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KMID : 0364819910290050301
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Korean Journal of Microbiology
1991 Volume.29 No. 5 p.301 ~ p.306
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Characterization of Extracellular Fructosyl Transferase from Aureobasidium pullulans C-23
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Abstract
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1
Extracellular fructosyl transferase from Aureobasidium pullulans C-23 was characterized. The molecular weight of the isolated enzyme was determined to be approximately 170,000 by SDS polyacrylamide gel electrophoresis. The enzyme has the pI value of about 3.7. The enzyme was almost completely inhibited by 5 mM Hg", but was not significantly affected by other cations tested. The enzyme was inactivated by treatment of tryptophan-specific reagent N-bromo- succinimide and tyrosine-specific reagent iodine. The substrate sucrose showed protective effect on the inactivation of the enzyme by the both reagents. These results suggest that tryptophan and tyrosine residues are probably located at or near active site of the enzyme.
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