Conjugation with inulin improves the environmental stability of haloalkane dehalogenase DhaA
文献类型：期刊论文
| 作者 | Shan, Yue2,3; Yu, Weili2; Shen, Lijuan2; Guo, Xuan1; Zheng, He1; Zhong, Jinyi1; Hu, Tao2; Han, Yinglun3 |
| 刊名 | ENZYME AND MICROBIAL TECHNOLOGY
 |
| 出版日期 | 2021-09-01 |
| 卷号 | 149页码:7 |
| ISSN号 | 0141-0229 |
| 关键词 | Haloalkane dehalogenase DhaA Inulin Conjugation Enzyme stability |
| 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. |
| WOS关键词 | PEGYLATION ; AMYLASE |
| 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 |
| 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.Res Inst Chem Def, State Key Lab NBC Protect Civilian, Beijing 102205, Peoples R China 2.Chinese Acad Sci, Inst Proc Engn, State Key Lab Biochem Engn, Beijing 100190, Peoples R China 3.Liaoning Normal Univ, Coll Life Sci, Dalian 116081, Liaoning, 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. |
入库方式： OAI收割
来源：过程工程研究所
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