The immobilization of penicillin G acylase on modified TiO2 with various micro-environments

doi:10.1016/j.colsurfa.2021.126316

	The immobilization of penicillin G acylase on modified TiO2 with various micro-environments
	Liu, Chunli 4,5; Wang, Xudong 4,5; Chen, Zhenbin 4,5; Zhou, Yongshan 4,5; Ruso, Juan M 6; Hu, Dongdong 3; Liu, Zhen 2; Liao, Yiliang 1
刊名	Colloids and Surfaces A: Physicochemical and Engineering Aspects
	2021-05-05
卷号	616
关键词	Drug products Enzyme activity Oxide minerals Titanium dioxide 3-aminopropyltriethoxysilane 3-Glycidoxypropyltrimethoxysilane Catalytic performance Glutaraldehydes Microenvironments Modification process Penicillin G Acylase Retention ratio
ISSN号	0927-7757
DOI	10.1016/j.colsurfa.2021.126316
英文摘要	Immobilization of penicillin G acylase (PGA) on carriers is an effective strategy for running away from the drawbacks of free PGA. In this work, modified TiO2 was employed as a carrier for the immobilization of PGA. Firstly, TiO2 was used as a nucleus and modified by two different approaches, one-step modification and two-step modification, to construct and regulate the micro-environment of carrier, particularly by changing the type of functional immobilization groups, and the arm-length of immobilization sites. In the one-step modification approach, TiO2 was altered by glutaraldehyde, 3-glycidoxypropyltrimethoxysilane (3-GCDPTMS) and 3-aminopropyltriethoxysilane (3-APTMS), separately; while in the two-step modification approach, primary TiO2 was firstly altered with a small amount of glutaraldehyde or 3-GCDPTMS, then followed by a secondary modification process using glutaraldehyde and 3-GCDPTMS, respectively. Secondly, the influence of the micro-environments of carrier on the catalytic performance of immobilized PGA, in terms of enzyme loading capacity (ELC), enzyme activity (EA) and activity retention ratio (EAR) was investigated. Results revealed that PGA immobilized on carrier modified by 3-GCDPTMS, with a graft rate of 30 % had the best performance, which had an ELC of 10,800 U, EA of 14,900 U/g. Both of the functional group and arm-length of immobilization site had influence on the catalytic performance of immobilized PGA, and the functional groups of immobilization site was the most essential one responsible for stabilizing PGA and improving its catalytic activity. Then PGA immobilized carrier with longer arm-length had better catalytic performance. © 2021 Elsevier B.V.
WOS研究方向	Chemistry
语种	英语
出版者	Elsevier B.V.
WOS记录号	WOS:000635444000003
内容类型	期刊论文
源URL	[http://ir.lut.edu.cn/handle/2XXMBERH/147703]
专题	材料科学与工程学院
作者单位	1.Department of Industrial and Manufacturing Systems Engineering, Iowa State University, Ames; IA; 50011, United States; 2.Department of Physics and Engineering, Frostburg State University, MD; 21532, United States 3.State Key Laboratory of Chemical Engineering, East China University of Science and Technology, Shanghai, China; 4.State Key Laboratory of Gansu Advanced Non-ferrous Metal Materials, Lanzhou University of Technology, Lanzhou; Gansu; 730050, China; 5.School of Material Science and Engineering, Lanzhou University of Technology, Lanzhou; Gansu; 730050, China; 6.Soft Matter and Molecular Biophysics Group, Department of Applied Physics, University of Santiago de Compostela, Santiago de Compostela; 15782, Spain;
推荐引用方式 GB/T 7714	Liu, Chunli,Wang, Xudong,Chen, Zhenbin,et al. The immobilization of penicillin G acylase on modified TiO2 with various micro-environments[J]. Colloids and Surfaces A: Physicochemical and Engineering Aspects,2021,616.
APA	Liu, Chunli.,Wang, Xudong.,Chen, Zhenbin.,Zhou, Yongshan.,Ruso, Juan M.,...&Liao, Yiliang.(2021).The immobilization of penicillin G acylase on modified TiO2 with various micro-environments.Colloids and Surfaces A: Physicochemical and Engineering Aspects,616.
MLA	Liu, Chunli,et al."The immobilization of penicillin G acylase on modified TiO2 with various micro-environments".Colloids and Surfaces A: Physicochemical and Engineering Aspects 616(2021).