Elucidation of lid open and orientation of lipase activated in interfacial activation by amphiphilic environment

doi:10.1016/j.ijbiomac.2018.07.158

CORC > 上海药物研究所 > 中国科学院上海药物研究所 > 上海中药现代化研究中心

	Elucidation of lid open and orientation of lipase activated in interfacial activation by amphiphilic environment
	Cheng, Cheng 2; Jiang, Tianyue 1; Wu, Yulu 2; Cui, Lupeng 2; Qin, Song 1,3; He, Bingfang 1
刊名	INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
	2018-11
卷号	119 页码:1211-1217
关键词	Lipase Amphiphilic media Interfacial activation
ISSN号	0141-8130
DOI	10.1016/j.ijbiomac.2018.07.158
文献子类	Article
英文摘要	Lipases have wide applications using as biocatalyst in numerous biotechnological and bioengineering fields, especially function at hydrophobic or amphiphilic interface. Previously, the lipase from Burkholderia ambifaria YCJO1 was significantly activated when immobilized on the amphiphilic environment. In this work, insights into the functional effect of amphiphilic surface on lipase activation are presented by molecular dynamic simulations. The notable open of "lid" (alpha 5 region) and the displacement of "flap" region (alpha 8 region) of the lipase are closely related with the activation mechanism of lipase, which makes the active site accessible. Strikingly, the hydrophobic analysis showed that most of the hydrophobic surface residues of lipase, as an interfacial enzyme, located at the "lid" and "flap" regions make the entry to active site naturally orient to the oil-water interface to achieve enzyme activation. Additionally, the analysis of Rg and hydrogen bonding interaction suggested that the amphiphilic environment benefits to the exposure of hydrophobic regions, especially the "lid" and "flap" regions, and the maintenance of the nonpolar environment of the active site. Observations from this work not only complement the activation mechanism of lipase induced by the amphiphilic environment, but also provide a reference for the engineering of immobilized media for interfacial enzyme. (C) 2018 Elsevier B.V. All rights reserved.
资助项目	National Natural Science Foundation of China[81673321] ; National Natural Science Foundation of China[21376119] ; National Natural Science Foundation of China[81503012] ; Natural Science Foundation of Jiangsu Province[BK20150963] ; Natural Science Foundation of Jiangsu Province[BK20151541] ; State Key Laboratory of Drug Research[SIMM1705KF-13] ; Jiangsu Synergetic Innovation Center for Advanced Bio-Manufacture[XTC1812]
WOS关键词	PARTICLE MESH EWALD ; CARBON NANOTUBES ; STATE ; IMMOBILIZATION ; DENATURATION ; CONFORMATION ; SOLVENT ; ENZYMES ; PROTEIN ; PH
WOS研究方向	Biochemistry & Molecular Biology ; Chemistry ; Polymer Science
语种	英语
出版者	ELSEVIER SCIENCE BV
WOS记录号	WOS:000447682100136
内容类型	期刊论文
源URL	[http://119.78.100.183/handle/2S10ELR8/279522]
专题	上海中药现代化研究中心中科院受体结构与功能重点实验室新药研究国家重点实验室
通讯作者	Jiang, Tianyue; He, Bingfang
作者单位	1.Nanjing Tech Univ, Sch Pharmaceut Sci, 30 South Puzhu Rd, Nanjing 211816, Jiangsu, Peoples R China; 2.Nanjing Tech Univ, Sch Biotechnol & Pharmaceut Engn, 30 South Puzhu Rd, Nanjing 211816, Jiangsu, Peoples R China; 3.Chinese Acad Sci, Shanghai Inst Mat Med, State Key Lab Drug Res, Beijing, Peoples R China
推荐引用方式 GB/T 7714	Cheng, Cheng,Jiang, Tianyue,Wu, Yulu,et al. Elucidation of lid open and orientation of lipase activated in interfacial activation by amphiphilic environment[J]. INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES,2018,119:1211-1217.
APA	Cheng, Cheng,Jiang, Tianyue,Wu, Yulu,Cui, Lupeng,Qin, Song,&He, Bingfang.(2018).Elucidation of lid open and orientation of lipase activated in interfacial activation by amphiphilic environment.INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES,119,1211-1217.
MLA	Cheng, Cheng,et al."Elucidation of lid open and orientation of lipase activated in interfacial activation by amphiphilic environment".INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES 119(2018):1211-1217.