Korean Journal of Microbiology (미생물학회지)

The Microbiological Society of Korea (한국미생물학회)
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Purification and Properties of Glucoamylase from Schwanniomyces castellii

Schwanniomyces castellii Glucoamylase의 정제 및 성질

  • Bai, Suk (Department of Microbiology, Chonnam National University) ;
  • Park, Jong-Chun (Department of Microbiology, Chonnam National University) ;
  • Kim, Dong-Ho (Department of Biology, Chonnam National University) ;
  • Kim, Kang-Hwa (Department of Food and Nutrition, Chonnam National University) ;
  • Chun, Soon-Bai (Department of Microbiology, Chonnam National University)
  • 배석 (전남대학교 미생물학과) ;
  • 박종천 (전남대학교 미생물학과) ;
  • 김동호 (전남대학교 생물학과) ;
  • 김강화 (전남대학교 식품영양학과) ;
  • 전순배 (전남대학교 미생물학과)
  • Published : 1991.05.01
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Abstract

The glucoamylase of Schwanniomyces castellii was purified to homogeneity from the culture filtrate. the purified enzyme was a glycoprotein with a molecular mass of about 145 KDa, which was monomeric protein with an isoelectric point of 4.3. The pH and temperature optima were 5.5 and 40.deg.C, respectively. The enzyme was fairly stable up to 50.deg.C and at acid pH range (pH 4.5-6.0). The apparent Km of the enzyme toward soluble starch, isomaltose and pullulan were 3.84, 0.51 and 13.7 mg/ml, respectively. The analysis of amino acid composition on this enzyme was found to be acidic protein like other fungal glucoamylase. The amino acid sequence of N-terminal peptide consisted of Ala-Pro-Ala-Asp-Gly-Ile-Gly-Asp-X-Ala-X-Ala.

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