Y. Oda et K. Tonomura, PURIFICATION AND CHARACTERIZATION OF INVERTASE FROM TORULASPORA-PRETORIENSIS-YK-1, Bioscience, biotechnology, and biochemistry, 58(6), 1994, pp. 1155-1157
Invertase was purified from Torulaspora pretoriensis YK-1 by acid trea
tment and column chromatography on DEAE-Togopearl 650M and phenyl-Toyo
pearl 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 wei
ght as carbohydrate. Properties of the invertase from T. pretoriensis
was similar to external invertase from Saccharomyces cerevisiae.