Efficient and stable enzyme immobilization in a block copolypeptide vesicle-templated biomimetic silica support

被引：42

作者：

Lai, Jun-Kun ^{[1
]}

Chuang, Tzu-Han ^{[2
]}

Jan, Jeng-Shiung ^{[2
]}

Wang, Steven Sheng-Shih ^{[1
]}

机构：

[1] Natl Taiwan Univ, Dept Chem Engn, Taipei 10617, Taiwan

[2] Natl Cheng Kung Univ, Dept Chem Engn, Tainan 70101, Taiwan

来源：

COLLOIDS AND SURFACES B-BIOINTERFACES | 2010年 / 80卷 / 01期

关键词：

Enzyme immobilization; Biomimetic; Block copolypeptide; Nanocomposites; Silica; PAPAIN; COAGGREGATION; NANOPARTICLES; ENCAPSULATION; ENTRAPMENT; CHEMISTRY;

D O I：

10.1016/j.colsurfb.2010.05.030

中图分类号：

Q6 [生物物理学];

学科分类号：

071011 [生物物理学];

摘要：

We report the immobilization of a model enzyme, papain, within silica matrices by combining vesiclization of poly-L-lysine-b-polyglycine block copolypeptides with following silica mineralization. Our novel strategy utilizes block polypeptide vesicles to induce the condensation of orthosilicic acid while trapping an enzyme within and between vesicles. The polypeptide mediated silica-immobilized enzyme exhibits enhanced pH and thermal stability and reusability, comparing with the free and vesicle encapsulated enzyme. The enhanced enzymatic activity in the immobilized enzyme is due to the confinement of the enzyme in the polypeptide mediated silica matrices. Kinetic analysis shows that the enzyme functionality is determined by the structure and property of silica/polypeptide matrices. The proposed novel strategy provides an alternative route for the synthesis of a broad range of functional bionanocomposites entrapped within silica nanostructures. (c) 2010 Elsevier B.V. All rights reserved.

引用

页码：51 / 58

页数：8

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