Mycobiology.  2011 Mar;39(1):67-69.

Digestion Pattern of Antihypertensive Angiotensin I-Converting Enzyme Inhibitory Peptides from Saccharomyces cerevisiae in a Successive Simulated Gastricintestinal Bioreactor

• Jang JH
• Jeong SC
• Lee JK
• Lee JS

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.

Keyword

Angiotensin I-converting enzyme inhibitory peptides; Digestion pattern; Simulated gastric-intestinal bioreactor

MeSH Terms

Absorption
Amylases
Angiotensins
Bioreactors
Digestion
Peptides
Peptidyl-Dipeptidase A
Saccharomyces
Saccharomyces cerevisiae
Spectrophotometry
Amylases
Angiotensins
Peptides
Peptidyl-Dipeptidase A