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Peptidase and proteinase activity ofLactococcus lactis, Lactobacillus casei andLactobacillus plantarum

Peptidase- und Proteinase-Aktivität vonLactococcus lactis, Lactobacillus casei undLactobacillus plantarum

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Zusammenfassung

Das proteolytische System von mehreren nicht kommerziellenLactococcus- undLactobacillus-Stämmen wurde direkt vom traditionellen spanischen halbfesten Ziegenmilchkäse isoliert und untersucht. Die Aktivität von Aminopeptidase, X-Prolyldipeptidylaminopeptidase, Dipeptidase and Proteinase dieser neuen Stämme wurde in cytoplasmatischen, Zellwand-Membran- und spontan freigesetzten Fraktionen gemessen. Die Aminopeptidase-Aktivität erfolgte ausschließlich intracellular und war höher fürLactobacillus casei subsp. casei als fürLactococcus lactis subsp.lactis. Lactobacillus plantarum zeigte höhere Dipeptidase Aktivität alsL. casei. Die höchsten Werte für die Proteinase-Aktivität wurden für die Zellwand-Membran-Fraktion vonLactococcus lactis subsp.lactis IFPL359 gemessen. Für alle untersuchten Stämme war die Aktivität höher bei β-Casein als bei αs-Casein. Dieses Ergebnis weist auf den unterschiedlichen Einfluß dieser Stämme bei der Proteolyse von Käse während der Reifung hin. Die Stämme scheinen sich gegenseitig zu ergänzen, wenn sie gemeinsam in Starterkulturen verwendet werden.

Abstract

The proteolytic system of several non-commercial strains of lactococci and lactobacilli that were isolated directly from traditional-Spanish, semi-hard, goats' milk cheese was studied. The aminopeptidase, X-prolyldipeptidyl aminopeptidase, dipeptidase and proteinase activity of these new strains was measured for the cytoplasmic, cell-wall/membrane and spontaneously released fractions. The aminopeptidase activity was exclusively intracellular and higher forLactobacillus casei subsp.casei than forLactococcus lactis subsp.lactis. Lactobacillus plantarum showed higher dipeptidase activity thanL. casei. The highest level of proteinase activity was recorded for the cell-wallmembrane fraction ofLactococcus lactis subsp.lactis IFPL 359, and was higher on β-casein than on αs-casein for all the strains studied. These results suggest some different contribution of these strains to the proteolysis of cheese during ripening and they seem to complement each other when used together in the starter culture.

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Author notes

  1. Teresa Requena

    Present address: Department of Food Science and Nutrition, University of Minnesota, 1334 Eckles Avenue, 55108, St. Paul, MN, USA

Authors and Affiliations

  1. Institute del Frío (CSIC), Ciudad Universitaria, E-28040, Madrid, Spain

    Teresa Requena & Carmen Pelaez

  2. Department of Food Chemistry, University College Cork, Cork, Ireland

    Patrick F. Fox

Authors
  1. Teresa Requena
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  2. Carmen Pelaez
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  3. Patrick F. Fox
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Requena, T., Pelaez, C. & Fox, P.F. Peptidase and proteinase activity ofLactococcus lactis, Lactobacillus casei andLactobacillus plantarum . Z Lebensm Unters Forch 196, 351–355 (1993). https://doi.org/10.1007/BF01197934

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  • DOI: https://doi.org/10.1007/BF01197934

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