Partial Purification of Fig Pectinesterase and Characterization of its in situ Activity

무화과 펙틴에스테라제의 부분 정제 및 in situ 상태에서의 활성 특성

  • Hou, Won-Nyoung (Department of Horticultural Crops Breeding, Mokpo National University) ;
  • Kim, Myoung-Hwa (Department of Horticultural Crops Breeding, Mokpo National University) ;
  • Go, Eun-Kyoung (Department of Horticultural Crops Breeding, Mokpo National University)
  • 허원녕 (국립 목포대학교 원예육종학과) ;
  • 김명화 (국립 목포대학교 원예육종학과) ;
  • 고은경 (국립 목포대학교 원예육종학과)
  • Published : 1998.10.01

Abstract

This study was performed to purify fig pectinesterase(F-PE) and characterize its in situ activity. Three kinds of F-PE were partially separated by using ammonium sulfate fractionation, Q-Sepharose column, CM-cation exchanger column chromatography, and HPLC. One of those was anionic protein and the others were cationic proteins. All of them had approximate molecular weight of 27,000 and lost rapidly their activity during storage. Therefore alternative crude enzyme was prepared by suspending the freeze dried and milled fig powder in 0.1 M NaCl at pH 7.5. F-PE had the optimum pH of 8.5, the optimum temperature of $50^{\circ}C$ with activation energy of 7,671 cal $mol^{-1}K^{-1}$ and stability up to $55^{\circ}C$ with 10 minutes heating. Optimum activity was obtained in $0.2{\sim}0.4$ M NaCl with optimum solubility at above 0.8 M NaCl.

Keywords

fig;pectinesterase;activation energy;in situ activity