Interactions between globular proteins and procyanidins of different degrees of polymerization
| Autor: | Alain Baron, Catherine M.G.C. Renard, S.V.E. Prigent, Harry Gruppen, G.A. van Koningsveld, Alphons G. J. Voragen |
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| Přispěvatelé: | Wageningen University and Research Centre (WUR), Station de Recherches Cidricoles et Biotransformation des Fruits et Légumes (SRC - BFL), Institut National de la Recherche Agronomique (INRA), Sécurité et Qualité des Produits d'Origine Végétale (SQPOV), Avignon Université (AU)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE) |
| Jazyk: | angličtina |
| Rok vydání: | 2009 |
| Předmět: |
[SDV.SA]Life Sciences [q-bio]/Agricultural sciences
binding Polymers PROTEIN POLYPHENOL PROANTHOCYANIDIN ISOTHERMAL TITRATION CALORIMETRY VEGETABLES TANNINS CALORIMETRIE TITRATION ISOTHERME polymérisation 01 natural sciences Oligomer Catechin chemistry.chemical_compound bovine serum-albumin Organic chemistry Solubility 2. Zero hunger chemistry.chemical_classification milk Food Chemistry haze formation additif Air Temperature 04 agricultural and veterinary sciences Hydrogen-Ion Concentration grape acidité 040401 food science Agricultural sciences products quality propriété physicochimique Dietary Proteins Lysozyme nutrition humaine condensed tannins Protein Binding émulsion Globular protein Protein digestion Calorimetry 0404 agricultural biotechnology precipitating capacity température Levensmiddelenchemie Polymer chemistry Genetics Biflavonoids Proanthocyanidins polyphenols VLAG Osmolar Concentration 010401 analytical chemistry Water Isothermal titration calorimetry fruit légume 0104 chemical sciences produit alimentaire Isoelectric point chemistry Ionic strength Food Technology Animal Science and Zoology Dairy Products Sciences agricoles Food Science |
| Zdroj: | Journal of Dairy Science Journal of Dairy Science, American Dairy Science Association, 2009, 92 (12), pp.5843-5853. ⟨10.3168/jds.2009-2261⟩ Journal of Dairy Science, 92, 5843-5853 Journal of Dairy Science 12 (92), 5843-5853. (2009) Journal of Dairy Science 92 (2009) |
| ISSN: | 0022-0302 |
| DOI: | 10.3168/jds.2009-2261⟩ |
| Popis: | Interactions of proteins with phenolic compounds occur in food products containing vegetable sources, such as cocoa, cereals, or yogurts containing fruit. Such interactions can modify protein digestion and protein industrial properties. Noncovalent interactions between globular proteins (proteins important in industry) and procyanidins (phenolic compounds present in large quantity in fruits) were studied. The affinity constants between procyanidins of various average degrees of polymerization ( DP ¯ ) and lysozyme or α-lactalbumin were measured by isothermal titration calorimetry. The effects of these interactions on protein solubility and foam properties were examined using α-lactalbumin and BSA. Weak interactions were found with epicatechin and procyanidin dimers. Procyanidins of DP ¯ n=5.5 and DP ¯ n=7.4 showed medium (1.5×10 5 M −1 ) and high (8.69×10 9 M −1 ) affinities, respectively, for α-lactalbumin at pH 5.5, with n the average number of subunits per oligomer. A positive cooperativity of binding at low procyanidin:protein molar ratios was observed. The affinities of α-lactalbumin and lysozyme for procyanidins increased when the pH was close to the isoelectric pH. Solubility of lysozyme was strongly decreased by procyanidins of DP ¯ n=5.5, whereas α-lactalbumin and BSA were less affected. Protein solubility in the presence of procyanidins was not affected by increased ionic strength but increased slightly with temperature. Procyanidins of DP ¯ n=5.5 and DP ¯ n=7.4 stabilized the average bubble diameter of foam formed with α-lactalbumin but had no effect on foam made from BSA. These results indicate that procyanidins of medium DP ¯ can lead to an undesirable decrease of protein solubility, but may play a positive role in foam stability. |
| Databáze: | OpenAIRE |
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