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Authors
Advisor(s)
Abstract(s)
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 certi"ed 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.
Description
Keywords
Dairy foods Lactic acid bacteria Peptidase activity
Pedagogical Context
Citation
MACEDO, Angela C....[et al] - Peptide hydrolase system of lactic acid bacteria isolated from Serra da Estrela cheese. International Dairy Journal. ISSN 0958-6946. Vol. 10 (2000), p. 769-774
Publisher
Elsevier