INVESTIGADORES
VIGNOLO Graciela Margarita
artículos
Título:
Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal proteins by the action of met-borne Lactobacillus
Autor/es:
CASTELLANO, PATRICIA; ARISTOY, MARIA CONCEPCIÓN; SENTANDREU, MIGUEL ANGEL; VIGNOLO, GRACIELA; TOLDRÁ, FIDEL
Revista:
JOURNAL OF PROTEOMICS
Editorial:
ELSEVIER SCIENCE BV
Referencias:
Lugar: Amsterdam; Año: 2013
ISSN:
1874-3919
Resumen:
Angiotensin I converting enzyme (ACE) inhibitory activity of peptides derived from the
hydrolysis of sarcoplasmic and myofibrillar porcine proteins by the action of Lactobacillus
sakei CRL1862 and Lactobacillus curvatus CRL705 (whole cells + cell free extracts) was
investigated at 30 °C for 36 h. The protein hydrolysates were subjected to RP-HPLC in
order to fractionate the extracts for further evaluation of ACE inhibitory activity. Bioactive
fractions were only found from the hydrolysis of sarcoplasmic proteins by both assayed
lactobacilli strains. Identification of peptides contained in the bioactive fractions was
carried out by tandem mass spectrometry using a nanoLC-ESI-QTOF instrument and the
mascot search engine. From the four most active fractions obtained, a total of eighteen and
fifty peptides were characterized from L. sakei CRL1862 and L. curvatus CRL705 protein
hydrolysates, respectively. The sequence FISNHAY was generated by the proteolytic activity
of the two lactobacilli species. Sequence similarity analyses between the peptides identified
in this study and those previously identified as ACE inhibitory peptides and detailed in the
BIOPEP database were outlined. Results suggest that meat-borne Lactobacillus were able to
generate peptides with ACE inhibitory activity, highlighting their potential to be used in the
development of functional fermented products.Lactobacillus
sakei CRL1862 and Lactobacillus curvatus CRL705 (whole cells + cell free extracts) was
investigated at 30 °C for 36 h. The protein hydrolysates were subjected to RP-HPLC in
order to fractionate the extracts for further evaluation of ACE inhibitory activity. Bioactive
fractions were only found from the hydrolysis of sarcoplasmic proteins by both assayed
lactobacilli strains. Identification of peptides contained in the bioactive fractions was
carried out by tandem mass spectrometry using a nanoLC-ESI-QTOF instrument and the
mascot search engine. From the four most active fractions obtained, a total of eighteen and
fifty peptides were characterized from L. sakei CRL1862 and L. curvatus CRL705 protein
hydrolysates, respectively. The sequence FISNHAY was generated by the proteolytic activity
of the two lactobacilli species. Sequence similarity analyses between the peptides identified
in this study and those previously identified as ACE inhibitory peptides and detailed in the
BIOPEP database were outlined. Results suggest that meat-borne Lactobacillus were able to
generate peptides with ACE inhibitory activity, highlighting their potential to be used in the
development of functional fermented products.CRL1862 and Lactobacillus curvatus CRL705 (whole cells + cell free extracts) was
investigated at 30 °C for 36 h. The protein hydrolysates were subjected to RP-HPLC in
order to fractionate the extracts for further evaluation of ACE inhibitory activity. Bioactive
fractions were only found from the hydrolysis of sarcoplasmic proteins by both assayed
lactobacilli strains. Identification of peptides contained in the bioactive fractions was
carried out by tandem mass spectrometry using a nanoLC-ESI-QTOF instrument and the
mascot search engine. From the four most active fractions obtained, a total of eighteen and
fifty peptides were characterized from L. sakei CRL1862 and L. curvatus CRL705 protein
hydrolysates, respectively. The sequence FISNHAY was generated by the proteolytic activity
of the two lactobacilli species. Sequence similarity analyses between the peptides identified
in this study and those previously identified as ACE inhibitory peptides and detailed in the
BIOPEP database were outlined. Results suggest that meat-borne Lactobacillus were able to
generate peptides with ACE inhibitory activity, highlighting their potential to be used in the
development of functional fermented products.L. sakei CRL1862 and L. curvatus CRL705 protein
hydrolysates, respectively. The sequence FISNHAY was generated by the proteolytic activity
of the two lactobacilli species. Sequence similarity analyses between the peptides identified
in this study and those previously identified as ACE inhibitory peptides and detailed in the
BIOPEP database were outlined. Results suggest that meat-borne Lactobacillus were able to
generate peptides with ACE inhibitory activity, highlighting their potential to be used in the
development of functional fermented products.Lactobacillus were able to
generate peptides with ACE inhibitory activity, highlighting their potential to be used in the
development of functional fermented products.