Purification and characterization of a dipeptidase from Streptococcus cremoris Wg2

Astract: A dipeptidase was purified to homogeneity from a crude cell extract of Streptococcus cremoris Wg2 by DEAE-Sephacel column chromatography followed by preparative disc gel electrophoresis. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the purified enzyme showed a single protein...

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Bibliographic Details
Published in:Applied and Environmental Microbiology 1988-01, Vol.54 (1), p.43-49
Main Authors: Boven, A. van, Tan, P.S.T, Konings, W.N
Format: Article
Language:English
Subjects:
Biological and medical sciences
Biology of microorganisms of confirmed or potential industrial interest
Biotechnology
dipeptidase
EPURATION
Food additives
Food industries
Food Microbiology
Fundamental and applied biological sciences. Psychology
General aspects
Mission oriented research
PEPTIDASAS
PEPTIDASE
Physiology and metabolism
PURIFICACION
STREPTOCOCCUS
Streptococcus cremoris
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Summary:Astract: A dipeptidase was purified to homogeneity from a crude cell extract of Streptococcus cremoris Wg2 by DEAE-Sephacel column chromatography followed by preparative disc gel electrophoresis. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the purified enzyme showed a single protein band with a molecular weight of 49,000. The dipeptidase is capable of hydrolyzing a range of dipeptides, but not peptides with longer chains. The enzyme was shown to be a metallo-Mn2+ enzyme with a pH optimum of 8 and a temperature optimum of 50 degrees C. The enzyme is strongly inhibited by thiol-reducing reagents but not by sulfhydryl reagents. Kinetic studies indicated that the enzyme has a relatively low affinity for leucyl-leucine and alanyl-alanine (Km, 1.6 and 7.9 mM, respectively) but can hydrolyze these substrates at very high rates (Vmax, 3,700 and 13,000 umol/mim per mg of protein, respectively)
ISSN:0099-2240
1098-5336
DOI:10.1128/AEM.54.1.43-49.1988