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 β-mercaptoethanol. Magnolia flower PPO showed the highest enzyme activity with chlorogenic acid as a substrate.
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