Conjugation with inulin improves the environmental stability of haloalkane dehalogenase DhaA

doi:10.1016/j.enzmictec.2021.109832

	Conjugation with inulin improves the environmental stability of haloalkane dehalogenase DhaA
	Shan, Yue 1,2; Yu, Weili 2; Shen, Lijuan 2; Guo, Xuan 3; Zheng, He 3; Zhong, Jinyi 3; Hu, Tao 2; Han, Yinglun 1
刊名	ENZYME AND MICROBIAL TECHNOLOGY
	2021-09-01
卷号	149 页码:7
关键词	Haloalkane dehalogenase DhaA Inulin Conjugation Enzyme stability
ISSN号	0141-0229
DOI	10.1016/j.enzmictec.2021.109832
英文摘要	Haloalkane dehalogenase DhaA catalyzes the hydrolytic cleavage of carbon-halogen bonds and produces alcohol, a proton and a halide. However, DhaA suffers from the poor environmental stability, such as sensitivity to high temperature, low pH, hypersaline and organic solvent. In order to improve the environmental stability of DhaA, DhaA was covalently conjugated with inulin, a hydrophilic polysaccharide in the present study. Each DhaA was averagely conjugated with 7-8 inulin molecules. The conjugated inulin could form a hydration layer around DhaA, which increased the conformational rigidity and decreased the entropy of the enzyme. Conjugation of inulin maintained 75.5 % of the enzymatic activity of DhaA and slightly altered the structure of DhaA. As compared with DhaA, the conjugate (inu-DhaA) showed slightly different kinetic parameters (Km of 2.9 mu mol/L and Kcat of 1.0 s-1). Inulin conjugation could delay the structural unfolding and/or slow the protonation process of DhaA under undesirable environment, including the long-term storage, low pH, hypersaline and organic solvent stability. As a result, the environmental stability of DhaA was markedly increased upon conjugation with inulin. Thus, inulin conjugation was an effective approach to enhance the environmental stability of DhaA.
资助项目	National Natural Science Foundation of China[31970875] ; Natural Science Foundation of Beijing Municipality[M21013] ; National Key Research and Development Project of China[2018YFA0900804]
WOS关键词	PEGYLATION ; AMYLASE
WOS研究方向	Biotechnology & Applied Microbiology
语种	英语
出版者	ELSEVIER SCIENCE INC
WOS记录号	WOS:000681204600004
资助机构	National Natural Science Foundation of China ; Natural Science Foundation of Beijing Municipality ; National Key Research and Development Project of China
内容类型	期刊论文
源URL	[http://ir.ipe.ac.cn/handle/122111/49581]
专题	中国科学院过程工程研究所
通讯作者	Zhong, Jinyi; Hu, Tao; Han, Yinglun
作者单位	1.Liaoning Normal Univ, Coll Life Sci, Dalian 116081, Liaoning, Peoples R China 2.Chinese Acad Sci, Inst Proc Engn, State Key Lab Biochem Engn, Beijing 100190, Peoples R China 3.Res Inst Chem Def, State Key Lab NBC Protect Civilian, Beijing 102205, Peoples R China
推荐引用方式 GB/T 7714	Shan, Yue,Yu, Weili,Shen, Lijuan,et al. Conjugation with inulin improves the environmental stability of haloalkane dehalogenase DhaA[J]. ENZYME AND MICROBIAL TECHNOLOGY,2021,149:7.
APA	Shan, Yue.,Yu, Weili.,Shen, Lijuan.,Guo, Xuan.,Zheng, He.,...&Han, Yinglun.(2021).Conjugation with inulin improves the environmental stability of haloalkane dehalogenase DhaA.ENZYME AND MICROBIAL TECHNOLOGY,149,7.
MLA	Shan, Yue,et al."Conjugation with inulin improves the environmental stability of haloalkane dehalogenase DhaA".ENZYME AND MICROBIAL TECHNOLOGY 149(2021):7.