Peptide hydrolase system of lactic acid bacteria isolated from Serra da Estrela cheese

• Type: Article in International Scientific Journal
• Date: 2000

Authors

Macedo, AC (Author) Other; Vieira, M (Author) Other; Pocas, R (Author) Other; F. Xavier Malcata (Author) Other

Journal

Title: International Dairy Journal

Vol. 10

Pages: 769-774

ISSN: 0958-6946

Publisher: Elsevier

Indexing

ISI Web of Knowledge - 47 Citations

Scopus - 55 Citations

Other information

Authenticus ID: P-001-1P8

DOI: 10.1016/s0958-6946(00)00111-4

Abstract (EN): Lactobacillus paracasei subsp. paracasei ESB 230, Leuconostoc mesenteroides subsp. mesenteroides ESB 136, Lactococcus lactis subsp. lactis ESB 117 and Enterococcus faecium ESB 50, previously isolated from certified Serra da Estrela cheeses, were tested for their aminopeptidase, dipeptidyl aminopeptidase, endopeptidase, dipeptidase and carboxypeptidase activities. The crude cell-free extracts (CFE) of Lb. paracasei ESB 230 exhibited the highest aminopeptidase activity, followed by CFE of Leuc. mesenteroides ESB 136 and, at last, by CFE of L. lactis ESB 117; the aminopeptidase activity in CFE of Ent. faecium was practically non-existent. The four CFE studied also showed appreciable carboxypeptidase activities, although these were lower than their dipeptidase counterparts; in addition, their dipeptidyl aminopeptidase and endopeptidase activities were lower than their aminopeptidase activities. Dipeptides consisting of hydrophobic amino acid residues (i.e. leucine, methionine and phenylalanine) were more rapidly attacked by all CFE than those with hydrophilic amino acid residues. The peptide hydrolase system of CFE of Lb, paracasei ESB 230 was qualitatively quite similar to, but quantitatively more active than that of CFE of Leuc. mesenteroides ESB 136 (except for the endopeptidase); additionally, the CFE of L, lactis ESB 117 and of Ent, faecium ESB 50 were quite distinct from each other, and from the other two CFE tested.

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 6