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Structural Insights into a Novel Esterase from the East Pacific Rise and Its Improved Thermostability by a Semirational Design

文献类型： 外文期刊

作者： Zhu, Chunhua 1 ; Chen, Yayu 4 ; Isupov, Michail N. 5 ; Littlechild, Jennifer A. 5 ; Sun, Lifang 4 ; Liu, Xiaodong 6 ;

作者机构： 1.Chinese Acad Sci, Fujian Inst Res Struct Matter, State Key Lab Struct Chem, Fuzhou 350002, Peoples R China

2.Univ Chinese Acad Sci, Beijing 100049, Peoples R China

3.Fujian Acad Agr Sci, Inst Anim Husb & Vet Med, Fuzhou 350013, Peoples R China

4.Fujian Normal Univ, Prov Univ Key Lab Cellular Stress Response & Meta, Coll Life Sci, Fuzhou 350117, Peoples R China

5.Univ Exeter, Henry Wellcome Bldg Biocatalysis Biosci, Exeter EX4 4QD, Devon, England

6.Fujian Acad Agr Sci, Inst Biotechnol, Fuzhou 350003, Peoples R China

7.Fujian Normal Univ, Coll Life Sci, Fuzhou 350117, Peoples R China

关键词： carboxyl esterase; structure; semirational design; thermostability; B-factor analysis; site-directed mutagenesis

期刊名称：JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY （ 影响因子：5.279； 五年影响因子：5.269 ）

ISSN： 0021-8561

年卷期： 2021 年 69 卷 3 期

页码：

收录情况： SCI

摘要： Lipolytic enzymes are essential biocatalysts in food processing as well as pharmaceutical and pesticide industries, catalyzing the cleavage of ester bonds in a variety of acyl chain substrates. Here, we report the crystal structure of an esterase from the deep-sea hydrothermal vent of the East Pacific Rise (EprEst). The X-ray structure of EprEst in complex with the ligand, acetate, has been determined at 2.03 angstrom resolution. The structure reveals a unique spatial arrangement and orientation of the helix cap domain and alpha/beta hydrolase domain, which form a substrate pocket with preference for short-chain acyl groups. Molecular docking analysis further demonstrated that the active site pocket could accommodate p-nitrophenyl (pNP) carboxyl ligands of varying lengths (<= 6 C atoms), with pNP-butyrate ester predicted to have the highest binding affinity. Additionally, the semirational design was conducted to improve the thermostability of EprEst by enzyme engineering based on the established structure and multiple sequence alignment. A mutation, K114P, introduced in the hinge region of the esterase, which displayed increased thermostability and enzyme activity. Collectively, the structural and functional data obtained herein could be used as basis for further protein engineering to ultimately expand the scope of industrial applications of marine-derived lipolytic enzymes.

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