INVESTIGADORES
FADDA Silvina Graciela
artículos
Título:
Characterization of muscle sarcoplasmic and myofibrillar protein hydrolysis caused by Lactobacillus plantarum.
Autor/es:
SILVINA GRACIELA FADDA; YOLANDA SANZ; GRACIELA VIGNOLO,; MC ARISTOY,; GUILLERMO OLIVER; FIDEL TOLDRÁ,
Revista:
APPLIED AND ENVIRONMENTAL MICROBIOLOGY
Editorial:
American Society For Microbiology
Referencias:
Lugar: Washington, DC; Año: 1999 vol. 65 p. 3540 - 3546
ISSN:
0099-2240
Resumen:
Strains of Lactobacillus plantarum originally isolated from sausages were screened for proteinase and
aminopeptidase activities toward synthetic substrates; on the basis of that screening, L. plantarum CRL 681
was selected for further assays on muscle proteins. The activities of whole cells, cell extracts (CE), and a
combination of both on sarcoplasmic and myofibrillar protein extracts were determined by protein, peptide,
and free-amino-acid analyses. Proteinase from whole cells initiated the hydrolysis of sarcoplasmic proteins.
The addition of CE intensified the proteolysis. Whole cells generated hydrophilic peptides from both sarcoplasmic
and myofibrillar proteins. Other peptides of a hydrophobic nature resulted from the combination of
whole cells and CE. The action of both enzymatic sources on myofibrillar proteins caused maximal increases
in lysine, arginine, and leucine, while the action of those on sarcoplasmic proteins mainly released alanine. In
general, pronounced hydrolysis of muscle proteins required enzyme activities from whole cells in addition to
those supplied by CE.Lactobacillus plantarum originally isolated from sausages were screened for proteinase and
aminopeptidase activities toward synthetic substrates; on the basis of that screening, L. plantarum CRL 681
was selected for further assays on muscle proteins. The activities of whole cells, cell extracts (CE), and a
combination of both on sarcoplasmic and myofibrillar protein extracts were determined by protein, peptide,
and free-amino-acid analyses. Proteinase from whole cells initiated the hydrolysis of sarcoplasmic proteins.
The addition of CE intensified the proteolysis. Whole cells generated hydrophilic peptides from both sarcoplasmic
and myofibrillar proteins. Other peptides of a hydrophobic nature resulted from the combination of
whole cells and CE. The action of both enzymatic sources on myofibrillar proteins caused maximal increases
in lysine, arginine, and leucine, while the action of those on sarcoplasmic proteins mainly released alanine. In
general, pronounced hydrolysis of muscle proteins required enzyme activities from whole cells in addition to
those supplied by CE.L. plantarum CRL 681
was selected for further assays on muscle proteins. The activities of whole cells, cell extracts (CE), and a
combination of both on sarcoplasmic and myofibrillar protein extracts were determined by protein, peptide,
and free-amino-acid analyses. Proteinase from whole cells initiated the hydrolysis of sarcoplasmic proteins.
The addition of CE intensified the proteolysis. Whole cells generated hydrophilic peptides from both sarcoplasmic
and myofibrillar proteins. Other peptides of a hydrophobic nature resulted from the combination of
whole cells and CE. The action of both enzymatic sources on myofibrillar proteins caused maximal increases
in lysine, arginine, and leucine, while the action of those on sarcoplasmic proteins mainly released alanine. In
general, pronounced hydrolysis of muscle proteins required enzyme activities from whole cells in addition to
those supplied by CE.
