Characterization of wheat o-diphenolase isoenzyme

Interesse, Francesco S.; Ruggiero, P.; D'Avella, Gerolmina; Lamparelli, Francesco

doi:10.1016/0031-9422(83)80006-5

Cited by 16 publications

(11 citation statements)

References 32 publications

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“…Consequently, this fraction, referred herein as PPO-al, was used for further characterization. It is of interest here to note that similar acidic PI values have been reported for polyphenol oxidases from potato tubers (Matheis and Belitz 1975) and olives (Ben-Shalom et al 1977), while wheat PPO was found to have a PI of 9.6 (Interesse et al 1983).…”

Section: Deae-sepharose Cl-4b Chromatographysupporting

confidence: 79%

“…The PPO-al contained high levels of glycine, followed by alanine and glutamic acid/glutamine. A comparison of our data with those reported for potato (Balasingam and Ferdinand 1970) and wheat (Interesse et al 1983) PPO indicated that there is a similarity in composition for all three enzymes as related to their contents of hydrophobic and sulfur amino acids. On the other hand, the artichoke PPO-al is distinguished from the other two enzymes by the greater residue content of glycine and alanine and the lower content of basic (lysine, arginine, histidine) amino acids.…”

Section: Amino Acid Compositionsupporting

confidence: 72%

“…interest further to note that the content of part of the hydrophobic residues (proline, valine, isoleucine, leucine, and phenylalanine) of the artichoke PPO (30.3%) lies at the crossover point (30.0%) between single chain (nonassociating) and multichain (associating) proteins (Jolley et al 1969). These data could thus account, at least in part, for the tendency of this enzyme to form multimeric aggregates (Zawistowski et al 1987).…”

Section: After Fractionation By Deae-sepharose Ion-exchange Chromatogmentioning

confidence: 92%

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Isolation and Some Properties of an Acidic Fraction of Polyphenol Oxidase From Jerusalem Artichoke(helianthus Tuberosus L.)

Zawistowski

Βiliaderis

Murray

1988

J Food Biochemistry

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An acidic fraction of polyphenol oxidase (EC 1.14.18.1), representing the bulk activity, has been isolated from Jerusalem artichoke tubers by copper affinity chromatography, followed by DEAE‐Sepharose ion‐exchange chromatography. Isoelectric focusing analysis showed a cluster of activity bands (microheterogeneity) in the pH region of 4.5. The amino acid composition of the enzyme was also determined. The pH optimum for oxidation of chlorogenic acid, 4‐methylcatechol and catechol was 6.0. Substrate inhibition was observed by high concentrations of chlorogenic acid. Thermal inactivation data indicated an apparent activation energy of 26.2 kcal/mol. Kinetics of inactivation, upon copper removal by KCN treatment, and reconstitution reactions revealed that the former is a much slower process than reactivation.

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Section: Deae-sepharose Cl-4b Chromatographysupporting

confidence: 79%

Section: Amino Acid Compositionsupporting

confidence: 72%

Section: After Fractionation By Deae-sepharose Ion-exchange Chromatogmentioning

confidence: 92%

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Isolation and Some Properties of an Acidic Fraction of Polyphenol Oxidase From Jerusalem Artichoke(helianthus Tuberosus L.)

Zawistowski

Βiliaderis

Murray

1988

J Food Biochemistry

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“…This is consistent with previous studies regarding the influence of protein on Chinese noodle color (Lang et al, 1998; Habernicht et al, 2002). Although protein can be an important determinant of color in an alkaline noodle (Miskelly, 1996), the higher pH of the alkaline noodle formula is closer to the optimum for polyphenol oxidase activity (Interesse et al, 1983). A number of studies have shown that polyphenol oxidase activity is related to the degree of time‐dependent discoloration of noodles (Kruger et al, 1994; Baik et al, 1995; Park et al, 1997).…”

Section: Discussionmentioning

confidence: 99%

Influence of Genotype, Environment, and Nitrogen Management on Spring Wheat Quality

et al. 2004

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Bread baking is the primary end‐use criterion used to select hard spring wheat (Triticum aestivum L.) genotypes for the northwestern USA, yet the use of hard wheats has expanded beyond traditional pan breads to include Asian noodles. We assessed the relative influence of genotype, N management, and location on quality characteristics of a set of spring wheat cultivars that provided a range in gluten strength and acceptability for bread and Asian noodle quality, and determined whether grain characteristics could predict bread and/or noodle market suitability. Seven spring cultivars were grown at four locations across 3 yr with two levels of N fertilizer in irrigated and moisture‐limited conditions. Bread quality, alkaline noodle color, and Chinese noodle color and texture were assessed on grain samples. Cultivar was the most important determinant of bread and noodle quality traits in both the irrigated and moisture‐limited environments. Nitrogen level influenced only Chinese noodle color in irrigated environments, but impacted test weight, flour ash, loaf volume, and bake absorption in moisture‐limited environments. Responses to N management and location were usually not cultivar specific, as interactions were not important relative to main effects of cultivar and location. Grain protein had more value than test weight or grain hardness in predicting bread and noodle quality, and was most useful in predicting loaf volume and Chinese noodle color characteristics. Cultivar selection is critical for achieving a desired end use, with location effects being of secondary importance. Nitrogen management for a particular end use will be difficult, with N level being much less important than cultivar selection and location. Grain protein may be the best predictor of the suitability of a particular cultivar produced in a specific year for alternative end‐use possibilities, with high‐protein grain most suitable for bread production and low‐protein, high‐quality grain more suitable for noodle production.

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“…Polyphenol oxidases isolated from food sources are oligomers and contain one copper prosthetic group per subunit [7]. Similar to other properties, the quaternary structure of PPO also differs with the source of the enzyme [8][9][10]. PPO enzymes react with the phenolic substrates, the aromatic ring of the phenolic compounds binds to the enzyme active center.…”

Section: Introductionmentioning

confidence: 99%

Properties of wheat bran polyphenol oxidase

Soysal

Söylemez²

2004

Nahrung

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Polyphenol oxidase (PPO) obtained from wheat bran catalyzed the oxidation of 4-methyl catechol. Phenolic compounds found naturally in crude extract played role as an endogeneous substrate and activity of crude extract needed correction. Activity versus enzyme concentration gave a linear plot at high substrate concentration whereas a nonlinear plot was obtained at low substrate concentration which proved the presence of endogeneous substrate. Adsorption on celite and extraction with polyvinylpyrrolidone (PVPP) caused the removal of phenols. Adsorption of PPO on celite yielded a 4-fold increase in specific activity whereas extraction with PVPP yielded a 2.5-fold increase in specific activity compared to the crude extract. The kinetics of PPO catalyzed oxidation obeyed Michaelis-Menten model; Km and Vmax values were found as 218 mM and 99 microM/min, respectively. The enzyme was inhibited by ethyl alcohol, dithiothreitol (DTT) and isoproterenol and exhibited heat stability up to a temperature of 90 degrees C. The optimum pH of the enzyme was found to be 5.0.

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Characterization of wheat o-diphenolase isoenzyme

Cited by 16 publications

References 32 publications

Isolation and Some Properties of an Acidic Fraction of Polyphenol Oxidase From Jerusalem Artichoke(helianthus Tuberosus L.)

Isolation and Some Properties of an Acidic Fraction of Polyphenol Oxidase From Jerusalem Artichoke(helianthus Tuberosus L.)

Influence of Genotype, Environment, and Nitrogen Management on Spring Wheat Quality

Properties of wheat bran polyphenol oxidase

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