Journal of the Korean Society of Food Science and Nutrition (한국식품영양과학회지)

The Korean Society of Food Science and Nutrition (한국식품영양과학회)
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Purification and Biological Characteristics of Alkaline Protease from Aspergillus sp. CC-29

Aspergillus sp. CC-29 생성하는 Alkaline Protease의 정제 및 특성

  • Choi, Cheong (Dept. of Food Science and Technology, Yeungnam University) ;
  • Kim, Doo-Ki (Dept. of Food Science and Technology, Yeungnam University) ;
  • Cho, Young-Je (Dept. of Food Science and Technology, Yeungnam University) ;
  • Sung, Tae-Soo (Dept. of Food and Nutrition, Chang won Junior College)
  • 최청 (영남대학교 식품가공학과) ;
  • 김두기 (영남대학교 식품가공학과) ;
  • 조영제 (영남대학교 식품가공학) ;
  • 성태수 (창원전문대학 식품영양학과)
  • Published : 1990.10.01
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Abstract

Aspergillus sp. CC-29 ws selected for its strong protease activity among various stains of molds found in soil. It was found that the production of alkaline protease reached to maximum when the wheat bran medium containing glucose as carbon source had been cultured for 4 days. Alkaline proteased was purified 36.10 fold from Aspergillus sp. CC-29 The purification procedures included ammonium sulfate fractunation gel filteration on Sepha-dex G-75 G-150 and DEAE-cellulose ion-exchange chromatography, The yield of the purified enzyme was 22.40% The purified enzyme was confirmed as a single band by the polyacryla-mide. When the purified enzyme was applied to SDS-PAGE the molecular weight was estima-ted 24000. The optimum pH for the enzyme activity was 9.0 and the optimum temperature was 4$0^{\circ}C$ The reaction of this enzyme followed typical Michaelis-Menten kinetics with the Km value of 2.10$\times$10-4M with the Vmax of 29.41 $\mu$g/min. The enzyme was reactively stable in alkalic condition and unstable by heat treatment. The activity of alkaline protease was increased by the addition of Ca2+ whereas it was inhibited by Hg2+ Zn2+ at concentration of 1$\times$10-3M.

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