Purification and Properties of Glucoamylase form Yeast Candida tsukuaensis

  • Kim, Sanga-Moon (Department of Spectacles and Optics, Kwang-ju Health Junior College) ;
  • Bai, Suk (Department of microbiology, College of Natural Sciences, Chonnam National University) ;
  • Chung, Hee-Young (Department of microbiology, College of Natural Sciences, Chonnam National University) ;
  • Park, Jong-Chun (Department of microbiology, College of Natural Sciences, Chonnam National University) ;
  • Lee, Jin-Jong (Department of microbiology, College of Natural Sciences, Chonnam National University) ;
  • Kim, Dong-Ho (Department of microbiology, College of Natural Sciences, Chonnam National University) ;
  • Song, Myoung-Hee (Department of microbiology, College of Natural Sciences, Chonnam National University) ;
  • Chun, Soon-Bai (Department of microbiology, College of Natural Sciences, Chonnam National University)
  • Published : 1992.12.01

Abstract

The glucoamylase of Candida tsuubaensis was purified to homogeneity form culture filtrate by means of ultrafiltration, Sephacryl S-200 gel filtration and Sp-Sephadex C-50 chromatography. The purified enzyme was a glycoprotein with a molecular mass of approximately 50 kDa, which was a monomeric protein. Km values were 5.8 mg/ml for soluble starch and 0.04 mM for maltose. Glucoamylase also released only glucose from both pullulan and isomaltose. The analysis of amino acid composition revealed that the enzyme contained a high content of acidic and polar amino acids. In addition, Western blotting analysis indicates that C. tsukubaensis glucoamylase is resistant to glucose repression.

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