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Conjugation with inulin improves the environmental stability of haloalkane dehalogenase DhaA
Shan, Yue1,2; Yu, Weili2; Shen, Lijuan2; Guo, Xuan3; Zheng, He3; Zhong, Jinyi3; Hu, Tao2; Han, Yinglun1
2021-09-01
Source PublicationENZYME AND MICROBIAL TECHNOLOGY
ISSN0141-0229
Volume149Pages:7
AbstractHaloalkane 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.
KeywordHaloalkane dehalogenase DhaA Inulin Conjugation Enzyme stability
DOI10.1016/j.enzmictec.2021.109832
Language英语
WOS KeywordPEGYLATION ; AMYLASE
Funding ProjectNational Natural Science Foundation of China[31970875] ; Natural Science Foundation of Beijing Municipality[M21013] ; National Key Research and Development Project of China[2018YFA0900804]
WOS Research AreaBiotechnology & Applied Microbiology
WOS SubjectBiotechnology & Applied Microbiology
Funding OrganizationNational Natural Science Foundation of China ; Natural Science Foundation of Beijing Municipality ; National Key Research and Development Project of China
WOS IDWOS:000681204600004
PublisherELSEVIER SCIENCE INC
Citation statistics
Document Type期刊论文
Identifierhttp://ir.ipe.ac.cn/handle/122111/49582
Collection中国科学院过程工程研究所
Corresponding AuthorZhong, Jinyi; Hu, Tao; Han, Yinglun
Affiliation1.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
Recommended Citation
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.
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