Superoxide Anion-Scavenging Activity of Alkaline Protease Hydrolysate from Sardine Meat.

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  • Moriyama Hironori
    Kochi Prefectural Industrial Technology Center
  • Katayama Yasuyuki
    Department of Bioresources Science, Faculty of Agriculture, Kochi University
  • Ukeda Hiroyuki
    Kochi Prefectural Industrial Technology Center Department of Bioresources Science, Faculty of Agriculture, Kochi University
  • Sawamura Masayoshi
    Department of Bioresources Science, Faculty of Agriculture, Kochi University
  • Osajima Katsuhiro
    Research Laboratories, Senmi Ekisu Co.
  • Matsui Toshiro
    Division of Bioscience and Biotechnology, Faculty of Agriculture, Graduate School Kyushu University
  • Matsumoto Kiyoshi
    Division of Bioscience and Biotechnology, Faculty of Agriculture, Graduate School Kyushu University

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Other Title
  • イワシ筋肉アルカリプロテアーゼ加水分解物のスーパーオキシドアニオン消去活性
  • イワシ キンニク アルカリプロテアーゼ カスイ ブンカイ ブツ ノ スーパーオキシドアニオン ショウキョ カッセイ

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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 IC50 value of 9.21mg 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 (IC50=4.11mg powder/ml). By elution with a stepwise gradient of acetonitrile containing 0.1% TFA on Sep-pak plus C18 cartridge, A/SE (IC50=2.12mg powder/ml) and B/SE (IC50=7.14mg 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 0.51mg 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.

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