Surface functionalization of chitosan-coated magnetic nanoparticles for covalent immobilization of yeast alcohol dehydrogenase from Saccharomyces cerevisiae

被引：57

作者：

Li, Gui-yin ^{[1
,2
]}

Zhou, Zhi-de ^{[2
]}

Li, Yuan-jian ^{[1
]}

Huang, Ke-long ^{[3
]}

Zhong, Ming ^{[3
]}

机构：

[1] Cent S Univ, Sch Pharmaceut Sci, Dept Pharmacol, Changsha 410078, Hunan, Peoples R China

[2] Guilin Univ Elect Technol, Biomed Engn Res Ctr, Guilin 541014, Guangxi, Peoples R China

[3] Cent S Univ, Coll Chem & Chem Engn, Changsha 410083, Hunan, Peoples R China

来源：

JOURNAL OF MAGNETISM AND MAGNETIC MATERIALS | 2010年 / 322卷 / 24期

关键词：

Immobilization; Magnetic nanoparticles; Yeast alcohol dehydrogenase; BOVINE SERUM-ALBUMIN; ADSORPTION; STABILITY; AGGREGATION; PROTECTION; PEPTIDE; LIPASE;

D O I：

10.1016/j.jmmm.2010.08.008

中图分类号：

T [工业技术];

学科分类号：

08 ;

摘要：

A novel and efficient immobilization of yeast alcohol dehydrogenase (YADH, EC1.1.1.1) from Saccharomyces cerevisiae has been developed by using the surface functionalization of chitosan-coated magnetic nanoparticles (Fe3O4/KCTS) as support. The magnetic Fe3O4/KCTS nanoparticles were prepared by binding chitosan alpha-ketoglutaric acid (KCTS) on to the surface of magnetic Fe3O4 nanoparticles. Later, covalent immobilization of YADH was attempted onto the Fe3O4/KCTS nanoparticles. The effect of various preparation conditions on the immobilized YADH process such as immobilization time, enzyme concentration and pH was investigated. The influence of pH and temperature on the activity of the free and immobilized YADH using phenylglyoxylic acid as substrate has alsobeenstudied. The optimum reaction temperature and pH value for the enzymatic conversion catalyzed by the immobilized YADH were 30 degrees C and 7.4, respectively. Compared to the free enzyme, the immobilized YADH retained 65% of its original activity and exhibited significant thermal stability and good durability. (C) 2010 Elsevier B.V. All rights reserved.

引用

页码：3862 / 3868

页数：7

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