Digestion Pattern of Antihypertensive Angiotensin I-Converting Enzyme Inhibitory Peptides from Saccharomyces cerevisiae in a Successive Simulated Gastricintestinal Bioreactor
Mycobiology
;
: 67-69, 2011.
Artigo
em Inglês
| WPRIM
| ID: wpr-729242
ABSTRACT
A cell-free extract of Saccharomyces cerevisiae containing the angiotensin I-converting enzyme (ACE) inhibitory peptide was treated in a successive simulated gastric-intestinal bioreactor (step 1 amylase digestion, step 2 gastric fluid digestion, step 3 intestinal fluid digestion) to illustrate the absorption pattern of antihypertensive ACE inhibitory peptide, and the ACE inhibitory activities of each step were determined. Total ACE inhibitory activities of step 1, step 2, and step 3 were 55.96%, 80.09%, and 76.77%, respectively. The peptide sequence of each steps was analyzed by MS/MS spectrophotometry. Eleven kinds of representative peptide sequences were conserved in each step, and representative new peptides including RLPTESVPEPK were identified in step 3.
Texto completo:
DisponíveL
Índice:
WPRIM (Pacífico Ocidental)
Assunto principal:
Peptídeos
/
Saccharomyces
/
Saccharomyces cerevisiae
/
Espectrofotometria
/
Angiotensinas
/
Peptidil Dipeptidase A
/
Reatores Biológicos
/
Digestão
/
Absorção
/
Amilases
Idioma:
Inglês
Revista:
Mycobiology
Ano de publicação:
2011
Tipo de documento:
Artigo
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