Purification and partial characterization of external and internal invertases from two strains of trichosporon adeninovorans

Abstract We investigated the extracellular and intracellular invertase activity of two Trichosporon adeninovorans strains. Both strains (SBUG 724 and CBS 2844) secrete one invertase into the medium. The external enzymes were purified by chromatography on hydroxylapatite. The molecular weight of the external invertase of SBUG 724 was found to be 650,000 and of CBS 2844 450,000. The internal invertases were separated by DEAE‐cellulose chromatography. The molecular weight of the enzyme from CBS 2844 was estimated to be 125,000. In the strain SBUG 724 we found two internal invertases (M r 230,000 and 70,000). The activity of all invertases has similar properties. The pH optimum of the reaction was determined between 5.0 and 5.2 and the temperature optimum was 60 to 70°C. The K m value for sucrose was determined to be 71 to 83 mM and for raffinosc 27 to 36 mM.