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Purification and properties of intracellular fructosyl transferase fromAureobasidium pullulans

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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 Hg2+ 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.

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Lee, K.J., Choi, J.D. & Lim, J.Y. Purification and properties of intracellular fructosyl transferase fromAureobasidium pullulans . World J Microbiol Biotechnol 8, 411–415 (1992). https://doi.org/10.1007/BF01198756

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  • DOI: https://doi.org/10.1007/BF01198756

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