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Substrate Specificity of the Magnolia Flower Polyphenol Oxidase Separated on the Cation Exchanger and Hydrophobic Interaction Column
- Authors
- Kim, Jae-Joon; Kim, Woo-Yeon
- Issue Date
- Dec-2013
- Publisher
- KOREAN SOC APPLIED BIOLOGICAL CHEMISTRY
- Keywords
- Cation exchanger; Magnolia flower polyphenol oxidase; Substrate specificity
- Citation
- JOURNAL OF THE KOREAN SOCIETY FOR APPLIED BIOLOGICAL CHEMISTRY, v.56, no.6, pp 755 - 757
- Pages
- 3
- Journal Title
- JOURNAL OF THE KOREAN SOCIETY FOR APPLIED BIOLOGICAL CHEMISTRY
- Volume
- 56
- Number
- 6
- Start Page
- 755
- End Page
- 757
- ISSN
- 1738-2203
2468-0842
- Abstract
- Polyphenol oxidase (PPO) was separated from Magnolia (Magnolia kobus) flower by acetone precipitation and CM-Sepharose and Phenyl-Sepharose chromatographies. Molecular weight of the purified PPO from Magnolia flower was assumed to be just over 20 kDa on the sodiumdodecylsulfate-polyacrylamide gel electrophoresis and around 40 kDa under non-boiling without beta-mercaptoethanol. Magnolia flower PPO showed the highest enzyme activity with chlorogenic acid as a substrate.
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