Effect of High Pressures on Enzymatic System of Mesophilic Starters Used for Cheesemaking

  • M. Krasowska
  • A. Reps
  • A. Jankowska
  • M. Bielecka
Conference paper


The influence of high pressures on enzymatic fractions of mesophilic lactic acid bacteria was studied. The extra- and intracellular enzymes were exposed, at an ambient temperature (15 minutes), to pressurization under 200, 400, 600 and 800 MPa. In the samples, quantitative analyses of aminopeptidase (Ala-pNa, Leu-pNa, Lys-pNa, Pro-pNa), dipeptidase (Ala-Pro, Leu-Leu), endopeptidase (N-Succinyl-L-Phe-pNa), caseinolytic as well as acidifying activity of the enzymes were performed. The variable degree of pressure-induced inactivation of activities determined in the experiment, was strictly dependent on substrate specificity of the enzymes. A significant reduction of acidifying activity of the bacterial enzymes processed at pressures higher than 200 MPa, and preservation of their proteolytic activity, indicated on possibility of obtaining enzymatic preparation for acceleration of cheese ripening.


Lactic Acid Bacterium Extracellular Enzyme Intracellular Enzyme Bacterial Enzyme Enzymatic Fraction 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. [1]
    Anson M.L. 1938. The estimation of pepsin, trypsin, papain and cathepsin with hemoglobin. J. Gen. Physiol. 22, 79–81.CrossRefGoogle Scholar
  2. [2]
    Bielecka M. 1984. Zakwasy mleczarskie. Instrukcje technologiczne produkcji zakwasów. CZSM Warszawa, pp 31.Google Scholar
  3. [3]
    Coolbear T., Reid J.R., Pritchard G.G. 1992. Stability and Specificity of the Cell Wall-Associated Proteinase from Lactococcus lactis subsp. cremoris H2 Released by Treatment with Lysozyme in the Presence of Calcium Ions. Appl. Environ. Microb., 58, 3263–3270.Google Scholar
  4. [4]
    Doi E., Shibata D., Matoba T. 1981. Modified Colorymetric Ninhydrin Methods for Peptidase Assay. Anal. Biochem. 118, 173–184.Google Scholar
  5. [5]
    Garcia-Graells C., Masschalck B., Michiels C. W. 1999. Inactivation of Escherichia coli in Milk by High-Hydrostatic-Pressure Treatment in Combination with Antimicrobial Peptides. J. Food Prot. 62, 1248–1254.Google Scholar
  6. [6]
    Gervilla R., Ferragut V., Guamis B. 2000. High Pressure Inactivation of Microorganisms Inoculated into Ovine Milk of Different Fat Contents. J. Dairy Sci. 83, 674–682.CrossRefGoogle Scholar
  7. [7]
    Lowry O. H., Rosebrough N. J., Farr A. L., Randall R. J. 1951. Protein measurement with the Folin reagent. J. Biol. Chem. 193, 265–274.Google Scholar
  8. [8]
    Requena T., Pelaez C., Fox P.F. 1993. Peptidase and proteinase activity of Lactococcus lactis, Lactobacillus casei and Lactobacillus plantarum. Z. Lebensm. Unters. Forsch. 196, 351–355.Google Scholar
  9. [9]
    Westhoff D. C., Cowman R. A., Speck M. L. 1971. Isolation and Partial Characterization of a Particulate Proteinase from a Slow Acid Producing Mutant of Streptococcus lactis. J. Dairy Sci. 54, 1253–1258.CrossRefGoogle Scholar

Copyright information

© Springer-Verlag Berlin Heidelberg 2003

Authors and Affiliations

  • M. Krasowska
    • 1
  • A. Reps
    • 1
  • A. Jankowska
    • 1
  • M. Bielecka
    • 1
  1. 1.Institute of Food BiotechnologyWarmia and Mazury UniversityOlsztynPoland

Personalised recommendations