Isolation and identification of peptidic α-glucosidase inhibitors derived from sardine muscle hydrolyzate

Toshiro Matsui, Tomoyuki Oki, Yutaka Osajima

Research output: Contribution to journalArticle

31 Citations (Scopus)

Abstract

We report here the isolation of α-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 tripeptide 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.

Original languageEnglish
Pages (from-to)259-263
Number of pages5
JournalZeitschrift fur Naturforschung - Section C Journal of Biosciences
Volume54
Issue number3-4
DOIs
Publication statusPublished - Jan 1 1999

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Glucosidases
Muscle
Muscles
Peptides
N-valyltryptophan
Inhibitory Concentration 50
Aromatic Amino Acids
Bacilli
Chain length
Amides
Purification
Tyrosine
Protons
Digestion
Fatty Acids
High Pressure Liquid Chromatography
Derivatives
Amino Acids

All Science Journal Classification (ASJC) codes

  • Biochemistry, Genetics and Molecular Biology(all)

Cite this

Isolation and identification of peptidic α-glucosidase inhibitors derived from sardine muscle hydrolyzate. / Matsui, Toshiro; Oki, Tomoyuki; Osajima, Yutaka.

In: Zeitschrift fur Naturforschung - Section C Journal of Biosciences, Vol. 54, No. 3-4, 01.01.1999, p. 259-263.

Research output: Contribution to journalArticle

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