PROPERTIES OF THE HYDANTOINASE FROM AGROBACTERIUM SP IP-I-671

被引：41

作者：

RUNSER, S

OHLEYER, E

机构：

[1] Institut de Chimie des Substances Naturelles, Centre National de la Recherche Scientifique, Gif-Sur-Yvette

来源：

BIOTECHNOLOGY LETTERS | 1990年 / 12卷 / 04期

关键词：

D O I：

10.1007/BF01093518

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

A hydantoin-hydrolyzing enzyme has been purified from an newly isolated Agrobacterium sp. by procedures including ammonium sulfate fractionation and ion-exchange chromatography. Kinetic studies have demonstrated that this enzyme, which is strictly d-selective and has a broad substrate specificity exhibits remarkable stability. Microbial bioconversion at 60°C and pH 10.0, allowed complete conversion of 30 g/L of d,l 5-benzylhydantoin into the dN-carbamyl derivative of phenylalanine (molar yield of 96%) in less than 10 h. The hydantoinase is activated by Ni2+ ions. © 1990 Kluwer Academic Publishers.

引用

页码：259 / 264

页数：6

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