Purification and Properties of $\beta$-Fructofuranosidase

마늘(Allium sativum L.)로부터 추출한 $\beta$-Frucdtofuranosidase의 정제 및 성질

  • 이종수 (배재대학교 유전공학과) ;
  • 권수진 (배재대학교 유전공학과) ;
  • 이성훈 (배재대학교 유전공학과) ;
  • 유진영 (한국 식품개발연구원 생물공학연구부)
  • Published : 1998.02.01

Abstract

A $\beta$-fructofuranosidase of garlic (Allium sativum L. ; Seosan) was purified by ammonium sulfate fractionation and gel filtration chromatography with a recovery of 8.3%. The molecular mass of the purified enzyme was estimated to be 79kDa by SDS-PAGE, which revealed two subunits of 41kDa and 38kDa. Maximum enzyme activity was observed at pH 5.0 and 40$^\circ C$ and the enzyme was stable over the pH range of 4.0-6.0 and below 50$^\circ C$. The Km value for sucrose was 15.5mM and the enzyme activity was significantly inhibited by bivalent metal ions(Hg$^2+$, Cu$^2+$, Cd$^2+$) and EDTA.

Keywords

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