Comparative LC–MS/MS profiling of free and protein-bound early and advanced glycation-induced lysine modifications in dairy products

Hegele, Jörg; Buetler, Timo M.; Delatour, Thierry

doi:10.1016/j.aca.2007.12.027

Cited by 100 publications

(97 citation statements)

References 39 publications

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“…One of the metabolites-P6-was identifieda sp yrraline (10)b yc omparisonw ith as tandard and by its characteristic UV and product ion spectra. Fragmentation reactions of the compound weres imilart ot hose found for other N-substituted 5-hydroxymethyl-1H-pyrrole-2-carbaldehyde derivatives, such as dehydration (m/z 254!236), and dehydration/decarbonylation [34] (m/z 254!208; m/z 254!190). P2 had ap rotonated pseudo-molecular ion ([M+ +H] + )a t m/z 256.…”

Section: Transformation Of Dipeptide-bound Glycated Amino Acidssupporting

confidence: 52%

Transformation of Free and Dipeptide‐Bound Glycated Amino Acids by Two Strains of Saccharomyces cerevisiae

et al. 2016

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The yeast Saccharomyces cerevisiae transforms branched-chain and aromatic amino acids into higher alcohols in the Ehrlich pathway. During microbiological culturing and industrial fermentations, this yeast is confronted with amino acids modified by reducing sugars in the Maillard reaction (glycation). In order to gain some preliminary insight into the physiological "handling" of glycated amino acids by yeasts, individual Maillard reaction products (MRPs: fructosyllysine, carboxymethyllysine, pyrraline, formyline, maltosine, methylglyoxal-derived hydroimidazolone) were administered to two strains of S. cerevisiae in a rich medium. Only formyline was converted into the corresponding α-hydroxy acid, to a small extent (10 %). Dipeptide-bound pyrraline and maltosine were removed from the medium with concomitant emergence of several metabolites. Pyrraline was mainly converted into the corresponding Ehrlich alcohol (20-60 %) and maltosine into the corresponding α-hydroxy acid (40-60 %). Five specific metabolites of glycated amino acids were synthesized and characterized. We show for the first time that S. cerevisiae can use glycated amino acids as a nitrogen source and transform them into new metabolites, provided that the substances can be transported across the cell membrane.

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Section: Transformation Of Dipeptide-bound Glycated Amino Acidssupporting

confidence: 52%

Transformation of Free and Dipeptide‐Bound Glycated Amino Acids by Two Strains of Saccharomyces cerevisiae

et al. 2016

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“…5 and 8) were only lightly modified with a molar GA:bLG ratio of 1:1. The respective lysine loss, determined by LC-MS/MS [28], was 80-90% for batches 1 and 2, 30% for batch 3 and 3-10% for batches 4, 5 and 6. Between 1 and 6% of the lost lysine was accounted for by the appearance of CML, whereas pyrraline and fructoselysine were not detectable (data not shown).…”

Section: Resultsmentioning

confidence: 99%

“…We attempted to characterize the modifications introduced by GA but could only detect small quantities of CML but no pyrraline or fructoselysine. We did not analyze for other modifications as our analytical method is restricted to the detection and quantification of these modified amino acids [28]. Spanneberg et al [31] recently described the glycation of gelatin by GA.…”

Section: Discussionmentioning

confidence: 99%

“…The solution was sterile filtered and incubated at 501C for 48 h. The solution was extensively diafiltered (Pellicon Labscale, Millipore, Switzerland) against water to remove residual GA and the protein was recovered by lyophilisation after determination of the protein concentration spectrophotometrically using a NanoDrop ND1000 (Witec, Littau, Switzerland). The extent of glycation (lysine loss) as well as the composition of the modified amino acids CML, pyrraline and fructoselysine was determined as described previously [28].…”

Section: Generation Of Ga-modified Blgmentioning

confidence: 99%

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Glycolaldehyde‐modified β‐lactoglobulin AGEs are unable to stimulate inflammatory signaling pathways in RAGE‐expressing human cell lines

Buetler

Latado

Leclerc

et al. 2010

Molecular Nutrition Food Res

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“…First, a Schiff Base or a lactosylamine is formed, which is further converted to the Amadori product lactulosylamine [2]. During prolonged heating, further glycation products can be formed such as N e -carboxymethyllysine, oxalic acid monolysinylamide, pyrraline, or pentosidine [3][4][5][6]. Furthermore, heating in the presence of lactose can induce protein oxidation leading to the formation of methionine sulfoxide, aminoadipic semialdehyde, or dityrosine [7][8][9][10].…”

Section: Introductionmentioning

confidence: 98%

Assessment of heat treatment of dairy products by MALDI‐TOF‐MS

Meltretter

Birlouez-Aragon²,

Becker

et al. 2009

Molecular Nutrition Food Res

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The formation of the Amadori product from lactose (protein lactosylation) is a major parameter to evaluate the quality of processed milk. Here, MALDI-TOF-MS was used for the relative quantification of lactose-adducts in heated milk. Milk was heated at a temperature of 70, 80, and 100 degrees C between 0 and 300 min, diluted, and subjected directly to MALDI-TOF-MS. The lactosylation rate of alpha-lactalbumin increased with increasing reaction temperature and time. The results correlated well with established markers for heat treatment of milk (concentration of total soluble protein, soluble alpha-lactalbumin and beta-lactoglobulin at pH 4.6, and fluorescence of advanced Maillard products and soluble tryptophan index; r=0.969-0.997). The method was also applied to examine commercially available dairy products. In severely heated products, protein pre-purification by immobilized metal affinity chromatography improved spectra quality. Relative quantification of protein lactosylation by MALDI-TOF-MS proved to be a very fast and reliable method to monitor early Maillard reaction during milk processing.

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Comparative LC–MS/MS profiling of free and protein-bound early and advanced glycation-induced lysine modifications in dairy products

Cited by 100 publications

References 39 publications

Transformation of Free and Dipeptide‐Bound Glycated Amino Acids by Two Strains of Saccharomyces cerevisiae

Transformation of Free and Dipeptide‐Bound Glycated Amino Acids by Two Strains of Saccharomyces cerevisiae

Glycolaldehyde‐modified β‐lactoglobulin AGEs are unable to stimulate inflammatory signaling pathways in RAGE‐expressing human cell lines

Assessment of heat treatment of dairy products by MALDI‐TOF‐MS

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