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Chaia AP, de Ruiz Holgado AP, Oliver G. Peptide Hydrolases of Propionibacteria: Effect of pH and Temperature. J Food Prot. 1990;53(3):237-240doi: 10.4315/0362-028X-53.3.237.
Chaia, A. P., de Ruiz Holgado, A. P., & Oliver, G. (1990). Peptide Hydrolases of Propionibacteria: Effect of pH and Temperature. Journal of food protection, 53(3), 237-240. https://doi.org/10.4315/0362-028X-53.3.237
Chaia, Adriana Perez, et al. "Peptide Hydrolases of Propionibacteria: Effect of pH and Temperature." Journal of food protection vol. 53,3 (1990): 237-240. doi: https://doi.org/10.4315/0362-028X-53.3.237
Chaia AP, de Ruiz Holgado AP, Oliver G. Peptide Hydrolases of Propionibacteria: Effect of pH and Temperature. J Food Prot. 1990 Mar;53(3):237-240. doi: 10.4315/0362-028X-53.3.237. PMID: 31018387.
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J Food Prot. 1990 Mar;53(3):237-240. doi: 10.4315/0362-028X-53.3.237.

Peptide Hydrolases of Propionibacteria: Effect of pH and Temperature.

Journal of food protection

Adriana Perez Chaia, Aida Pesce de Ruiz Holgado, Guillermo Oliver

Affiliations

  1. Centro de Referencia para Lactobacilos (CERELA), Chacabuco 145, 4000 Tucumán, Argentina, and Facultad de Bioquímica, Química y Farmacia, Universidad Nacional de Tucumán.

PMID: 31018387 DOI: 10.4315/0362-028X-53.3.237

Abstract

A comparative study of the activity of peptidases belonging to the four classic propionibacteria species cultured in milk was carried out at different values of pH and temperature. Leucine aminopeptidase and proline iminopeptidase showed greater activity in Propionibacterium freudenreichii than in the other species studied. With the single exception of Propionibacterium jensenii , the propionibacteria peptidase tested exhibited greater affinity for proline than for leucine-p-nitroanilide. Optimum temperature and pH in relation to the activity of both substrates varied according to the species under consideration.

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