Hexanal and t-2-hexenal form covalent bonds with whey proteins and sodium caseinate in aqueous solution

Autor: Anne Meynier, Michèle Dalgalarrondo, Claude Genot, V. Rampon
Přispěvatelé: ProdInra, Migration, Laboratoire d'étude des interactions des molécules alimentaires, Institut National de la Recherche Agronomique (INRA)
Jazyk: angličtina
Rok vydání: 2004
Předmět:
Zdroj: International Dairy Journal
International Dairy Journal, Elsevier, 2004, 14, pp.681-690
ISSN: 0958-6946
Popis: In food systems, a reduction of aroma intensity can occur in presence of proteins by hydrophobic or covalent interactions. The aim of this paper was to identify the nature of the interactions of aldehydes in flavoured dairy media. The addition of either hexanal or t-2-hexenal to whey proteins and sodium caseinate dissolved in water caused a rapid and substantial decrease in the maximum intensity of fluorescence of the tryptophanyl residues of the proteins (Trp). The decrease was proportional to the aldehyde concentration and probably due to quenching of the Trp fluorescence but was also associated with appearance of new fluorophores, which exhibited spectral characteristics depending on the aldehyde added. The proportion of Lys residues decreased with both aldehydes, while the His proportion decreased with t-2-hexenal. The covalent binding of t-2-hexenal to milk proteins therefore had a large effect on its partitioning between the liquid and the gaseous phase whilst that of hexanal was less important.
Databáze: OpenAIRE