Isolation and identification of peptidic alpha-glucosidase inhibitors derived from sardine muscle hydrolyzate.
We report here the isolation of alpha-glucosidase (AGH) inhibitory peptides derived from sardine muscle hydrolyzate, which was prepared by digestion with Bacillus licheniformis alkaline protease. As a result of reversed-phase HPLC purification, two AGH inhibitory peptides were isolated from a DEAE-Sephadex A-25 column eluate. The peptides were identified as follows: Val-Trp (IC50 = 22.6 mM) and Try-Tyr-Pro-Leu (IC50 = 3.7 mM). AGH inhibitory studies of Try-Tyr-Pro-Leu and its derivatives demonstrated the importance of the tri-peptide chain length as well as the hydrophobic aromatic amino acid tyrosine at the N-terminus, aliphatic amino acids at the C-terminus, as well as an amide proton from the peptide chain at the middle position of the tri-peptide to develop AGH inhibition activity.
Matsui
T
T
Department of food Science and Technology, Kyusu University, Fukuoka, Japan. tmatsui@agr.kyushu-u.ac.jp
Oki
T
T
Osajima
Y
Y
D000818:Animals; D002851:Chromatography, High Pressure Liquid; D002852:Chromatography, Ion Exchange; D010450:Endopeptidases; D004791:Enzyme Inhibitors / Q000737:chemistry / Q000302:isolation & purification*; D005399:Fishes; D065089:Glycoside Hydrolase Inhibitors; D007700:Kinetics; D018482:Muscle, Skeletal / Q000737:chemistry*; D010455:Peptides / Q000737:chemistry / Q000302:isolation & purification*; D012441:Saccharomyces cerevisiae / Q000201:enzymology
D004791:Enzyme Inhibitors; D065089:Glycoside Hydrolase Inhibitors; D010455:Peptides; D010450:Endopeptidases