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Postharvest Biology and Technology
Yue-Ming, J., Dept. Postharvest Sci. Fresh Produce, Inst. Technol. Storage Agric. Prod., Volcani Center, P.O. Box 6, Bet Dagan 50250, Israel, Department of Plant Physiology, South China Institute of Botany, Academia Sinica, Guangzhou 510650, China
Zauberman, G., Dept. Postharvest Sci. Fresh Produce, Inst. Technol. Storage Agric. Prod., Volcani Center, P.O. Box 6, Bet Dagan 50250, Israel
Fuchs, Y., Dept. Postharvest Sci. Fresh Produce, Inst. Technol. Storage Agric. Prod., Volcani Center, P.O. Box 6, Bet Dagan 50250, Israel, Department of Plant Biology, 111 Koshland Hall, University of California Berkeley, Berkeley, CA 94720-3102, United States
Litchi (Litchi chinensis Sonn.) fruit peel polyphenol oxidase (PPO) was partially purified 21 fold by ammonium sulfate fractionation and gel filtration. Pyrogallol, catechol, and 4-methylcatechol were good substrates for the enzyme: with no activity observed with chlorogenic acid, p-cresol, resorcinol, or tyrosine. The optimal pH for PPO activity was 7.0 with 4-methylcatechol, with the enzyme being most stable at pH 7.4. The enzyme was relatively temperature stable with maximum activity at 70°C and requiring a little less than 10 min at 90°C for 50% loss of activity. The K(m) and V(max) for the enzyme, with 4-methylcatechol were 10 mM and 1.47 x 104 units/min per mg protein, respectively. The enzyme was not activated by SDS. Reduced glutalhione, L-cysteine, tropolone, thiourea, FeSO4 and SnCl2 markedly inhibited PPO activity, whereas MnSO4 and CaCl2 enhanced PPO activity. Data obtained in this study might help to better understand and control commercially, litchi fruit peel browning.
פותח על ידי קלירמאש פתרונות בע"מ -
הספר "אוצר וולקני"
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תנאי שימוש
Partial purification and some properties of polyphenol oxidase extracted from litchi fruit pericarp
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Yue-Ming, J., Dept. Postharvest Sci. Fresh Produce, Inst. Technol. Storage Agric. Prod., Volcani Center, P.O. Box 6, Bet Dagan 50250, Israel, Department of Plant Physiology, South China Institute of Botany, Academia Sinica, Guangzhou 510650, China
Zauberman, G., Dept. Postharvest Sci. Fresh Produce, Inst. Technol. Storage Agric. Prod., Volcani Center, P.O. Box 6, Bet Dagan 50250, Israel
Fuchs, Y., Dept. Postharvest Sci. Fresh Produce, Inst. Technol. Storage Agric. Prod., Volcani Center, P.O. Box 6, Bet Dagan 50250, Israel, Department of Plant Biology, 111 Koshland Hall, University of California Berkeley, Berkeley, CA 94720-3102, United States
Partial purification and some properties of polyphenol oxidase extracted from litchi fruit pericarp
Litchi (Litchi chinensis Sonn.) fruit peel polyphenol oxidase (PPO) was partially purified 21 fold by ammonium sulfate fractionation and gel filtration. Pyrogallol, catechol, and 4-methylcatechol were good substrates for the enzyme: with no activity observed with chlorogenic acid, p-cresol, resorcinol, or tyrosine. The optimal pH for PPO activity was 7.0 with 4-methylcatechol, with the enzyme being most stable at pH 7.4. The enzyme was relatively temperature stable with maximum activity at 70°C and requiring a little less than 10 min at 90°C for 50% loss of activity. The K(m) and V(max) for the enzyme, with 4-methylcatechol were 10 mM and 1.47 x 104 units/min per mg protein, respectively. The enzyme was not activated by SDS. Reduced glutalhione, L-cysteine, tropolone, thiourea, FeSO4 and SnCl2 markedly inhibited PPO activity, whereas MnSO4 and CaCl2 enhanced PPO activity. Data obtained in this study might help to better understand and control commercially, litchi fruit peel browning.
Scientific Publication
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