Intermediary and/or advanced Maillard products exhibit prooxidant activity on Trp: In vitro study on α-lactalbumin

Pușcașu, Cristina Gabriela; Birlouez‐Aragon, Inès

doi:10.1016/s0308-8146(01)00334-x

Cited by 20 publications

(9 citation statements)

References 27 publications

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“…The ϵ-NH 2 group from W has been shown to be able to participate in Maillard reactions 93 . In addition, W may be further degraded by oxidative species 30 which are generated during Maillard reactions 134 . The oxidative degradation of W via Maillard reaction products is also termed glycoxidation (glycation and oxidation).…”

Section: Effect Of Processing Conditions On W Stability and Bioactivitymentioning

confidence: 99%

“…W glycoxidation only appears to occur in native -La. This may arise from the fact that W residues within heat-denatured -La are not easily accessible 35 to radicals due to the formation of -La aggregates 134 . Similarly, the effect of lipid-derived oxidative products on the reduced bioavailability of W (-27.9%) from whey proteins following storage at 37C for 4 weeks has been reported 133 .…”

Section: Effect Of Processing Conditions On W Stability and Bioactivitymentioning

confidence: 99%

“…93 In addition, W may be further degraded by oxidative species which are generated during Maillard reactions. 134 The oxidative degradation of W via Maillard reaction products is also termed glycoxidation (glycation and oxidation). W glycoxidation only appears to occur in native α-La.…”

Section: Effect Of Processing Conditions On W Stability and Bioactivitymentioning

confidence: 99%

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Milk proteins as a source of tryptophan-containing bioactive peptides

Nongonierma

Fitzgerald

2015

Food Funct.

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Tryptophan (W) is an essential amino acid which is primarily required for protein synthesis. It also acts as 5 a precursor of key biomolecules for human health (serotonin, melatonin, tryptamine, niacin, nicotinamide adenine dinucleotide (NAD), phosphorylated NAD (NADP), quinolinic acid, kynureric acid, etc.). Among dietary proteins, milk proteins are particularly rich in W. W residues within milk proteins may be released by proteolytic/peptidolytic enzymes either as a free amino acid or as part of peptide sequences. Different W-containing peptides originating from milk proteins have been shown in vitro to display a 10 wide range of bioactivities such as angiotensin converting enzyme (ACE) inhibition along with antioxidant, antidiabetic and satiating related properties. Free W has been shown in certain instances to have an effect on cognition and the aforementioned bioactive properties. However, a higher bioactive potency has generally been observed with specific W-containing peptides compared to free W. Since W is thermolabile, the impact of processing on the stability of W-containing peptides needs to be considered. 15Milk protein-derived W-containing peptides may have significant potential as natural health promoting agents in humans.

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Section: Effect Of Processing Conditions On W Stability and Bioactivitymentioning

confidence: 99%

Section: Effect Of Processing Conditions On W Stability and Bioactivitymentioning

confidence: 99%

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Milk proteins as a source of tryptophan-containing bioactive peptides

Nongonierma

Fitzgerald

2015

Food Funct.

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“…In particular, the role of vitamin C degradation products on the development of the Maillard reaction (Leclère et al, 2002) and radical reactions initiated by the ironvitamin C mixture (Stadtman, 1991;Almaas et al, 1997) have been reported. The loss of protein digestibility (Rowley and Richardson, 1985;Jelen and Rattray, 1995), the decrease in the bioavailability of several essential amino acids (particularly lysine and tryptophan), and formation of undesirable compounds such as carboxymethyllysine (Birlouez-Aragon et al, 2004) could be explained by vitamin C-derived Maillard reaction (Leclère et al, 2002;Puscasu and Birlouez-Aragon, 2002).…”

Section: Introductionmentioning

confidence: 99%

Effects of Sterilization, Packaging, and Storage on Vitamin C Degradation, Protein Denaturation, and Glycation in Fortified Milks

Gliguem

Birlouez-Aragon

2005

Journal of Dairy Science

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Monitoring the nutritional quality of dietetic milk throughout its shelf life is particularly important due to the high susceptibility of some vitamins to oxidation, and the continuous development of the Maillard reaction during storage. The objective of this paper was to evaluate the vitamin C content and protein modification by denaturation and glycation on fortified milk samples (growth milks) destined for 1- to 3-yr-old children. The influences of the sterilization process, formulation, packaging, and storage duration at ambient temperature in the dark were studied. Vitamin C degradation was particularly influenced by type of packaging. The use of a 3-layered opaque bottle was associated with complete oxidation of vitamin C after 1 mo of storage, whereas in the 6-layered opaque bottle, which has an oxygen barrier, the vitamin C content slowly decreased to reach 25% of the initial concentration after 4 mo of storage. However, no significant effect of vitamin C degradation during storage could be observed in terms of Maillard reaction, despite the fact that a probable impact occurred during sterilization. Furosine content and the FAST (fluorescence of advanced Maillard products and soluble tryptophan) index-indicators of the early and advanced Maillard reaction, respectively-were significantly higher in the in-bottle sterilized milk samples compared with UHT samples, and in fortified milk samples compared with cow milk. However, after 1 mo, the impact of storage was predominant, increasing the furosine level and the FAST index at similar levels for the differently processed samples. The early Maillard reaction developed continuously throughout the storage period.In conclusion, only packaging comprising an oxygen and light barrier is compatible with vitamin C fortification of milk. Furthermore, short storage time or low storage temperature is needed to retard vitamin C degradation, protein denaturation, and development of the Maillard reaction.

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“…Added iron and ascorbic acid appear to have a particularly destructive effect on tryptophan in dairy systems. It is hypothesized that the main pathway for tryptophan destruction under mild heating conditions is not direct glycation of the indole N but a consequence of oxidation due either to the activity of the Fe-ascorbate system or the pro-oxidant activity of Maillard reaction products following ascorbylation of lysine "-NH 2 groups (Puscasu and Birlouez-Aragon, 2002;Leclère et al, 2002). The presence of oxygen is particularly detrimental under such conditions (Gliguem and Birlouez-Aragon, 2005).…”

Section: Immunoassaysmentioning

confidence: 99%

Non-Enzymatic Degradation Pathways of Lactose and Their Significance in Dairy Products

O’Brien

2009

Advanced Dairy Chemistry

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Intermediary and/or advanced Maillard products exhibit prooxidant activity on Trp: In vitro study on α-lactalbumin

Cited by 20 publications

References 27 publications

Milk proteins as a source of tryptophan-containing bioactive peptides

Milk proteins as a source of tryptophan-containing bioactive peptides

Effects of Sterilization, Packaging, and Storage on Vitamin C Degradation, Protein Denaturation, and Glycation in Fortified Milks

Non-Enzymatic Degradation Pathways of Lactose and Their Significance in Dairy Products

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