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Appl. Environ. Microbiol., Sep 1995, 3430-3435, Vol 61, No. 9
Copyright © 1995, American Society for Microbiology

Purification and Characterization of a Dipeptidase from Lactobacillus helveticus SBT 2171

PST Tan, M Sasaki, BW Bosman and T Iwasaki
Snow Brand European Research Laboratories B.V., 9747 AN, Groningen, The Netherlands

A metal-dependent dipeptidase was purified to homogeneity from a cell extract of Lactobacillus helveticus SBT 2171 by fast protein liquid chromatography. The enzyme was purified 237-fold from the extract, with a yield of 1.8%. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the purified enzyme showed a single protein band with a molecular weight of 50,000. The dipeptidase hydrolyzes a range of only dipeptides. Dipeptides containing proline, glutamic acid, and aspartic acid are not hydrolyzed. The enzyme was shown to be a metalloenzyme with a pH optimum of 8.0 and a temperature optimum of 55(deg)C. Dithiol-reducing reagents exert strong inhibition on enzyme activity. Kinetic studies indicated that the enzyme has a relative average affinity for leucyl-leucine (K(infm), 0.5 mM). The negative immunoresponse of the purified enzyme with monoclonal antibodies raised against a dipeptidase from Lactococcus lactis subsp. cremoris Wg2 shows that both enzymes can be immunologically distinguished.


This article has been cited by other articles:

  • Goldstein, J. M., Kordula, T., Moon, J. L., Mayo, J. A., Travis, J. (2005). Characterization of an Extracellular Dipeptidase from Streptococcus gordonii FSS2. Infect. Immun. 73: 1256-1259 [Abstract] [Full Text]  


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