Open AccessPurification and characterization of a prolidase from Lactobacillus casei subsp. casei IFPL 731
Author(s) -
M. D. Fernández-Esplá,
M. C. Martín-Hernández,
P.F. Fox
Publication year - 1997
Publication title -
applied and environmental microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.552
H-Index - 324
eISSN - 1070-6291
pISSN - 0099-2240
DOI - 10.1128/aem.63.1.314-316.1997
Subject(s) - lactobacillus casei , enzyme , molecular mass , chemistry , biochemistry , chelation , proline , michaelis–menten kinetics , amino acid , enzyme assay , organic chemistry , fermentation
A peptidase showing a high level of specificity towards dipeptides of the X-Pro type was purified to homogeneity from the cell extract of Lactobacillus casei subsp. casei IFPL 731. The enzyme was a monomer having a molecular mass of 41 kDa. The pH and temperature optima were 6.5 to 7.5 and 55 degrees C, respectively. Metal chelating agents completely inhibited enzyme activity, indicating that the prolidase was a metalloenzyme. The Michaelis constant (K(m)) and Vmax for several proline-containing dipeptides were determined.
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