Use of Experimental Design Methodology To Prepare Maillard Reaction Products from Glucose and Cysteine Inhibitors of Polyphenol Oxidase from Eggplant (Solanum melongena)
Polyphenol oxidase (PPO) from eggplant was extracted and partially purified by a two-step fractionation−precipitation using ammonium sulfate and phenylsepharose hydrophobic interaction chromatography. The eggplant PPO extract was characterized concerning its kinetic properties. Optimal conditions to...
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Published in | Journal of agricultural and food chemistry Vol. 54; no. 14; pp. 5120 - 5126 |
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Main Authors | , , |
Format | Journal Article |
Language | English |
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American Chemical Society
12.07.2006
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Abstract | Polyphenol oxidase (PPO) from eggplant was extracted and partially purified by a two-step fractionation−precipitation using ammonium sulfate and phenylsepharose hydrophobic interaction chromatography. The eggplant PPO extract was characterized concerning its kinetic properties. Optimal conditions to obtain Maillard reaction products (MRPs) with a maximal inhibitory potency (IP) toward PPO activity were determined using the surface response methodology and a four-factor and five-level experimental design. The MRPs were prepared from cysteine (0.25 M) and glucose (0−1 M), at several initial pH values (2−6) and at differing heating times (3−19 h) and temperatures (95−115 °C). The maximal IP was obtained after heating a model system of glucose/cysteine (1/0.25 M) at pH 2 for 3 h 20 min at 115 °C. The soluble part of this MRP, called MRPIPmax, was a noncompetitive inhibitor toward eggplant PPO. The IP of MRPIPmax on PPO activity was very potent as compared to that displayed by benzoic, p-coumaric, and t-cinnamic acids, as well as sorbic acid and 4-hexylresorcinol. The activity of preincubated PPO at 0 °C with MRPIPmax was only slightly restored after dialysis or gel filtration. Keywords: Maillard reaction products; cysteine; eggplant; polyphenol oxidase; enzymatic browning |
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AbstractList | Polyphenol oxidase (PPO) from eggplant was extracted and partially purified by a two-step fractionation-precipitation using ammonium sulfate and phenylsepharose hydrophobic interaction chromatography. The eggplant PPO extract was characterized concerning its kinetic properties. Optimal conditions to obtain Maillard reaction products (MRPs) with a maximal inhibitory potency (IP) toward PPO activity were determined using the surface response methodology and a four-factor and five-level experimental design. The MRPs were prepared from cysteine (0.25 M) and glucose (0-1 M), at several initial pH values (2-6) and at differing heating times (3-19 h) and temperatures (95-115 degrees C). The maximal IP was obtained after heating a model system of glucose/cysteine (1/0.25 M) at pH 2 for 3 h 20 min at 115 degrees C. The soluble part of this MRP, called MRP(IPmax), was a noncompetitive inhibitor toward eggplant PPO. The IP of MRP(IPmax) on PPO activity was very potent as compared to that displayed by benzoic, p-coumaric, and t-cinnamic acids, as well as sorbic acid and 4-hexylresorcinol. The activity of preincubated PPO at 0 degrees C with MRP(IPmax) was only slightly restored after dialysis or gel filtration. Polyphenol oxidase (PPO) from eggplant was extracted and partially purified by a two-step fractionation-precipitation using ammonium sulfate and phenylsepharose hydrophobic interaction chromatography. The eggplant PPO extract was characterized concerning its kinetic properties. Optimal conditions to obtain Maillard reaction products (MRPs) with a maximal inhibitory potency (IP) toward PPO activity were determined using the surface response methodology and a four-factor and five-level experimental design. The MRPs were prepared from cysteine (0.25 M) and glucose (0-1 M), at several initial pH values (2-6) and at differing heating times (3-19 h) and temperatures (95-115 C). The maximal IP was obtained after heating a model system of glucose/cysteine (1/0.25 M) at pH 2 for 3 h 20 min at 115 C. The soluble part of this MRP, called MRPIPmax, was a noncompetitive inhibitor toward eggplant PPO. The IP of MRPIPmax on PPO activity was very potent as compared to that displayed by benzoic, p-coumaric, and t-cinnamic acids, as well as sorbic acid and 4-hexylresorcinol. The activity of preincubated PPO at 0 C with MRPIPmax was only slightly restored after dialysis or gel filtration. Polyphenol oxidase (PPO) from eggplant was extracted and partially purified by a two-step fractionation−precipitation using ammonium sulfate and phenylsepharose hydrophobic interaction chromatography. The eggplant PPO extract was characterized concerning its kinetic properties. Optimal conditions to obtain Maillard reaction products (MRPs) with a maximal inhibitory potency (IP) toward PPO activity were determined using the surface response methodology and a four-factor and five-level experimental design. The MRPs were prepared from cysteine (0.25 M) and glucose (0−1 M), at several initial pH values (2−6) and at differing heating times (3−19 h) and temperatures (95−115 °C). The maximal IP was obtained after heating a model system of glucose/cysteine (1/0.25 M) at pH 2 for 3 h 20 min at 115 °C. The soluble part of this MRP, called MRPIPmax, was a noncompetitive inhibitor toward eggplant PPO. The IP of MRPIPmax on PPO activity was very potent as compared to that displayed by benzoic, p-coumaric, and t-cinnamic acids, as well as sorbic acid and 4-hexylresorcinol. The activity of preincubated PPO at 0 °C with MRPIPmax was only slightly restored after dialysis or gel filtration. Keywords: Maillard reaction products; cysteine; eggplant; polyphenol oxidase; enzymatic browning |
Author | Cheriot, Sophie C Billaud, Catherine Nicolas, Jacques |
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Cites_doi | 10.1111/j.1365-2621.1999.tb15062.x 10.1007/s11746-001-0392-y 10.1021/jf990292r 10.1002/mnfr.200400101 10.1016/S0308-8146(02)00376-X 10.1016/S0308-8146(03)00207-3 10.1016/0308-8146(81)90048-0 10.1016/S0031-9422(00)82157-3 10.1046/j.1365-2621.2002.00580.x 10.1016/0924-2244(92)90131-F 10.1021/jf980928z 10.1021/jf00125a014 10.1002/(SICI)1097-0010(199904)79:5<750::AID-JSFA247>3.0.CO;2-A 10.1016/0003-9861(59)90090-6 10.1006/fstl.1996.0181 10.1080/10408399409527653 10.1002/jsfa.2740460111 10.1021/jf9607932 10.1021/jf026250b 10.1016/0003-2697(76)90527-3 |
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Keywords | Heat treatment Cysteine Vegetables Methodology enzymatic browning Catechol oxidase Glucose Eggplant Dicotyledones Angiospermae Carbohydrate polyphenol oxidase Solanaceae Solanum melongena Enzyme Reaction product Use Maillard reaction products Maillard reaction Browning Experimental design Aminoacid Spermatophyta Inhibitor Oxidoreductases Enzymatic reaction |
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Snippet | Polyphenol oxidase (PPO) from eggplant was extracted and partially purified by a two-step fractionation−precipitation using ammonium sulfate and... Polyphenol oxidase (PPO) from eggplant was extracted and partially purified by a two-step fractionation-precipitation using ammonium sulfate and... |
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SubjectTerms | Benzoic Acid - pharmacology Biological and medical sciences catechol oxidase Catechol Oxidase - antagonists & inhibitors Cinnamates - pharmacology Coumaric Acids - pharmacology cysteine Cysteine - chemistry eggplants enzymatic browning enzyme inhibition enzyme inhibitors Enzyme Inhibitors - chemistry Enzyme Inhibitors - pharmacology Food industries Fruit and vegetable industries Fundamental and applied biological sciences. Psychology glucose Glucose - chemistry Hot Temperature Hydrogen-Ion Concentration Maillard Reaction Maillard reaction products Propionates purification Solanum melongena Solanum melongena - enzymology Sorbic Acid - pharmacology Time Factors |
Title | Use of Experimental Design Methodology To Prepare Maillard Reaction Products from Glucose and Cysteine Inhibitors of Polyphenol Oxidase from Eggplant (Solanum melongena) |
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