Comparative Studies on Immobilized Invertase on Sepharose and Phenoxyacetyl Cellulose

Sepharose와 Phenoxyacetyl Cellulose에 고정화 시킨 Invertase에 관한 비교 연구

  • Choi, Choon-Soon (Department of Food Science and Technology, Gwangju Health Junior College) ;
  • Jeon, Moon-Jin (Department of Agricultrual Chemistry, Korea University) ;
  • Byun, Si-Myung (Department of Biological Science and Engineering, The Korea Advanced Institute of Science)
  • 최춘순 (광주보건전문대학 식품제조과) ;
  • 전문진 (고려대학교 농화학과) ;
  • 변시명 (한국과학원 생물공학과)
  • Published : 1980.09.30


Yeast invertase was immobilized on the 2 kinds of matrices : one is an indirectly coupled enzyme to the cyanogen bromide activated Sepharose by using ${\omega}-aminohexyl$ group as an extension arm, and the other is a tightly adsorbed enzyme on the modified hydrophobic cellulose derivative which has a phenoxyacetyl group as a linkage. The enzyme preparation coupled on Sepharose retained 26.0% of the original activity against sucrose as a substrate, while the preparation immobilized on phenoxyacetyl cellulose retained 72.9% . The immobilized invertase preparation on ${\omega}-aminohexyl$ Sepharose showed the optimal pH 4.5, optimal temperature $60^{\circ}C$, activation energy $5,941\;cal/mole{\cdot}deg$ and Km' 22.2 mM against sucrose, while the preparation adsorbed on phenoxyacetyl cellulose showed the optimal pH 4.0, optimal temperature $60^{\circ}C$, activation energy $7,769\;cal/mole{\cdot}deg$ and Km' 69.9 mM.