Purification and characterization of polyphenol oxidase from fresh ginseng
- Authors
- Kim, J.-J.; Kim, W.-Y.
- Issue Date
- Jan-2013
- Publisher
- Elsevier B.V.
- Keywords
- Carboxymethyl-sepharose; Catechol; Panax ginseng; Polyphenol oxidase; Purification
- Citation
- Journal of Ginseng Research, v.37, no.1, pp 117 - 123
- Pages
- 7
- Journal Title
- Journal of Ginseng Research
- Volume
- 37
- Number
- 1
- Start Page
- 117
- End Page
- 123
- URI
- https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/19830
- DOI
- 10.5142/jgr.2013.37.117
- ISSN
- 1226-8453
2093-4947
- Abstract
- Polyphenol oxidase (PPO) was purified from fresh ginseng roots using acetone precipitation, carboxymethyl (CM)-Sepharose chromatography, and phenyl-Sepharose chromatography. Two isoenzymes (PPO 1 and PPO 2) were separated using an ion-exchange column with CM-Sepharose. PPO 1 was purified up to 13.2-fold with a 22.6% yield. PPO 2 bound to CM-Sepharose, eluted with NaCl, and was purified up to 22.5-fold with a 17.4% yield. PPO 2 was further chromatographed on phenyl-Sepharose. The molecular weight of the purified PPO 2 from fresh ginseng was determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and was about 40 kDa. The optimum temperature and pH were 20°C and 7.0, respectively, using catechol as a substrate. Pyrogallol showed the highest substrate specificity. The effect of a PPO inhibitor showed that its activity increased slightly in the presence of a low concentration of citric acid. High concentrations of acidic compounds and sulfite agents significantly inhibited purified ginseng PPO 2. © The Korean Society of Ginseng.
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Collections - College of Biotechnology & Natural Resource > Department of Systems Biotechnology > 1. Journal Articles
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