 22;29(11):2444. doi: 10.3390/molecules29112444.

DOI:10.3390/molecules29112444
PMID:38893320
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC11173743/
Abstract

Lipases, crucial catalysts in biochemical synthesis, find extensive applications across industries such as food, medicine, and cosmetics. The efficiency of lipase-catalyzed reactions is significantly influenced by the choice of solvents. Polar organic solvents often result in a decrease, or even loss, of lipase activity. Conversely, nonpolar organic solvents induce excessive rigidity in lipases, thereby affecting their activity. While the advent of new solvents like ionic liquids and deep eutectic solvents has somewhat improved the activity and stability of lipases, it fails to address the fundamental issue of lipases' poor solvent tolerance. Hence, the rational design of lipases for enhanced solvent tolerance can significantly boost their industrial performance. This review provides a comprehensive summary of the structural characteristics and properties of lipases in various solvent systems and emphasizes various strategies of protein engineering for non-aqueous media to improve lipases' solvent tolerance. This study provides a theoretical foundation for further enhancing the solvent tolerance and industrial properties of lipases.

摘要

脂肪酶是生化合成中至关重要的催化剂,在食品、医药和化妆品等多个行业得到广泛应用。脂肪酶催化反应的效率受到溶剂选择的显著影响。极性有机溶剂通常会导致脂肪酶活性降低,甚至丧失。相反,非极性有机溶剂会使脂肪酶过度僵化,从而影响其活性。尽管新型溶剂,如离子液体和深共熔溶剂的出现,在一定程度上提高了脂肪酶的活性和稳定性,但未能解决脂肪酶对溶剂耐受性差的根本问题。因此,合理设计具有增强溶剂耐受性的脂肪酶可以显著提高其工业性能。本综述全面总结了脂肪酶在各种溶剂体系中的结构特征和性质,并强调了蛋白质工程在非水介质中提高脂肪酶溶剂耐受性的各种策略。本研究为进一步提高脂肪酶的溶剂耐受性和工业性能提供了理论基础。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3ea9/11173743/c3d6df98572e/molecules-29-02444-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3ea9/11173743/e0ca26677c2f/molecules-29-02444-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3ea9/11173743/aae00c27c565/molecules-29-02444-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3ea9/11173743/dcece50c2ddb/molecules-29-02444-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3ea9/11173743/c3d6df98572e/molecules-29-02444-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3ea9/11173743/e0ca26677c2f/molecules-29-02444-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3ea9/11173743/aae00c27c565/molecules-29-02444-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3ea9/11173743/dcece50c2ddb/molecules-29-02444-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3ea9/11173743/c3d6df98572e/molecules-29-02444-g004.jpg

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Int J Biol Macromol. 2023 Dec 31;253(Pt 8):127656. doi: 10.1016/j.ijbiomac.2023.127656. Epub 2023 Oct 24.
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Enhancing the Hydrolytic Activity of a Lipase towards Larger Triglycerides through Lid Domain Engineering.
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