Purification and Characterization of Invertase from Torulaspora pretoriensis YK-1
1994 年 58 巻 6 号 p. 1155-1157
詳細
1994 年 58 巻 6 号 p. 1155-1157
Invertase was purified from Torulaspora pretoriensis YK-1 by acid treatment and column chromatography on DEAE-Toyopearl650M and phenyl-Toyopearl 650M to homogeneity. The molecular weight of the purified enzyme was estimated to be 130, 000 by SDS-polyacrylamide gel electrophoresis and 530, 000 by gel filtration. The enzyme contained 50% molecular weight as carbohydrate. Properties of the invertase from T. pretoriensis was similar to external invertase from Saccharomyces cerevisiae.
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