Characterization of cholylglycine hydrolase from a bile-adapted strain of Xanthomonas maltophilia and its application for quantitative hydrolysis of conjugated bile salts

被引:37
作者
Dean, M
Cervellati, C
Casanova, E
Squerzanti, M
Lanzara, V
Medici, A
de Laureto, PP
Bergamini, CM
机构
[1] Univ Ferrara, Dept Biochem & Mol Biol, I-44100 Ferrara, Italy
[2] Univ Ferrara, Dept Chem, I-44100 Ferrara, Italy
[3] Univ Ferrara, Ctr Study Inflammatory Dis, ICSI, I-44100 Ferrara, Italy
[4] Univ Padua, Ctr Biotechnol, CRIBI, Padua, Italy
关键词
D O I
10.1128/AEM.68.6.3126-3128.2002
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
Purified bile salt hydrolase from bile-adapted Xanthomonas maltophilia displays Michaelis-Menten kenetics on cholylglycine and cholyltaurine and hydrolyzes bile salts also in crude bovine bile. The protein is a dimer and is resistant to proteinases and to heating at 55 to 60degreesC for up to 60 min, in agreement with calorimetric data.
引用
收藏
页码:3126 / 3128
页数:3
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