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通过交联酶聚集体实现酶的稳定化。

Enzyme stabilization via cross-linked enzyme aggregates.

作者信息

Gupta Munishwar N, Raghava Smita

机构信息

Chemistry Department, Indian Institute of Technology Delhi, Hauz Khas, New Delhi, India.

出版信息

Methods Mol Biol. 2011;679:133-45. doi: 10.1007/978-1-60761-895-9_11.

DOI:10.1007/978-1-60761-895-9_11
PMID:20865393
Abstract

Extensive cross-linking of a precipitate of a protein by a cross-linking reagent (glutaraldehyde has been most commonly used) creates an insoluble enzyme preparation called cross-linked enzyme aggregates (CLEAs). CLEAs show high stability and performance in both conventional aqueous media as well as nonaqueous media. These are also stable at fairly high temperatures. CLEAs having more than one kind of enzyme activity can be prepared and such CLEAs are called combi-CLEAs or multipurpose CLEAs. Extent of cross-linking often influences their morphology, stability, activity, and enantioselectivity.

摘要

通过交联剂(最常用的是戊二醛)对蛋白质沉淀进行广泛交联,可产生一种不溶性酶制剂,称为交联酶聚集体(CLEAs)。CLEAs在传统水性介质和非水性介质中均表现出高稳定性和性能。它们在相当高的温度下也很稳定。可以制备具有多种酶活性的CLEAs,这种CLEAs称为组合CLEAs或多功能CLEAs。交联程度通常会影响它们的形态、稳定性、活性和对映选择性。

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