Substrate specificity of the Magnolia flower polyphenol oxidase separated on the cation exchanger and hydrophobic interaction column

• Published in: Applied biological chemistry Vol. 56; no. 6; pp. 755 - 757
• Main Authors: Kim, Jae-Joon, Kim, Woo-Yeon
• Format: Journal Article
• Language: English
• Published: Dordrecht Springer Netherlands 01.12.2013; Springer Nature B.V; 한국응용생명화학회
• Subjects: Acetone; Applied Microbiology; Biological Techniques; Bioorganic Chemistry; Cation exchanging; Chemical precipitation; Chemistry; Chemistry and Materials Science; Chlorogenic acid; Electrophoresis; Enzymatic activity; Enzyme activity; Gel electrophoresis; Hydrophobicity; Molecular weight; Polyacrylamide; Polyphenol oxidase; Short Communication; Substrate specificity; Substrates; 농학; Magnolia flower polyphenol oxidase; Substrate specificity; Cation exchanger
• ISSN: 1738-2203; 2468-0834; 2234-344X; 2468-0842
• DOI: 10.1007/s13765-013-3223-5

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.