Characterization of extracellular fructosyl transferase from aureobasidium pullulans C-23

Aureobasidium pullulans C-23이 생산하는 세포외 fructosyl transferase의 특성

  • 이광준 (충북대학교 자연과학대학 미생물학과) ;
  • 최정도 (충북대학교 자연과학대학 생화학과) ;
  • 임재윤 (충북대학교 자연과학대학 미생물학과)
  • Published : 1991.11.01


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 5mM $Hg^{2+}$ , 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.


Fructosyl transferase;Aureobasidium pullulans;Fructo-oligosaccharides