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Intracellular X‐prolyl dipeptidyl peptidase from Lactococcus lactis spp. lactis : purification and properties
Author(s) -
Zevaco C.,
Monnet Véronique,
Gripon J.C.
Publication year - 1990
Publication title -
journal of applied bacteriology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.889
H-Index - 156
eISSN - 1365-2672
pISSN - 0021-8847
DOI - 10.1111/j.1365-2672.1990.tb02886.x
Subject(s) - lactococcus lactis , biochemistry , enzyme , proteases , dipeptidyl peptidase , size exclusion chromatography , intracellular , chemistry , gel electrophoresis , serine , biology , chromatography , microbiology and biotechnology , bacteria , lactic acid , genetics
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.