Development of Free Radical Products during the Greening Reaction of Caffeic Acid Esters (or Chlorogenic Acid) and a Primary Amino Compound

Namiki, Mitsuo; Yabuta, Goro; Koizumi, Yukimichi; Yano, Midori

doi:10.1271/bbb.65.2131

Cited by 39 publications

(51 citation statements)

References 12 publications

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“…Quinone-quinone interactions preceded protein binding and led to the formation of dimeric and higher molecular weight condensation products [23], [45]. Moreover, polymerized phenolics were found to be more reactive toward proteins [46]. The latter data are in agreement with the type of interaction observed in complexes formed at low protein/polyphenol ratios in our study.…”

Section: Resultssupporting

confidence: 91%

A New Look on Protein-Polyphenol Complexation during Honey Storage: Is This a Random or Organized Event with the Help of Dirigent-Like Proteins?

2013

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Honey storage initiates melanoidin formation that involves a cascade of seemingly unguided redox reactions between amino acids/proteins, reducing sugars and polyphenols. In the process, high molecular weight protein-polyphenol complexes are formed, but the mechanism involved remains unknown. The objective of this study was twofold: to determine quantitative and qualitative changes in proteins in honeys stored for prolonged times and in different temperatures and to relate these changes to the formation of protein-polyphenol complexes. Six -month storage decreased the protein content by 46.7% in all tested honeys (t-test, p<0.002) with the rapid reduction occurring during the first three month. The changes in protein levels coincided with alterations in molecular size and net charge of proteins on SDS –PAGE. Electro-blotted proteins reacted with a quinone-specific nitro blue tetrazolium (NBT) on nitrocellulose membranes indicating that quinones derived from oxidized polyphenols formed covalent bonds with proteins. Protein-polyphenol complexes isolated by size-exclusion chromatography differed in size and stoichiometry and fall into two categories: (a) high molecular weight complexes (230–180 kDa) enriched in proteins but possessing a limited reducing activity toward the NBT and (b) lower molecular size complexes (110–85 kDa) enriched in polyphenols but strongly reducing the dye. The variable stoichiometry suggest that the large, “protein-type” complexes were formed by protein cross-linking, while in the smaller, “polyphenol-type” complexes polyphenols were first polymerized prior to protein binding. Quinones preferentially bound a 31 kDa protein which, by the electrospray quadrupole time of flight mass spectrometry (ESI-Qtof-MS) analysis, showed homology to dirigent-like proteins known for assisting in radical coupling and polymerization of phenolic compounds. These findings provide a new look on protein-polyphenol interaction in honey where the reaction of quinones with proteins and polyphenols could possibly be under assumed guidance of dirigent proteins.

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Section: Resultssupporting

confidence: 91%

A New Look on Protein-Polyphenol Complexation during Honey Storage: Is This a Random or Organized Event with the Help of Dirigent-Like Proteins?

2013

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“…The results partly support an initial dimerization of chlorogenic acid (5-caffeoyl quinic acid or CQA) upon oxidation in the model system containing N-BOC-Lys as proposed by Prigent et al (2003). Furthermore, this leads to the formation of an adduct assigned to be a benzacridine derivative according to a mechanism described by Namiki et al (2001). The reaction of NAc-Cys with enzymatically generated CQA produced two adducts containing one and two N-Ac-Cys moieties (Schilling et al 2008) (Fig.…”

Section: Reactions With Amino Acids and Proteinssupporting

confidence: 69%

“…The magnitude of pigmentation strongly depends on the nature of the factor, its structure, and other parameters, such as pH, transition-metal, and solvent concentration (Kunsagi-Mate et al 2007). Different colored products ranging from yellow, pink, red, green, brown, to black can be produced during the reaction of oxidized chlorogenic/ caffeic acid and proteins or amines depending on the conditions applied (Pierpoint 1966(Pierpoint , 1969bCater et al 1972;Namiki et al 2001;Yabuta et al 2001;Kroll et al 2003). Similarly, the addition of certain amino acids (tryptophan, histidine, cysteine, and cystine) to model solutions of caffeic acid and hydroxytyrosol (the two most characteristic o-diphenols of ripe olives) improved the dark color obtained after oxidation (Romero et al 1998).…”

Section: Reactions With Amino Acids and Proteinsmentioning

confidence: 99%

Nature of hydroxycinnamate-protein interactions

2009

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In the context of this review the type and nature of possible interactions between hydroxycinnamates and proteins are discussed. These interactions can be classified in two sub-groups: non-covalent and covalent interactions. A short introduction is given on different sites of possible interactions. The first part of the article then focuses mainly on such reactions of phenolic substances with proteins and enzymes that lead to covalent bonds and thus to their derivatization respectively consequent cross-linking reactions. The corresponding postulated reaction mechanisms in the literature are also described. Effects on physicochemical, structural and techno-functional properties of the modified proteins are discussed, with consequent impact on their digestibility and subsequently on their nutritional quality. The second part incorporates the chemistry behind the (non-covalent) binding potential of the hydroxycinnamates to proteins. The different aspects of the nutritional-physiological consequences of such interactions with focus on their significance to food science and technology are presented. This review finally summarizes the development of potential new research strategies in this field.

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“…For all protein-GCE and protein-5-CQA interactions, a shift from green to red pigments was observed or the content of red pigments rose. Increased content of red pigments may be caused by the formation of new structures between amino acids and radical semiquinones derived from HCAs, which result in the formation of browning reaction products [40]. Among all products of protein-HCA interactions, the slightest color changes were caused by addition of HCAs in the form of inclusion complexes with β-CD.…”

Section: Color Of Proteins After Interactions With Hcasmentioning

confidence: 99%

Changes in properties of food proteins after interaction with free and β-cyclodextrin encapsulated hydroxycinnamic acids

Budryn

Zaczyńska

Rachwał-Rosiak

2015

Eur Food Res Technol

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Development of Free Radical Products during the Greening Reaction of Caffeic Acid Esters (or Chlorogenic Acid) and a Primary Amino Compound

Cited by 39 publications

References 12 publications

A New Look on Protein-Polyphenol Complexation during Honey Storage: Is This a Random or Organized Event with the Help of Dirigent-Like Proteins?

A New Look on Protein-Polyphenol Complexation during Honey Storage: Is This a Random or Organized Event with the Help of Dirigent-Like Proteins?

Nature of hydroxycinnamate-protein interactions

Changes in properties of food proteins after interaction with free and β-cyclodextrin encapsulated hydroxycinnamic acids

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