Partial Purification and Characterization of Halotolerant Alkaline Protease from Halomonas marisflava KCCM 10457 Isolated from Salt-fermented Food

  • In, Man-Jin (Department of Human Nutrition and Food Science, Chungwoon University) ;
  • Oh, Nam-Soon (Department of Food Science and Technology, Kongju National University) ;
  • Kim, Dong-Chung (Department of Food Science, Suncheon First College)
  • Published : 2005.06.30

Abstract

Halotolerant protease produced by Halomonas marisflava KCCM 10457 was partially purified through ammonium sulfate precipitation and Sephacryl S-200HR gel permeation chromatography. Optimal pH and temperature of protease were 11.0 and $45^{\circ}C$, respectively. Enzyme activity was inhibited by $Cu^{2+}$, $Hg^{2+}$, $Fe^{2+}$, and $Fe^{3+}$, and selectively inhibited by p-chloromercuribenzoic acid (PCMB), suggesting this enzyme is cysteine protease. The enzyme is halotolerant, because it retained 77% of original activity in presence of 3.33 M NaCl. The protease showed broad substrate specificity to various natural proteins; BSA, casein, egg albumin, gelatin, and hemoglobin.

Keywords

References

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