INVESTIGADORES
VIGNOLO Graciela Margarita
artículos
Título:
Hydrolysis of muscle myofibrillar proteins by Lactobacillus curvatus and Lactobacillus sake
Autor/es:
YOLANDA SANZ; S FADDA,; G VIGNOLO,; MC ARISTOY,; G OLIVER,; F TOLDRA,; GRACIELA MARGARITA VIGNOLO
Revista:
INTERNATIONAL JOURNAL OF FOOD MICROBIOLOGY
Editorial:
Elsevier
Referencias:
Lugar: Amsterdam; Año: 1999 vol. 53 p. 115 - 125
ISSN:
0168-1605
Resumen:
Proteolytic enzyme activities of whole cells and cell free extracts (CFE) of Lactobacillus curvatus CECT 904 andLactobacillus curvatus CECT 904 and
Lactobacillus sake CECT 4808 were characterised using synthetic chromogenic compounds and myofibrillar proteins as
substrates. The hydrolytic action was monitored by SDSPAGE and reverse phase-HPLC analyses. The CFE of L. sakeCECT 4808 were characterised using synthetic chromogenic compounds and myofibrillar proteins as
substrates. The hydrolytic action was monitored by SDSPAGE and reverse phase-HPLC analyses. The CFE of L. sakeL. sake
partially contributed, together with muscle enzymes, to the initial hydrolysis of myofibrillar proteins. Whole-cells of both L.L.
curvatus and L. sake generated peptides considered important for cured-meat taste. The peptide mapping, resulting from the
action on the substrates assayed, revealed a profile of extra and intracellular enzymes. Both strains expressed strong amino
acid metabolism.and L. sake generated peptides considered important for cured-meat taste. The peptide mapping, resulting from the
action on the substrates assayed, revealed a profile of extra and intracellular enzymes. Both strains expressed strong amino
acid metabolism.