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Cloning and Characterization of Chitin Deacetylase from Euphausia superba

文献类型： 外文期刊

作者： Wang, Xutong 1 ; Tan, Jiahao 1 ; Zou, Huaying 1 ; Wang, Fang 2 ; Xu, Jiakun 2 ;

作者机构： 1.Shanghai Ocean Univ, Coll Food Sci & Technol, Shanghai 201306, Peoples R China

2.Chinese Acad Fishery Sci, Yellow Sea Fisheries Res Inst, Lab Marine Drugs & Byproducts, Pilot Natl Lab Marine Sci & Technol,State Key Lab, Qingdao 266071, Peoples R China

3.Minist Agr & Rural Affairs, Key Lab Sustainable Dev Polar Fisheries, Qingdao 266071, Peoples R China

关键词： chitin deacetylase; Euphausia superba; heterologous expression; enzymatic properties; molecular simulation

期刊名称：INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES （ 影响因子：5.6； 五年影响因子：6.2 ）

ISSN： 1661-6596

年卷期： 2024 年 25 卷 4 期

页码：

收录情况： SCI

摘要： Chitin deacetylase (CDA) can catalyze the deacetylation of chitin to produce chitosan. In this study, we identified and characterized a chitin deacetylase gene from Euphausia superba (EsCDA-9k), and a soluble recombinant protein chitin deacetylase from Euphausia superba of molecular weight 45 kDa was cloned, expressed, and purified. The full-length cDNA sequence of EsCDA-9k was 1068 bp long and encoded 355 amino acid residues that contained the typical domain structure of carbohydrate esterase family 4. The predicted three-dimensional structure of EsCDA-9k showed a 67.32% homology with Penaeus monodon. Recombinant chitin deacetylase had the highest activity at 40 degrees C and pH 8.0 in Tris-HCl buffer. The enzyme activity was enhanced by metal ions Co2+, Fe3+, Ca2+, and Na+, while it was inhibited by Zn2+, Ba2+, Mg2+, and EDTA. Molecular simulation of EsCDA-9k was conducted based on sequence alignment and homology modeling. The EsCDA-9k F18G mutant showed a 1.6-fold higher activity than the wild-type enzyme. In summary, this is the first report of the cloning and heterologous expression of the chitin deacetylase gene in Euphausia superba. The characterization and function study of EsCDA-9k will serve as an important reference point for future application.

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