Interactions of globular protein with simple polyphenols

Neucere, Navin J.; Jacks, T. J.; Sumrell, Gene

doi:10.1021/jf60215a041

Cited by 31 publications

(20 citation statements)

References 11 publications

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“…A similar observation was also made during experiments concerning interactions of a globular protein (arachin) exposed to simple polyphenols (catechol and pyrogallol) and was attributed to the number of the introduced hydroxyl groups (Neucere et al, 1978). The interaction was thought to be of the hydrogen bond type, either through interpeptide chains or encompassing the phenols themselves (Neucere et al, 1978). Derivatization with myricetin causes a decrease in ␣-helix, with a parallel increase in ␤-strand and -turn.…”

Section: Characterization Of Structural Changes In Protein-phenolderisupporting

confidence: 56%

Reactions of Plant Phenolics with Food Proteins and Enzymes under Special Consideration of Covalent Bonds

Kröll

Rawel

Rohn

2003

FSTR

317

273

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Secondary plant metabolites are important native food components, which are becoming more and more interesting due to their physiological effects on human beings. One of the largest groups of these compounds is represented by plant phenols. This review summarizes the structure, classification and distribution of the phenolic compounds in plant foods, their chemistry and signification with regard to food processing and -storage as well as their physiological effects. This work focuses mainly on such reactions of the phenolic substances with proteins and enzymes that lead to covalent bonds. The derivatives formed have been characterized in terms of changes in their physicochemical and structural properties. The effect on the proteolytic in vitro digestion has been also illustrated. Further aspects reported include the influence on enzyme activity and -kinetic parameters. The different aspects of the nutritional-physiological consequences of such reactions in food and body, especially considering their significance to food science and technology are discussed.

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Section: Characterization Of Structural Changes In Protein-phenolderisupporting

confidence: 56%

Reactions of Plant Phenolics with Food Proteins and Enzymes under Special Consideration of Covalent Bonds

Kröll

Rawel

Rohn

2003

FSTR

317

273

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“…For instance, covalent interaction with CGA reduced the solubility of soy glycinin,61, 62 whose molecular structure largely resembles that of helianthinin. As for the covalent binding of CGA to proteins, non‐covalent binding has been reported to result in decreased protein solubility 63. A recent publication,64 however, reported the absence of decreased solubility of globular proteins in the presence of CGA by non‐covalent interactions, even at high CGA/protein ratios.…”

Section: Phenolic Compounds Of Sunflower Seedmentioning

confidence: 99%

“…As for the covalent binding of CGA to proteins, non-covalent binding has been reported to result in decreased protein solubility. 63 A recent publication, 64 however, reported the absence of decreased solubility of globular proteins in the presence of CGA by non-covalent interactions, even at high CGA/protein ratios.…”

Section: Phenolic Compounds Of Sunflower Seedmentioning

confidence: 99%

Sunflower proteins: overview of their physicochemical, structural and functional properties

2007

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There is increasing worldwide demand for proteins of both animal and plant origin. However, animal proteins are expensive in terms of both market price and environmental impact. Among alternative plant proteins, sunflower seeds are particularly interesting in view of their widespread availability in areas where soy is not or only sparsely produced. Compared with other sources of vegetable proteins, sunflower seeds have been reported to have a low content of antinutritional factors. Although the absence of these factors is important, the functionality of the protein preparations will mainly determine their applicability. This review provides detailed information about sunflower seed composition and processing, including processes to remove phenolic compounds from meals. The main part of the review concerns the structure and functionality of the two major protein fractions, helianthinin and 2S albumins. Regarding functionality, emphasis is on solubility, thermal behaviour and surface activity. Protein structure and functionality are discussed as a function of extrinsic factors such as pH, ionic strength, temperature and the presence of other seed components, particularly chlorogenic acid. In addition, sunflower proteins are compared from a structural and functional point of view with other plant proteins, particularly soy proteins.

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“…Principally, two types of interactions can be classified between phenolic compounds and proteins: covalent and non-covalent binding . With respect to hydroxycinnamates, much work has been directed towards the significance of these interactions in complex food matrices in order to improve the nutritional and functional quality of plant proteins (Neucere et al 1978;Sosulski 1979b;Friedman 1996aFriedman , b, 1997Tsai and She 2006;Gonzalez-Perez and Vereijken 2007). A series of studies demonstrates that this primarily refers to the role of the interactions of chlorogenic acid (CQA) with the seed proteins as observed in, for example sunflower (Cater et al 1972;Sabir et al 1974a, b;Davies et al 1978;Sosulski 1979a;Prasad 1988;Saeed and Cheryan 1989;Rao 1990, 1991;Suryaprakash et al 2000;Gonzalez-Perez et al 2002;Gonzalez-Perez and Vereijken 2007), or in canola (Rubino et al 1996b;Naczk et al 1998;Diosady 2000, 2002).…”

Section: Introductionmentioning

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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Interactions of globular protein with simple polyphenols

Cited by 31 publications

References 11 publications

Reactions of Plant Phenolics with Food Proteins and Enzymes under Special Consideration of Covalent Bonds

Reactions of Plant Phenolics with Food Proteins and Enzymes under Special Consideration of Covalent Bonds

Sunflower proteins: overview of their physicochemical, structural and functional properties

Nature of hydroxycinnamate-protein interactions

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