INVESTIGADORES
VIGNOLO Graciela Margarita
artículos
Título:
Hydrolytic action of Lactobacillus casei CRL705 on pork muscle sarcoplasmic and myofibrillar proteins
Autor/es:
Y SANZ,; S FADDA,; G VIGNOLO,; MC ARISTOY,; G OLIVER,; F TOLDRA,; GRACIELA MARGARITA VIGNOLO
Revista:
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
Editorial:
ACS Publications
Referencias:
Lugar: Washington; Año: 1999 vol. 47 p. 3441 - 3448
ISSN:
0021-8561
Resumen:
Lactobacillus casei CRL 705 was screened, among other meat isolates, for its proteinase and
aminopeptidase activities toward synthetic substrates and, according to that, selected for specific
assays on muscle proteins. The hydrolytic effects of whole cells, cell free extracts (CFE), and the
combination of both on muscle sarcoplasmic and myofibrillar protein extracts was evaluated by
SDS-PAGE and reverse phase HPLC analyses. The proteinase activity of whole cells caused the
degradation of a great number of sarcoplasmic protein bands. A partial hydrolysis was also associated
with CFE that when combined with whole cells showed an important additional degradation. Peptide
profiles from sarcoplasmic protein extracts were greatly modified regardless of the addition of whole
cells or CFE, although their combination intensified these changes. The generation of free amino
acids was remarkable when whole cells and CFE were incorporated together to sarcoplasmic protein
extracts.
degradation of a great number of sarcoplasmic protein bands. A partial hydrolysis was also associated
with CFE that when combined with whole cells showed an important additional degradation. Peptide
profiles from sarcoplasmic protein extracts were greatly modified regardless of the addition of whole
cells or CFE, although their combination intensified these changes. The generation of free amino
acids was remarkable when whole cells and CFE were incorporated together to sarcoplasmic protein
extracts.
aminopeptidase activities toward synthetic substrates and, according to that, selected for specific
assays on muscle proteins. The hydrolytic effects of whole cells, cell free extracts (CFE), and the
combination of both on muscle sarcoplasmic and myofibrillar protein extracts was evaluated by
SDS-PAGE and reverse phase HPLC analyses. The proteinase activity of whole cells caused the
degradation of a great number of sarcoplasmic protein bands. A partial hydrolysis was also associated
with CFE that when combined with whole cells showed an important additional degradation. Peptide
profiles from sarcoplasmic protein extracts were greatly modified regardless of the addition of whole
cells or CFE, although their combination intensified these changes. The generation of free amino
acids was remarkable when whole cells and CFE were incorporated together to sarcoplasmic protein
extracts.
degradation of a great number of sarcoplasmic protein bands. A partial hydrolysis was also associated
with CFE that when combined with whole cells showed an important additional degradation. Peptide
profiles from sarcoplasmic protein extracts were greatly modified regardless of the addition of whole
cells or CFE, although their combination intensified these changes. The generation of free amino
acids was remarkable when whole cells and CFE were incorporated together to sarcoplasmic protein
extracts.
CRL 705 was screened, among other meat isolates, for its proteinase and
aminopeptidase activities toward synthetic substrates and, according to that, selected for specific
assays on muscle proteins. The hydrolytic effects of whole cells, cell free extracts (CFE), and the
combination of both on muscle sarcoplasmic and myofibrillar protein extracts was evaluated by
SDS-PAGE and reverse phase HPLC analyses. The proteinase activity of whole cells caused the
degradation of a great number of sarcoplasmic protein bands. A partial hydrolysis was also associated
with CFE that when combined with whole cells showed an important additional degradation. Peptide
profiles from sarcoplasmic protein extracts were greatly modified regardless of the addition of whole
cells or CFE, although their combination intensified these changes. The generation of free amino
acids was remarkable when whole cells and CFE were incorporated together to sarcoplasmic protein
extracts.
degradation of a great number of sarcoplasmic protein bands. A partial hydrolysis was also associated
with CFE that when combined with whole cells showed an important additional degradation. Peptide
profiles from sarcoplasmic protein extracts were greatly modified regardless of the addition of whole
cells or CFE, although their combination intensified these changes. The generation of free amino
acids was remarkable when whole cells and CFE were incorporated together to sarcoplasmic protein
extracts.
-PAGE and reverse phase HPLC analyses. The proteinase activity of whole cells caused the
degradation of a great number of sarcoplasmic protein bands. A partial hydrolysis was also associated
with CFE that when combined with whole cells showed an important additional degradation. Peptide
profiles from sarcoplasmic protein extracts were greatly modified regardless of the addition of whole
cells or CFE, although their combination intensified these changes. The generation of free amino
acids was remarkable when whole cells and CFE were incorporated together to sarcoplasmic protein
extracts.