폴리비닐 말콜 분해균 Pseudomonas cepaia G5Y의 Polyvinyl alcohol oxidase 정제 및 특성

Purification and characteristics of the Polyvinyl Alcohol Oxidase from Pseucomonas cepacia G5Y

  • 장대균 (영남대학교 응용미생물학과) ;
  • 조윤래 (영남대학교 응용미생물학과)
  • 발행 : 1995.05.01

초록

The Polyvinyl alcohol (PVA) oxidase is a key enzyme involved in degradation of PVA with PVA hydrolase. The PVA oxidase has been purified to homogeneity from the culture broth of PVA grown Pseudomonas cepacia G5Y strain by ammonium sulfate precipitation, DEAE-cellulose column chromatography, and Sephadex G-150 gel filtration. The molecular weight of the purified enzyme was estimated about 60, 000 daltons by SDS-polyacrylamid gel electrophoresis. The enzyme is most active at 45$\circ$C and at pH 8.5, and is stable below 55$\circ$C and between pH 6 and 9. The enzyme activity was strongly inhibited by Ag$^{2+}$ and Hg$^{2+}$.

키워드

참고문헌

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