Title Purification and properties of glucoamylase form yeast candida tsukuaensis
Author Kim, Sanga Moon * · Bai, Suk · Chung, Hee Young · Park, Jong Chun · Lee, Jin Jong · Kim, Dong Ho · Song, Myung Hee · Chun, Soon Bai
Address * Department of Spectacles and Opticd, Kwang-ju Health Junior College; Department of Microbiology, College of Natural Sciences, Chonnam National University
Bibliography Korean Journal of Microbiology, 30(6),519-523, 1992
DOI
Key Words Candida tsukubaensis, glucoamylase
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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