Your browser doesn't support javascript.
loading
Mostrar: 20 | 50 | 100
Resultados 1 - 2 de 2
Filtrar
Mais filtros











Base de dados
Intervalo de ano de publicação
1.
J Dairy Sci ; 95(10): 5536-43, 2012 Oct.
Artigo em Inglês | MEDLINE | ID: mdl-22901481

RESUMO

The ability of specific wild Lactococcus lactis strains to hydrolyze milk proteins to release angiotensin I-converting enzyme (ACE) inhibitory peptides was evaluated. The peptide profiles were obtained from the <3 kDa water-soluble extract and subsequently fractionated by reversed-phase HPLC. The fractions with the lowest half-maximal inhibitory concentration estimated values (peptide concentration necessary to inhibit ACE activity by 50%) were Lc. lactis NRRL B-50571 fraction (F)1 (0.034 ± 0.002 µg/mL; mean ± SD) and Lc. lactis NRRL B-50572B F 0005 (0.041 ± 0.003 µg/mL; mean ± SD). All peptide fractions were analyzed by reversed-phase HPLC tandem mass spectrometry. Twenty-one novel peptide sequences associated with ACE inhibitory (ACEI) activity were identified. Several novel ACEI peptides presented peptides encrypted with proven hypotensive activity. In conclusion, specific wild Lc. lactis strains were able to hydrolyze milk proteins to generate potent ACEI peptides. However, further studies are necessary to find out the relationship between Lc. lactis strain proteolytic systems and their ability to biogenerate hypotensive peptides.


Assuntos
Inibidores da Enzima Conversora de Angiotensina/análise , Lactococcus lactis/metabolismo , Leite/microbiologia , Peptídeos/análise , Animais , Bovinos , Cromatografia Líquida de Alta Pressão/métodos , Cromatografia de Fase Reversa/métodos , Fermentação , Leite/química , Leite/metabolismo , Peptidil Dipeptidase A/metabolismo , Espectrometria de Massas em Tandem/métodos
2.
J Dairy Sci ; 94(8): 3794-800, 2011 Aug.
Artigo em Inglês | MEDLINE | ID: mdl-21787916

RESUMO

The objective of this study was to evaluate if Mexican Fresco cheese manufactured with specific lactic acid bacteria (LAB) presented angiotensin I-converting enzyme inhibitory (ACEI) activity. Water-soluble extracts (3 kDa) obtained from Mexican Fresco cheese prepared with specific LAB (Lactococcus, Lactobacillus, Enterococcus, and mixtures: Lactococcus-Lactobacillus and Lactococcus-Enterococcus) were evaluated for ACEI activity. Specific peptide fractions with high ACEI were analyzed using reverse phase-HPLC coupled to mass spectrometry for determination of amino acid sequence. Cheese containing Enterococcus faecium or a Lactococcus lactis ssp. lactis-Enterococcus faecium mixture showed the largest number of fractions with ACEI activity and the lowest half-maximal inhibitory concentration (IC(50); <10 µg/mL). Various ACEI peptides derived from ß-casein [(f(193-205), f(193-207), and f(193-209)] and α(S1)-casein [f(1-15), f(1-22), f(14-23), and f(24-34)] were found. The Mexican Fresco cheese manufactured with specific LAB strains produced peptides with potential antihypertensive activity.


Assuntos
Inibidores da Enzima Conversora de Angiotensina/análise , Queijo/análise , Queijo/normas , Cromatografia Líquida de Alta Pressão , Manipulação de Alimentos/métodos , Proteínas do Leite/análise , Espectrometria de Massas por Ionização por Electrospray
SELEÇÃO DE REFERÊNCIAS
DETALHE DA PESQUISA