Protein Immobilization in Metal-Organic Frameworks by Covalent Binding

被引：36
|
作者：
Wang, Xuan [1 ]
Makal, Trevor A. [2 ]
Zhou, Hong-Cai [1 ]
机构：
[1] Texas A&M Univ, Dept Chem, College Stn, TX 77843 USA
[2] Univ Virginias Coll Wise, Dept Nat Sci, Wise, VA 24293 USA
来源：
AUSTRALIAN JOURNAL OF CHEMISTRY | 2014年 / 67卷 / 11期
关键词：
INORGANIC POROUS MATERIALS; BIOCATALYSIS; MOF;
D O I：
10.1071/CH14104
中图分类号：
O6 [化学];
学科分类号：
0703 ;
摘要：
Metal-organic frameworks (MOFs), possessing a well defined system of pores, demonstrate extensive potential serving as a platform in biological catalysis. Successful immobilization of enzymes in a MOF system retains the enzymatic activity, renders the active site more accessible to the substrate, and promises recyclability for reuse, and solvent adaptability in a broad range of working conditions. This highlight describes enzyme immobilization on MOFs via covalent binding and its significance.
引用
收藏
页码：1629 / 1631
页数：3
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