Purification and Characterization of the Alkaline Serine Protease Produced by <i>Bacillus</i> sp. N4 Strain from Fish Skin Mucus

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  • Asakawa Makio
    Laboratory of Food Science, Faculty of Education, Kumamoto University
  • Sadakata Yoshiko
    Laboratory of Food Science, Faculty of Education, Kumamoto University
  • Araki Toshiyoshi
    Faculty of Bioresources, Mie University
  • Sumi Toshihisa
    Department of Applied Biological Sciences, Faculty of Agriculture, Saga University
  • Nakagawa Hiroki
    Department of Applied Biological Sciences, Faculty of Agriculture, Saga University

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  • Purification and Characterization of the Alkaline Serine Protease Produced by Bacillus sp.N4 Strain from Fish Skin Mucus
  • Purification and Characterization of th

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Abstract

Bacillus sp. N4 strain was isolated from the skin mucus of horse mackerel Trachurus japonicus. A protease was purified to homogeneity from the culture fluid by application of ammonium sulfate precipitation, gel nitration, and ion-exchange chromatography. The enzyme (N4-protease) had a single polypeptide chain with apparent molecular weight of 28, 000 estimated by SDS-PAGE, and an isoelectric point around 9.5. The enzyme was most active toward azocasein and Suc-Leu-Leu-Val-Tyr-MCA at pH 10 and toward casein at pH 11, and was stable between pH 6 and pH 11. The optimum temperature of the enzyme was 50°C and its activity was stable below 50°C. Calcium ion was effective to activate and stabilize the enzyme especially at high temperature. Since the activity was completely inhibited by PMSF and DFP but not by sulfhydryl and metal chelating agents, it was concluded that N4-protease is an alkaline serine protease belonging to a member of the subtilisin family.

Journal

  • Fisheries science

    Fisheries science 64 (5), 793-797, 1998

    The Japanese Society of Fisheries Science

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