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polyphenol/ジャガイモ

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Purification and characterization of polyphenol oxidase from waste potato peel by aqueous two-phase extraction.

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Potato peel from food industrial waste is a good source of polyphenol oxidase (PPO). This work illustrates the application of an aqueous two-phase system (ATPS) for the extraction and purification of PPO from potato peel. ATPS was composed of polyethylene glycol (PEG) and potassium phosphate buffer.

Inactivation of Potato Polyphenol Oxidase Using Microwave Cold Plasma Treatment.

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This study was conducted to examine the effects of microwave cold plasma (CP) treatment on inactivation of polyphenol oxidase (PPO) of potato. The PPO activity and treatment variables were fit to first-order kinetics, the Weibull model, and the second-order model. The optimum CP-generation power and

Inhibition of potato polyphenol oxidase by anions and activity in various carboxylate buffers (pH 4.8) at constant ionic strength.

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The activity of potato polyphenol oxidase (tyrosinase) toward DL-3,4-dihydroxyphenylalanine (K(M) 5.39 mM) was studied using a variety of carboxylate buffers at a common pH and ionic strength. Enzyme activity, greatest in citrate and least in oxalate, correlated with increasing carboxyl

Purification of Polyphenol Oxidase from Potato and Investigation of the Inhibitory Effects of Phenolic Acids on Enzyme Activity.

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Polyphenol oxidase (PPO) belongs to the oxidoreductase enzyme family.Here, PPO was purified from potato using Sepharose 4B-L-tyrosine-p-aminobenzoic acid affinity chromatography. It determined the interactions between some phenolic acids and the

Pyridine and other coal tar constituents as inhibitors of potato polyphenol oxidase: a non-animal model for neurochemical studies.

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Potato polyphenol oxidase activity was strongly and noncompetitively inhibited by the "Perov mixture" of coal tar components and by pyridine alone, while phenol competitively inhibited the enzyme. These two inhibitors are structural components of the parkinsonogenic neurotoxin

A new insight into purification of polyphenol oxidase and inhibition effect of curcumin and quercetin on potato polyphenol oxidase.

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In the literature, the polyphenol oxidase (PPO) enzyme has been purified a many times via Sepharose 4B-l-tyrosine-p-aminobenzoic acid affinity column. In order to study PPO purification efficiency, 2-aminophenol and 4-aminophenol were applied as a spacer arm to CNBr-activated Sepharose 4B. The

Biological performance of Colorado potato beetle larvae on potato genotypes with differing levels of polyphenol oxidase.

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Two potato genotypes resistant to the Colorado potato beetle (CPB) and three susceptible genotypes were used to investigate the role of total foliar polyphenol oxidase (PPO) on the performance of CPB larvae in long-term feeding assays. A significant positive correlation was found between larval

Degradation of pentachlorophenol by potato polyphenol oxidase.

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In this study, polyphenol oxidase (PPO) was extracted from commercial potatoes. Degradation of pentachlorophenol by potato PPO was investigated. The experimental results show that potato PPO is more active in weak acid than in basic condition and that the optimum pH for the reaction is 5.0. The

The In Vitro Antioxidant Activity and Inhibition of Intracellular Reactive Oxygen Species of Sweet Potato Leaf Polyphenols.

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The in vitro antioxidant activity and inhibition of intracellular reactive oxygen species (ROS) of the total and individual phenolic compounds from Yuzi No. 7 sweet potato leaves were investigated in this study. Sweet potato leaf polyphenols possessed significantly higher antioxidant activity than

Purification, kinetic parameters, and isoforms of polyphenol oxidase from "Xushu 22" sweet potato skin

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We purified and compared the polyphenol oxidase (PPO) isoenzymes present in "Xushu 22," a sweet potato. A membrane-bound form (mPPO) and two soluble forms (sPPO1 and sPPO2) were identified and purified using ammonium sulphate precipitation, ion exchange chromatography, gel filtration chromatography,

Screening, separating, and completely recovering polyphenol oxidases and other biochemicals from sweet potato wastewater in starch production.

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Polyphenol oxidase (PPO) has multiple functions, and the lack of commercially available enzyme sources limits its widespread application in various industries. An accurate PPO assay was developed by HPLC determination of the substrate oxidation. Resources screening indicated that sweet potato
Effects of high hydrostatic pressure (100, 200, and 400 MPa) and soaking solution (citric acid, calcium chloride, ascorbic acid, and distilled water) on proximate composition, polyphenols, anthocyanins, β-carotene, and antioxidant activity of white, orange, and purple fleshed sweet potato flour were

Potato and mushroom polyphenol oxidase activities are differently modulated by natural plant extracts.

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Enzymatic browning is a major quality issue in fruit and vegetable processing and can be counteracted by different natural inhibitors. Often, model systems containing a single polyphenol oxidase (PPO) are used to screen for new inhibitors. To investigate the impact of the source of PPO on the

Polarity of Production of Polyphenols and Development of Various Enzyme Activities in Cut-injured Sweet Potato Root Tissue.

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Investigation of polyphenol production in cut-injured sweet potato (Ipomoea batatas Lam. cv. Kokei 14) roots by histochemical and quantitative methods showed that polyphenols were produced in striking amounts in the proximal side of the tissue pieces (2 cm thick), but only in small amounts in cells
This work reports the development and application of a multi-compound analysis method for the determination of 17 flavonoids and polyphenols in sweet potato leaves. Samples were processed by microwave-enhanced accelerated solvent extraction under low pressure at 120 °C for 10 min. Salting-out
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