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KMID : 0370219960400010065
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Yakhak Hoeji
1996 Volume.40 No. 1 p.65 ~ p.71
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Effects of Amino Acids on the Inhibition of Polyphenol Oxidase Activity from Perillae Folium
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박수선/Park SS
김안근/손은수/Kim AK/Sohn ES
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Abstract
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Characterization of Polyphenol oxidase (PPO) in Perillae Folium, particullarly inhibitor studies were investigated. This enzyme was stable at pH 5.0 and the residual activity of PPO at >or= ph 5.5 was estimated to be very low. PPO activity was decreased slightly by adding amino acid with catechol as a substrate, particullary PPO activity was inhibited markedly by cystein, histidine, lysine and arginine. In the absorption spectra of the product formed when catechol was oxidized by PPO, with a ramdamax at 410nm, the peak shifted toward ramdamax 520nm by addition of L-proline. At relatively low concentrations(10-3M), sulfite and dithiothreithol completely inhibited PPO activity. Inhibition of PPO activity by amino acids and inhibitors increased or decreased depending on the pH used to measure it.
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KEYWORD
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