Nitrile hydratase CLEAs: The immobilization and stabilization of an industrially important enzyme
Nitrile hydratase CLEAs: The immobilization and stabilization of an industrially important enzyme
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DOI：
10.1039/b714258g
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发表时间：
2008-04
期刊：
影响因子：
9.8
通讯作者：
S. V. Pelt;Sandrine Quignard;D. Kubáč;D. Sorokin;F. V. Rantwijk;R. Sheldon
中科院分区：
文献类型：
--
作者：
S. V. Pelt;Sandrine Quignard;D. Kubáč;D. Sorokin;F. V. Rantwijk;R. Sheldon
描述了以交联酶聚集体（CLEA®）形式成功固定和稳定腈水合酶的方法。以硫酸铵为凝聚剂，与戊二醛交联制备CLEAs。研究了不同浓度戊二醛对CLEA酶活性恢复和CLEA基质酶泄漏的影响。虽然活性回收率很低（21%），但CLEA有利于分离和回收腈水合酶。研究还发现，与粗提取液和全细胞制剂中的腈水合酶相比，在暴露于高浓度丙烯酰胺和丙烯腈环境下，腈水合酶CLEA具有显著提高的储存稳定性和操作稳定性。
The successful immobilization and stabilization of a nitrile hydratase in the form of a cross-linked enzyme aggregate (CLEA®) is described. CLEAs were prepared by using ammonium sulfate as an aggregation agent followed by cross-linking with glutaraldehyde. The effect of different glutaraldehyde concentrations on the recovery of enzyme activity in the CLEA and enzyme leakage from the CLEA matrix was investigated. Although activity recovery was low (21%) the CLEA facilitates easy separation and recycling of the nitrile hydratase. It was also found that the nitrile hydratase CLEA had substantially increased storage stability as well as increased operational stability during exposure to high concentrations of acrylamide and acrylonitrile compared to that of the nitrile hydratase in the crude cell-free extract and whole cell formulation.