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KMID : 0903519870300030278
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Journal of the Korean Society of Agricultural Chemistry and Biotechnology
1987 Volume.30 No. 3 p.278 ~ p.284
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Characteristics and Inhibition of Polyphenol Oxidase from Fuji Apples
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최언호/Choi, Eon Ho
정동선/조남숙/심영현/Jung, Dong Sun/Cho, Nam Sook/Shim.Young Hyun
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Abstract
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As a basic research for inhibition of enzymatic browning of apples during dehydration or processing, polyphenol oxidase was extracted from Fuji apples to investigate heat inactivation, chemical inhibition and other properties. Polyphenol oxidase showed the highest activity at 20℃ and pH 5.5 with catechol as substrate, and the Michaelis constant of 0.14 M under the same condition of substrate and pH. The thermal inactivation followed pseudo first-order kinetics to have activation energy of 23.0 k㎈/㏖ and z value of 19.7℃. As for substrate specificity the polyphenol oxidase showed high affinity toward the o-diphenolic compounds, particularly chlorogenic acid. Neither the m- and p-dihydroxy phenols nor monophenols were attacked. Browning by polyphenol oxidase was completely inhibited at the concentrations of l0mM for potassiummetasulfite and thiourea and 1mM for L-cysteine, ascorbic acid and sodium diethyldithiocarbarnate.
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KEYWORD
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