INTRACELLULAR X-PROLYL DIPEPTIDYL PEPTIDASE FROM LACTOCOCCUS-LACTIS SPP LACTIS - PURIFICATION AND PROPERTIES

被引：87

作者：

ZEVACO, C ^{[1
]}

MONNET, V ^{[1
]}

GRIPON, JC ^{[1
]}

机构：

[1] INRA,STN RECH LAITIERES,F-78350 JOUY EN JOSAS,FRANCE

来源：

JOURNAL OF APPLIED BACTERIOLOGY | 1990年 / 68卷 / 04期

关键词：

D O I：

10.1111/j.1365-2672.1990.tb02886.x

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：

An X‐prolyl dipeptidyl peptidase (EC 3.4.14.5) has been purified from a crude intracellular extract from Lactococcus lactis spp. lactis NCDO 763 by ion‐exchange chromatography and gel filtration. One protein band was detected after electrophoresis of the purified enzyme in the presence or absence of sodium dodecyl sulphate. The enzyme is a 190 kDa dimer composed of identical subunits. Optimal activity occurs at pH 8.5 and 40–45°C and the enzyme is inhibited by reagents specific for serine proteases, such as diisopropylfluorophosphate. The enzyme hydrolyzes p‐nitroanilide‐ or β‐naphthylamide‐substituted X‐Pro dipeptides, as well as β‐casomorphin. Copyright © 1990, Wiley Blackwell. All rights reserved

引用

页码：357 / 366

页数：10

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