Characterization of Acid Phosphatase from Welsh Onion

파의 Acid Phosphatase의 특성

  • Kim, Gi-Nahm (Department of Food Science and Nutrition, Dong-A University) ;
  • Kim, Suk-Ji (Department of Food Science and Nutrition, Dong-A University) ;
  • Kim, Seok-Hwan (Department of Food Science and Nutrition, Dong-A University) ;
  • Park, In-Shik (Department of Food Science and Nutrition, Dong-A University)
  • 김기남 (동아대학교 식품영양학과) ;
  • 김석지 (동아대학교 식품영양학과) ;
  • 김석환 (동아대학교 식품영양학과) ;
  • 박인식 (동아대학교 식품영양학과)
  • Published : 1996.08.30

Abstract

Acid phosphatase (EC 3.1.3.2) from Welsh onion was partially purified by Sephacryl S-200 gel filtration and CM-Sepharose CL-6B ion exchange chromatography. The optimum pH and temperature of acid phosphatase from green onion were pH 5.5 and $60^{\circ}C$, respectively. The enzyme was the most stable at pH 6.0 and unstable above pH 9.0. The activation energy of the enzyme was determined to be 4.86kcal/mole. The enzyme utilized p-nitrophenyl phosphate most as a best substrate among tested possible substrates, while 5'-GMP and 5'-IMP were poor substrates for the enzyme. $K_{m.app.}$ of the enzyme with p-nitrophenyl phosphate as a substrate was identified as 0.87mM. Among metal ions and inhibitors tested, $Cr^{+++},\;Zn^{++},\;Cu^{++}$, molybdate and metavanadate ions inhibited the enzyme reaction drastically.

Keywords

welsh onion;acid phosphatase;characterization