지원사업
학술연구/단체지원/교육 등 연구자 활동을 지속하도록 DBpia가 지원하고 있어요.
커뮤니티
연구자들이 자신의 연구와 전문성을 널리 알리고, 새로운 협력의 기회를 만들 수 있는 네트워킹 공간이에요.
논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 저널정보
- 한국식품영양과학회 Journal of Food Science and Nutrition Journal of Food Science and Nutrition Vol.1 No.1
- 발행연도
- 1996.6
- 수록면
- 111 - 116 (6page)
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초록· 키워드
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Polyphenol oxidase(PPO) isolated from the crude extract of ascidian, Halocynthia roretzi, showed higher affinity for catechol than tyrosine or DL-DOPA. Successful enzyme assay could be performed at 25℃, 10 min. by mixing 0.2ml of crude enzyme extract with 2.8ml of 0.13M catechol in 0.1M sodium phosphate buffer (pH 6.4). The specific activity of PPO which had been purified with a combination of ammonium sulfate treatment, ion exchange chromatography on DEAE-cellulose, and gel filtration on Sepharose 6B was 13-fold higher than that of crude extract. The purified enzyme was homogeneous as confirmed by polyacrylamide disc gel electrophoresis. The activity of PPO was stable from pH 5.0 to 8.0 and showed the peak activity at pH 6.4. The optimum reaction temperature for PPO oxidation on catechol was 35℃ and those enzyme were heat stable up to 40℃. Molecular weight of the enzyme was estimated about 170 kDa. One molecule was found to be composed of four subunits. Two of them had molecular weight of 55 kDa and the others 30 kDa. The K_m values, V_(max) and catalytic efficiency(V_(max)/K_m) for catechol were 0.12mM, 2.56mM/liter/min. and 0.18min^(-1) respectively. The substrate affinity and electrophorectic pattern suggested that the enzyme of ascidian was considered to be not tyrosine but catechol oxidase.
목차
Abstract
INTRODUCTION
MATERIALS AND METHODS
RESULTS AND DISCUSSION
ACKNOWLEDGEMENTS
REFERENCES
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UCI(KEPA) : I410-ECN-0101-2009-511-018072325