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- W1954376999 abstract "Polyphenol oxidase (PPO) was extracted from Jipicao yam grown in China, and its characteristic was studied. Among the various substrates employed, the Vmax/Km ratio indicated that PPO had the best affinity to catechol and the worst affinity to p-hydroxyphenylalanine. The optimum pH for this enzyme was 6.8, and the optimum temperature was 30C. When the temperature was lower than 60C, PPO was relatively stable. Fe3+ and Mg2+ improved the activity, while Ca2+, K+, Ba2+ and Mn2+ ions could significantly inhibit the activity. NaHSO3, Vc, L-cysteine, phytic acid, oxalic acid, citric acid and ethylenediaminetetraacetic acid-2Na had different inhibiting effects on the activity of PPO, and the former three were strong inhibitors of PPO activities. Practical Applications Our paper studied the properties of polyphenol oxidase (PPO) from Jipicao yam, including optimum temperature, optimum pH, thermal stability, substrate specificity and the effect of metal ions and inhibitors so as to select a reasonable method to restrain the activity of PPO, then providing a theoretical basis for inhibiting enzymatic browning that occurred during the process of manufacturing and storage to improve the nutritional value and exterior quality." @default.
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- W1954376999 date "2015-01-21" @default.
- W1954376999 modified "2023-09-23" @default.
- W1954376999 title "Characterization of Polyphenol Oxidase from Jipicao Yam" @default.
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- W1954376999 doi "https://doi.org/10.1111/jfbc.12117" @default.
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