Solubilization of the Red Beet Cell Wall Betanin Decolorizing Enzyme

Wasserman, Bruce P.; Guilfoy, Michael P.

doi:10.1111/j.1365-2621.1984.tb10395.x

Cited by 9 publications

(7 citation statements)

References 22 publications

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“…Such activity can be extracted by digestion of tissue slices of beet root with cellulase and pectinase, which suggest that it is located in the cell wall. (Waserman and Guilfoy, 1984). Despite this and other reports that point to an extracellular localization of this activity, the existence of a soluble Bt decolorizing activity in Amaranthus tricolor has been described (Elliot et al, 1983).…”

Section: Introductionmentioning

confidence: 93%

An Approach to the Characterization of Betanine Oxidation Catalyzed by Horseradish Peroxidase

Parra

Muñoz

1997

J. Agric. Food Chem.

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Horseradish peroxidase (HRP, EC 1.1.11.7) catalyzed oxidation of betanine is complex, as judged by the shape of the consecutive absorption spectra of the reaction medium. Graphic analysis of these spectra by a matricial test revealed the presence of at least three kinetically related absorbent species in the reaction mixture. Analysis by HPLC confirmed the presence of several reaction products. During the course of the reaction, a red intermediate and several yellow products, presumably of a polymeric nature, are generated, betalamic acid being one of the final products. Even in the absence of enzyme, the reaction, once initiated, continued again, yielding betalamic acid as a final product, which is formed as both substrate and intermediate product disappear. The chemical nature of the intermediate product and the possible reaction mechanism are discussed. Keywords: Beta vulgaris; betanine oxidation; peroxidase; red beet

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Section: Introductionmentioning

confidence: 93%

An Approach to the Characterization of Betanine Oxidation Catalyzed by Horseradish Peroxidase

Parra

Muñoz

1997

J. Agric. Food Chem.

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“…Considerable betalain decomposition may also result in the presence of betalain degrading enzymes. Both membrane‐bound and cell wall‐bound peroxidases were identified in red beet (Wasserman and Guilfoy 1984), the membrane‐bound peroxidase exhibiting a pH optimum of 3.4 (Wasserman and Guilfoy 1983). Interestingly, betacyanins were found to be more prone to degradation by peroxidases than betaxanthins, while the latter were more susceptible to chemical oxidation by hydrogen peroxide, as was proven by almost complete suppression of betaxanthin oxidation upon catalase addition (Wasserman and others 1984).…”

Section: Factors Governing Betalain Stabilitymentioning

confidence: 99%

Betalain Stability and Degradation—Structural and Chromatic Aspects

Herbach¹,

Stintzing²,

Carle³

2006

Journal of Food Science

504

349

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In recent years, food coloring with artificial colorants has been increasingly disapproved by consumers. In return, application of coloring foodstuffs, among them betalain‐containing fruits and vegetables, has gained importance for the food industry. As commonly true for natural pigments, betalains are afflicted with inferior stability compared to synthetic dyes. Especially temperature, oxygen, and light are known to exhibit detrimental effects on betalain integrity, while certain antioxidants and chelating agents may act as stabilizers. Only recently, several studies expanded the knowledge on betalain degradation pathways, especially focusing on betacyanin decomposition. Additionally, new findings on stability and stabilization of betalains in cactus fruit juices extended the application range of betalainic foodstuffs. Focusing on betacyanins, the present review discusses betalain degradation mechanisms and provides a survey of compounds and conditions governing betalain stability in a beneficial or an unfavorable way. Finally, strategies for maintaining the chromatic properties and tinctorial strength of betalain‐based juices and pigment preparations as well as tools for color modulation by targeted betacyanin degradation are discussed.

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“…Since the pioneering studies of Soboleva et al (), who described the occurrence of a betacyanin decolorizing enzymatic activity in red beets, a number of papers on the catabolism of betalains in Beta vulgaris ( − ) and Amaranthus tricolor () have been published. This decolorizing activity might be a peroxidase (EC 1.11.1.7), as can be deduced from the fact that betanin (Bt) decolorization by a red beet preparation is stimulated by H 2 O 2 ( , ). Moreover, horseradish peroxidase (HRP) can oxidize Bt ( , ).…”

Section: Introductionmentioning

confidence: 99%

Characterization of Betacyanin Oxidation Catalyzed by a Peroxidase fromBeta vulgarisL. Roots

Martínez-Parra

Muñoz

2001

J. Agric. Food Chem.

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A protein fraction with peroxidase (EC 1.11.1.7) activity against guaiacol from Beta vulgaris L. roots oxidized both betanidin and betanin (betanidin 5-O-beta-D-glucoside), the former being the more efficient substrate for the enzyme. The protein fraction contained three strongly basic perxidase isoenzymes. Betanidin quinone was formed as the only product in the course of enzymatic betanidin oxidation, whereas betalamic acid and several oxidized cyclo-DOPA 5-O-beta-D-glucoside polymers were generated during the oxidation of betanin. In accordance with the catalytic properties of peroxidase, a possible mechanism for betanidin oxidation is proposed. This mechanism includes the formation of a betanidin radical, which, by further dismutation, yields betanidin quinone and betanidin. The betanidin oxidation rate showed a Michaelis-type dependence on the substrate concentration. The apparent K(M) for the reaction was 0.46 mM. On the basis of the spectral properties of the enzyme responsible for both betanidin and betanin oxidations, its peroxidase nature is suggested.

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Solubilization of the Red Beet Cell Wall Betanin Decolorizing Enzyme

Cited by 9 publications

References 22 publications

An Approach to the Characterization of Betanine Oxidation Catalyzed by Horseradish Peroxidase

An Approach to the Characterization of Betanine Oxidation Catalyzed by Horseradish Peroxidase

Betalain Stability and Degradation—Structural and Chromatic Aspects

Characterization of Betacyanin Oxidation Catalyzed by a Peroxidase fromBeta vulgarisL. Roots

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