Covalent immobilization of glucose oxidase onto Poly(St-GMA-NaSS) monodisperse microspheres via BSA as spacer arm

被引：34

作者：

Du, Tanxin ^{[1
,2
]}

Liu, Bailing ^{[1
]}

Hou, Xiaohui ^{[1
,2
]}

Zhang, Baotan ^{[1
,2
]}

Du, Cuiming ^{[1
,2
]}

机构：

[1] Chinese Acad Sci, Chengdu Inst Organ Chem, Chengdu 610041, Peoples R China

[2] Chinese Acad Sci, Grad Sch, Beijing 100039, Peoples R China

来源：

APPLIED SURFACE SCIENCE | 2009年 / 255卷 / 18期

基金：

中国国家自然科学基金;

关键词：

Covalent immobilization; BSA-spacer; Conformational change; Monodisperse microspheres; DISPERSION POLYMERIZATION; TRYPSIN; MODEL; BEADS;

D O I：

10.1016/j.apsusc.2009.04.172

中图分类号：

O64 [物理化学（理论化学）、化学物理学];

学科分类号：

070304 ; 081704 ;

摘要：

In this study, the immobilization of glucose oxidase (GOD) onto micron-size monodisperse Poly(Styrene-Glycidyl Methacrylate-Sodium Sulfonate Styrene) microspheres was investigated. In order to improve their surface biocompatibility, bovine serum albumin (BSA) was introduced onto the microspheres' surface as a new type of spacer arm. Both the immobilization amount and enzymatic activity were determined in different experimental conditions (enzyme concentration, pH, temperature, etc.). It was found that BSA could serve as a good spacer because it increases both the immobilization amount and enzymatic activity of GOD. The tolerance of immobilized GOD against pH, temperatures was examined. Moreover, the kinetic parameters for native and immobilized GOD were obtained and compared. (C) 2009 Elsevier B. V. All rights reserved.

引用

页码：7937 / 7941

页数：5

共 24 条

[1] Immobilization of Candida rugosa lipase onto spacer-arm attached poly(GMA-HEMA-EGDMA) microspheres [J].

Bayramoglu, G ;

Kaya, B ;

Arica, MY .

FOOD CHEMISTRY, 2005, 92 (02) :261-268

[2] Non-isothermal bioreactors in enzymatic remediation of waters polluted by endocrine disruptors: BPA as a model of pollutant [J].

Diano, N. ;

Grano, V. ;

Fraconte, L. ;

Caputo, P. ;

Ricupito, A. ;

Attanasio, A. ;

Bianco, M. ;

Bencivenga, U. ;

Rossi, S. ;

Manco, I. ;

Mita, L. ;

Del Pozzo, G. ;

Mita, D. G. .

APPLIED CATALYSIS B-ENVIRONMENTAL, 2007, 69 (3-4) :252-261

[3] Polymer microspheres for controlled drug release [J].

Freiberg, S ;

Zhu, X .

INTERNATIONAL JOURNAL OF PHARMACEUTICS, 2004, 282 (1-2) :1-18

[4] Detection of polyclonal antibody against any area of the protein-antigen using immobilized protein-antigens:: The critical role of the immobilization protocol [J].

Fuentes, M ;

Mateo, C ;

Fernández-Lafuente, R ;

Guisán, JM .

BIOMACROMOLECULES, 2006, 7 (02) :540-544

[5] Modern analytical approaches to high-throughput drug discovery [J].

Gomez-Hens, A. ;

Aguilar-Caballos, M. P. .

TRAC-TRENDS IN ANALYTICAL CHEMISTRY, 2007, 26 (03) :171-182

[6] Covalent immobilization of glucose oxidase onto poly(styrene-co-glycidyl methacrylate) monodisperse fluorescent microspheres synthesized by dispersion polymerization [J].

Hou, Xiaohui ;

Liu, Bailing ;

Deng, Xiaobo ;

Zhang, Baotan ;

Chen, Hualin ;

Luo, Rong .

ANALYTICAL BIOCHEMISTRY, 2007, 368 (01) :100-110

[7] Functional polymer microspheres [J].

Kawaguchi, H .

PROGRESS IN POLYMER SCIENCE, 2000, 25 (08) :1171-1210

[8] Dispersion polymerization [J].

Kawaguchi, S ;

Ito, K .

POLYMER PARTICLES, 2005, 175 (175) :299-328

[9] Immobilization of trypsin on porous glycidyl methacrylate beads: effects of polymer hydrophilization [J].

Malmsten, M ;

Larsson, A .

COLLOIDS AND SURFACES B-BIOINTERFACES, 2000, 18 (3-4) :277-284

[10] A fluorescence polarization-based screening assay for nucleic acid polymerase elongation activity [J].

Mestas, Santano P. ;

Sholders, Aaron J. ;

Peersen, Olve B. .

ANALYTICAL BIOCHEMISTRY, 2007, 365 (02) :194-200

← 1 2 3 →