title: Purification and properties of intracellular fructosyl transferase fromAureobasidium pullulans.
abstract: Intracellular frustosyl transferase was purified fromAureobasidium pullulans C-23 by ethanol fractionation, CM-Sephadex chromatography and preparative disc gel electrophoresis. It was shown to be homogeneous on disc polyacrylamide gel electrophoresis, with a molecular size of 190kDa. The pI value of the enzyme was about 3.7. The enzyme has aK m value of 0.43 mM for sucrose and was optimally active at pH 5.0 and 60°C. The enzyme was stable from pH 2.5 to 12. It was almost completely inhibited by 5mM Hg(2+) but was not significantly affected by other cations. The transferase was inactivated by treatment with the tryptophan-specific reagentN-bromosuccinimide and the tyrosine-specific reagent, I2, suggesting that tryptophan and tyrosine residues are probably located at or near the active site of the enzyme.
authors.affiliation: Department of Microbiology, College of Natural Sciences, Chungbuk National University, 360-763, Cheong-ju, South Korea.
authors.forename: K J
authors.initials: KJ
authors.lastname: Lee
authors.forename: J D
authors.initials: JD
authors.lastname: Choi
authors.forename: J Y
authors.initials: JY
authors.lastname: Lim