Superoxide anion-scavenging activity of alkaline protease hydrolysate from sardine meat

Hironori Moriyama, Yasuyuki Katayama, Hiroyuki Ukeda, Masayoshi Sawamura, Katsuhiro Osajima, Toshiro Matsui, Kiyoshi Matsumoto

Research output: Contribution to journalArticlepeer-review

Abstract

Superoxide anion-scavenging activity (SOSA) of alkaline protease hydrolysate from sardine meat (A-1) was measured by colorimetry using water-soluble tetrazolium salt (WST-1). A-1 showed low activity with IC 50 value of 9.21 mg powder/ml. The hydrolysate was separated into F-1-F-6 on an ODS column. The most, active fraction (F-4) was fractionated by ion exchange chromatography on SP-Sephadex C-25 into three active fractions (1/SP-3/SP). The first fraction, 1/SP, showed the most potent activity (IC 50=4.11 mg powder/ml). By elution with a stepwise gradient of acetonitrile containing 0.1% TFA on Sep-pak plus C18 cartridge, A/SE (IC 50=2.12 mg powder/ml) and B/SE (IC50=7.14 mg powder/ml) were obtained from 1/SP. A/SE was extracted with water or 20% acetonitrile. A/ SE W, the water extract, showed high SOSA with an IC50 value of 0.51 mg powder/ml. The amino acid analysis of each active fraction indicated that five amino acid residues (Leu, Phe, Pro, Met, Tyr) played important roles in the activity. Moreover, it was suggested that the potent scavenger contained few histidine residue.

Original languageEnglish
Pages (from-to)392-398
Number of pages7
JournalNippon Shokuhin Kagaku Kogaku Kaishi
Volume50
Issue number9
DOIs
Publication statusPublished - 2003

All Science Journal Classification (ASJC) codes

  • Food Science

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