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

Meynier, Anne; Rampon, Vincent; Dalgalarrondo, Michèle; Génot, Claude

doi:10.1016/j.idairyj.2004.01.003

Cited by 104 publications

(88 citation statements)

References 28 publications

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“…L'origine de ces différences n'a pu être clairement déterminée. Elle pourrait être liée à des réac-tions de composés, notamment les aldéhydes insaturés, avec certains acides aminés des protéines [4,6,43], ou à une formation privilégiée de certains composés dans l'une ou l'autre condition réactionnelle. Toutefois, ces hypothèses ne suffisent pas à expliquer l'ensemble des différences observées, aucun lien n'ayant pu être établi avec les mécanismes de formation des composés ou leur fonction chimique.…”

Section: Formation Des Composés Volatilsunclassified

Approche physico-chimique et sensorielle de l’oxydation des lipides en émulsions

Villière

Génot

2006

OCL

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Section: Formation Des Composés Volatilsunclassified

Approche physico-chimique et sensorielle de l’oxydation des lipides en émulsions

Villière

Génot

2006

OCL

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“…The inhibition was even more marked when amounts of volatile compounds typical of secondary products of lipid oxidation, such as alkanals, 2-alkenal and 2,4-alkadienals, were considered. As the decreases in volatile amounts were low when the peptides were added to the already oxidized liposomes, interactions or reactions of the volatiles with the peptides [43], reducing their release from the liposomes during dynamic headspace analysis, can hardly explain the observed inhibition. β-Casein tryptic hydrolysate and β-caseinophosphopeptide (f1-25) inhibited, on the hourly scale, the formation of both primary (conjugated dienes) and secondary (TBARS and volatile compounds, particularly alkanals and 2-alkenals) products of lipid oxidation when the degradation of PL liposomes was initiated by the iron-ascorbate redox mixture.…”

Section: Discussionmentioning

confidence: 99%

?-Caseinophosphopeptide (f1-25) confers on ?-casein tryptic hydrolysate an antioxidant activity during iron/ascorbate-induced oxidation of liposomes

Kansci

Génot²,

Meynier³

et al. 2004

Lait

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-Protein ingredients such as hydrolysates of milk proteins may improve the nutritive value of functional foods. For instance, β-casein tryptic hydrolysate could simultaneously increase iron absorption and prevent lipid oxidation in foods containing high contents of polyunsaturated fatty acids (PUFA). The aim of this study was to determine the antioxidant activity of β-casein tryptic hydrolysate and of its β-caseinophosphopeptide (f1-25) on Fe(III)/ascorbate-induced oxidation of muscle phospholipids in a liposome system. Oxygen consumption, conjugated dienes (CD), thiobarbituric acid reactive substances (TBARS) and volatile compounds were measured during oxidation at 25 °C of the liposomes in the presence of either the β-casein tryptic hydrolysate (0.24-2.4 mg·mL -1 ) or of its phosphopeptide (0.1-0.31 mg·mL -1 ). Oxygen consumption was significantly enhanced in the presence of β-casein tryptic hydrolysate or of the phosphopeptide (f1-25) and staircase curves were observed for the highest concentrations, showing complex oxidative interactions between iron, β-casein tryptic hydrolysate or phosphopeptide and the phospholipids. In contrast, on an hourly scale, formation of CD, TBARS and total volatile compounds were inhibited. The inhibition of CD and TBARS reached 50% after 20 h of oxidation in the presence of 1.2 mg·mL -1 β-casein tryptic hydrolysate or 0.16 mg·mL -1 phosphopeptide (f1-25). Amounts of total volatile compounds produced after 24 h decreased by about 60% in the presence of the hydrolysate (1.2 mg·mL -1 ) and 50% with the phosphopeptide (f1-25) (0.31 mg·mL -1 ) due to drastic decrease or even disappearance of alkanals and 2-alkenals. Several alcohols such as pentanol and hexanol were produced in higher amounts. Thus β-casein tryptic hydrolysate can protect rich-in-PUFA phospholipid liposomes against long-term iron-induced oxidation, mainly due to iron chelation by β-caseinophosphopeptide (f1-25). This antioxidant activity could benefit specific food products.

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“…Covalent and irreversible binding of trans-2-hexenal to whey protein was evidenced by fluorescence spectroscopy, suggesting the addition of the double bond to the imidazole ring of histidyl residues and the reaction of carbonyl groups with the free amine of lysyl residues via the Michael addition pathway (Meynier et al, 2004). By heating an aqueous solution containing thiols and disulphides in the presence of egg albumin, Mottram et al (1996) obtained a disulphide (2-furanmethyl disulphide) exchange and formation of the corresponding thiol.…”

Section: Nature and Strength Of The Interactionsmentioning

confidence: 99%

Interaction of aroma compounds with food matrices

Guichard¹

2015

Flavour Development, Analysis and Perception in Food and Beverages

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

Cited by 104 publications

References 28 publications

Approche physico-chimique et sensorielle de l’oxydation des lipides en émulsions

Approche physico-chimique et sensorielle de l’oxydation des lipides en émulsions

?-Caseinophosphopeptide (f1-25) confers on ?-casein tryptic hydrolysate an antioxidant activity during iron/ascorbate-induced oxidation of liposomes

Interaction of aroma compounds with food matrices

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