Amadori Compounds Research Articles

Characterization and in Vitro Digestibility of Bovine β-Lactoglobulin Glycated with Galactooligosaccharides

Galactooligosaccharides (GOS) are well-known prebiotic ingredients which can form the basis of new functional dairy products. In this work, the production and characterization of glycated beta-lactoglobulin (beta-LG) with prebiotic GOS through the Maillard reaction under controlled conditions ( a(w) = 0.44, 40 degrees C for 23 days) have been studied. The extent of glycation of beta-LG was evaluated by formation of furosine which progressively increased with storage for up to 16 days, suggesting that the formation of Amadori compounds prevailed over their degradation. RP-HPLC-UV, SDS-PAGE, and IEF profiles of beta-LG were modified as a consequence of its glycation. MALDI-ToF mass spectra of glycated beta-LG showed an increase of up to approximately 21% in its average molecular mass after storage for 23 days. Moreover, a decrease in unconjugated GOS (one tri-, two tetra-, and one pentasaccharide) was observed by HPAEC-PAD upon glycation. These results were confirmed by ESI MS. The stability of the glycated beta-LG to in vitro simulated gastrointestinal digestion was also described and compared with that of the unglycated protein. The yield of digestion products of glycated beta-LG was lower than that observed for the unglycated protein. The conjugation of prebiotic carbohydrates to stable proteins and peptides could open new routes of research in the study of functional ingredients.

Formation Pathways and Opioid Activity Data for 3‐Hydroxypyridinium Compounds Derived from Glucuronic Acid and Opioid Peptides by Maillard Processes

The kinetics of formation and identity of the reaction products of the glucuronic acid with three representative opioid peptides were investigated in vitro. Peptides were conjugated with glucuronic acid either in solution or under dry-heating conditions. From the incubations performed in solution N-(1-deoxy-D-fructofuranos-1-yluronic acid)-peptide derivatives (Amadori compounds) were isolated, whereas from the dry-heated reactions products containing the 3-hydroxypyridinium moiety at the N-terminal of the peptide chain were obtained. Experiments performed under mild dry-heating conditions (40 degrees C) in model systems based on Leu-enkephalin and glucuronic acid, and in environment of either 40% or 75% relative humidity, revealed that the higher level of humidity promoted a process that enhanced 3-hydroxypyridinium compound generation. The mechanism of 3-hydroxypyridinium formation is discussed. In comparison with their respective parent peptides, the N-(1-deoxy-D-fructofuranosyl-uronic acid) derivatives of the opioid peptides showed three- to 11-fold lower mu- and delta-receptor-binding affinities and agonist potencies in the functional assays, likely as a consequence of the steric bulk introduced at the N-terminal amino group. The further decrease in opioid activity observed with the 3-hydroxypyridinium-containing peptides may be due to the lower pK(a) of the 3-hydroxypyridinium moiety and to delocalization of the positive charge in the pyridinium ring system.

1H, 13C, 195Pt NMR study on platinum(II) interaction with sulphur containing Amadori compounds

The NMR study on the interaction of Pt(II) with Amadori compounds is performed. The Amadori compounds are derived from the reaction of β- d-glucose with l-cystine leading to N, N′-di-(1-deoxy-β-fructos-1-yl)- l-cystine [FruCyscys], and with l-methionine leading to N-(1-deoxy-β-fructos-1-yl)- l-methionine [FruMet]. The great instability of 2-(1,2,3,4,5-pentahydroxypentyl)-1,3-thiazolidine-4-carboxylic acid [GlcCys], formed by the condensation reaction of β- d-glucose and l-cysteine, prevents the formation of its Pt(II) complexes. Differently, FruMet well reacts with K 2PtCl 4 in 1:1 M/L molar ratio leading to the formation of [Pt(FruMet- N, S)Cl 2], in which the Amadori compound coordinates the metal ion through nitrogen and sulphur atoms. FruMet originates also a solid trans complex [Pt(FruMet- N, S) 2]Cl 2. Its NMR solution study allowed to identify two isomers with respect to nitrogen and sulphur atoms: R, R and S, S. In [Pt 2FruCyscysCl 4] species, FruCyscys molecule links two Pt(II) ions giving rise to two pentaatomic N, S-chelate rings.

Forty years of furosine – Forty years of using Maillard reaction products as indicators of the nutritional quality of foods

The Maillard reaction products (MRPs) most widely used as markers of the nutritional quality of foods are furosine, N(epsilon)-carboxymethyllysine (CML), hydroxymethylfurfural, pyrraline, pentosidine and pronyl-lysine. One of the MRPs identified first was furosine, which was quantified in foods 40 years ago as a chemical indicator of the Amadori compound N(epsilon)-fructoselysine. Since then, furosine has gained broad attention by food chemists and biomedical researchers, as its formation upon heat treatment is well characterised. Moreover, it represents the Amadori products from early Maillard reactions in which amino acids react with reducing carbohydrates, resulting in a loss of their availability. This is of importance for the essential amino acid lysine, which is also the limiting amino acid in many proteins. In order to evaluate the nutritional quality of a protein, the concomitant analysis of free - and nutritionally available - lysine and the amount of lysine reacted to form the respective MRP is essential, even for mildly processed foods. The other chemical markers of heat treatment such as CML, pyrraline, pentosidine or pronyl-lysine seem to be useful markers of the advanced stages of Maillard reactions. Compared to the conditions in which furosine is formed, these compounds are generated under more severe conditions of heat treatment. However, the concentrations analysed are significantly lower than those of furosine. Therefore, the nutritional evaluation of a food protein should include not only furosine, but also other chemical markers of heat treatment such as, for example, CML, pyrraline and pentosidine.

Crystal structure of N-(1-deoxy-β- d-fructopyranos-1-yl)- l-proline—an Amadori compound

Here we report the crystal structure data on N-(1-deoxy-β- d-fructopyranos-1-yl)- l-proline (Fru-Pro)—an Amadori compound. X-ray crystal and molecular structures of its two isomorphous crystalline forms, (Fru-Pro)·MeOH, C 11H 19NO 7·CH 4O ( 1a) and (Fru-Pro)·2H 2O, C 11H 19NO 7·2H 2O ( 1b) were determined. In 1a and 1b the compound crystallizes as the β-anomer with the overall geometry of Fru-Pro zwitterions being very similar. Fructose ring adopts the chair 2 C 5 conformation with the proline moiety bonded to equatorial C-1 atom and remaining in a trans–gauche ( tg) orientation with respect to the sugar ring. The five-membered pyrrolidine ring adopts an envelope conformation, with the Cβ atom puckered. Fructosyl and carboxylate groups are in bisectional and axial positions of pyrrolidine ring, respectively. The overall molecular geometry of Fru-Pro zwitterions, especially the relative orientation of sugar and amino acid moieties, is stabilized by intramolecular, three-centred N–H⋯O Fru/O Pro hydrogen bonds (with bifurcated acceptor) formed between aminium and hydroxyl/carboxylate groups. The packing diagrams are very similar in both 1a and 1b with the adjacent zwitterions linked to each other by the extensive network of O–H⋯O and C–H⋯O hydrogen bonds to form channels along the a-axis, filled up with solvent molecules.

Separation of amino acids, peptides and corresponding Amadori compounds on a silica column at elevated temperature

Maillard reaction of glucose with amino acids and peptides has become a very important experimental model in the food flavor and pharmaceutical industries for better understanding the mechanism of food flavor generation and drug stability. Because of the amino acid and sugar functional groups present in their structures, most of the reaction components formed during the initial stages of Maillard reaction as well as the substrates are relatively polar. These compounds are poorly retained on a conventional reversed phase column. While polar stationary phases like HILIC column do provide better retention for these polar components, method selectivity could still be a challenge due to the structural similarity between these analytes. In this report, parameters such as pH, mobile phase composition and temperature were investigated using different brands of bare silica columns in order to separate glycine (G), diglycine (DG), triglycine (TG), and the corresponding Amadori compounds of glucose–glycine (GG), glucose–diglycine (GDG) and glucose–triglycine (GTG). An excellent separation for glycine, glycine peptides and their Amadori compounds was obtained on a bare silica column at an elevated temperature.

NMR study on Pt(II) interaction with Amadori compounds

Here we report the first evidence of Pt(II) interaction with Amadori compound [ N-(1-deoxy- d-Fructos-1-yl)glycine (Fru-Hgly)]. The 1H and 195Pt NMR results show that complexation of Pt(II) by Fru-Hgly is strongly dependent on pH and reaction molar ratio. In 1/1 Pt/Fru-Hgly molar ratio, at acidic pH, the first coordination site is the carboxylic oxygen, while at physiological pH the anchoring group is the aminic one, in both cases the system slowly evolves towards an N, O chelating mode. In 1/2 Pt/Fru-Hgly molar ratio the only coordination site is nitrogen atom while the carboxylic oxygen is not involved in metal coordination.

Solubility and crystal structure of N-(1-deoxy-β- d-fructopyranos-1-yl)- l-histidine monohydrate (‘ d-fructose- l-histidine’)

Within a set of food-related Amadori compounds, crystalline N-(1-deoxy-β- d-fructopyranos-1-yl)- l-histidine monohydrate (Fru- l-His × H 2O) has an unusually low solubility in water, which we determined as 0.21 g/100 g at 25 °C. The majority of the other fructose-amino acid conjugates have solubilities exceeding 100 g/100 g in water at this temperature. We report the crystal structure data on Fru- l-His × H 2O. The conformation of the carbohydrate is the normal 2C 5 pyranose chair. Bond lengths and valence angles compare well with the average values from a number of pyranose structures. All hydroxyl and carboxyl oxygen atoms, all nitrogen atoms and the water molecule are involved in an extensive hydrogen bonding, which forms a network of infinite chains with small antidromic rings.

Fragmentation behavior of glycated peptides derived from D‐glucose, D‐fructose and D‐ribose in tandem mass spectrometry

Nonenzymatic glycosylation (or glycation) is a common nonenzymatic side-chain specific sequence-independent posttranslational modification formed by the reaction of reducing carbohydrates with free amino groups. Thus, proteins can react with aldoses or ketoses to yield Amadori or Heynes compounds, respectively. Here, the fragmentation behavior of D-glucose and D-ribose-derived Amadori peptides as well as D-fructose-derived Heynes peptides were studied by collision-induced fragmentation (CID) after electrospray (ESI) or matrix-assisted laser desorption/ionization (MALDI) mass spectrometry (MS). All three sugar moieties displayed characteristic fragmentation patterns accompanying the parent and the fragment ions, which could be explained by consecutive losses of water and formaldehyde. Glucose-derived Amadori parent and fragment ions displayed losses of 18, 36, 54, 72, and 84 u at a characteristic intensity distribution compared with losses of 18, 36, 54, 72, 84, and 96 u for D-fructose-derived ions and losses of 18, 36, and 54 u for ribose-derived ions. Furthermore, each sugar moiety produced indicative lysine-derived immonium ions that were successfully used in a precursor ion scan analysis to identify Amadori peptides in a tryptic digest of bovine serum albumin (BSA) glycated with D-glucose. BSA was modified on lysine residues at positions 36, 160, 235, 256, 401, and 548.

Biodistribution and catabolism of 18F-labeled N-ε-fructoselysine as a model of Amadori products

Amadori products are formed in the early stage of the so-called Maillard reaction between reducing sugars and amino acids or proteins. Such nonenzymatic glycosylation may occur during the heating or storage of foods, but also under physiological conditions. N-epsilon-fructoselysine is formed via this reaction between the epsilon-amino group of peptide-bound lysine and glucose. Despite the fact that, in certain heated foods, up to 50% of lysyl moieties may be modified to such lysine derivatives, up to now, very little is known about the metabolic fate of alimentary administered Amadori compounds. In the present study, N-succinimidyl-4-[18F]fluorobenzoate was used to modify N-epsilon-fructoselysine at the alpha-amino group of the lysyl moiety. The in vitro stability of the resulting 4-[18F]fluorobenzoylated derivative was tested in different tissue homogenates. Furthermore, the 4-[18F]fluorobenzoylated N-epsilon-fructoselysine was used in positron emission tomography studies, as well as in studies concerning biodistribution and catabolism. The results show that the 4-[18F]fluorobenzoylated N-epsilon-fructoselysine is phosphorylated in vitro, as well as in vivo. This phosphorylation is caused by fructosamine 3-kinases and occurs in vivo, particularly in the kidneys. Despite the action of these enzymes, it was shown that a large part of the intravenously applied radiolabeled N-epsilon-fructoselysine was excreted nearly unchanged in the urine. Therefore, it was concluded that the predominant part of peptide-bound lysine that was fructosylated during food processing is not available for nutrition.

Characterization of a New Maillard Type Reaction Product Generated by Heating 1-Deoxymaltulosyl-glycine in the Presence of Cysteine

The reaction between Amadori compounds and cysteine was investigated. When 1-deoxymaltulosyl-glycine (glycyl-fructosyl-glucose) was heated at 100 degrees C with cysteine in a neutral aqueous solution, a novel intermediate composed of 1-deoxyosone and cysteine was detected. NMR and mass spectrometry studies revealed the structure of the isolated intermediate to be 7,8a-dihydroxy-4a-methyl-8-(alpha-d-glucopyranosyloxy)hexahydro-5-oxa-4-thia-1-azanaphthalene-2-carboxylic acid. This intermediate easily generated isomaltol and acetylfuran as volatile compounds in 1 mol/L HCl at 100 degrees C.

Gas chromatographic determination and mechanism of formation of D-amino acids occurring in fermented and roasted cocoa beans, cocoa powder, chocolate and cocoa shell

Fermented cocoa beans of various countries of origin (Ivory Coast, Ghana, Sulawesi), cocoa beans roasted under defined conditions (100-150 degrees C; 30-120 min), low and high fat cocoa powder, various brands of chocolate, and cocoa shells were analyzed for their contents of free L-and D-amino acids. Amino acids were isolated from defatted products using a cation exchanger and converted into volatile N(O)-pentafluoropropionyl amino acid 2-propyl esters which were analyzed by enantioselective gas chromatography mass spectrometry on a Chirasil-L-Val capillary column. Besides common protein L-amino acids low amounts of D-amino acids were detected in fermented cocoa beans. Quantities of D-amino acids increased on heating. On roasting cocoa beans of the Forastero type from the Ivory Coast at 150 degrees C for 2 h, relative quantities of D-amino acids approached 17.0% D-Ala, 11.7% D-Ile, 11.1% D-Asx (Asp + Asn), 7.9% D-Tyr, 5.8% D-Ser, 4.8% D-Leu, 4.3% D-Phe, 37.0% D-Pro, and 1.2% D-Val. In cocoa powder and chocolate relative quantities amounted to 14.5% D-Ala, 10.6% D-Tyr, 9.8% D-Phe, 8.1% L-Asx, and 7.2% D-Ile. Lower quantities of other D-amino acids were also detected. In order to corroborate our hypothesis that D-amino acids are generated from Amadori compounds (fructose amino acids) formed in the course of the Maillard reaction, fructose-L-phenylalanine and fructose-D-phenylalanine were synthesized and heated at 200 degrees C for 5-60 min. Already after 5 min release of 11.7% D-Phe and 11.8% L-Phe in the free form could be analyzed. Based on the data a racemization mechanism is presented founded on the intermediate and reversible formation of an amino acid carbanion in the Amadori compounds.

Changes in antioxidant activity of dehydrated onion and garlic during storage

The effect of the Maillard reaction evolution on the overall antioxidant activity (AA) of stored dehydrated onion and garlic has been studied. Extent of the reaction was followed through the determination of the Amadori compounds, measured as 2-furoylmethyl-amino acids (2-FM-AA), and colour development whereas AA was evaluated by the ORACFL assay. Dehydrated garlic exhibited a very slow progress of the Maillard reaction which did not lead to any noticeable change in its AA upon storage. However, a substantial increase of AA was observed in dehydrated onion samples, in agreement with a major Maillard reaction evolution. Moreover, a positive correlation between colour and antioxidant properties was observed during the storage of dehydrated onion at 50 °C, suggesting the predominant role of the advanced stages of the Maillard reaction over the AA. In conclusion, this study demonstrated that, although the Amadori compounds might exert a moderate effect on the AA, the advanced Maillard reaction products are the major contributors to this property.

Transformations of bioactive peptides in the presence of sugars—Characterization and stability studies of the adducts generated via the Maillard reaction

Glycation of biomolecules, such as proteins, peptide hormones, nucleic acids, and lipids, may be a major contributor to the pathological manifestations of aging and diabetes mellitus. These nonenzymatic reactions, also termed the Maillard reaction, alter the biological and chemical properties of biomolecules. In order to investigate the effect of various reducing sugars on the products formed from small bioactive peptides (Tyr-Gly-Gly-Phe-Leu, Tyr-Gly-Gly-Phe-Leu-NH 2, Tyr-Gly-Gly-Phe-Leu-OMe, Tyr-Gly-Gly-Phe, and Tyr-Gly-Gly), model systems were prepared with glucose, mannose or galactose. Peptide-sugar mixtures were incubated at 37 or 50 °C in phosphate-buffered saline, pH 7.4, or in methanol. The extent of glycation was determined periodically by RP HPLC. All sugar–peptide mixtures generated two different types of glycation products: N-(1-deoxy-ketos-1-yl)-peptide (Amadori compound) and the imidazolidinone compound substituted by sugar pentitol and peptide residue. The amount and distribution of peptide glycation products depended on the structure of the reactants, and increased in both concentration- and time-dependent manner in relation to exposure to sugar. Additionally, the rate of hydrolysis of glucose-derived imidazolidinone compounds, obtained either from leucine–enkephalin ( 1) or its shorter N-terminal fragments 2 and 3, was determined by incubation at 37 °C in human serum. These results revealed that imidazolidinones obtained from glucose and small peptides are almost completely protected from the action of enzymes in serum, the predominant route of degradation being spontaneous hydrolysis to initial sugar and peptide compound.

Gas chromatographic detection of d-amino acids in natural and thermally treated bee honeys and studies on the mechanism of their formation as result of the Maillard reaction

Relative quantities of d-amino acids, (%D) calculated from the sum of d- and l-amino acids were determined in bee honeys (n=6) by GC-SIM-MS. Amino acids were isolated by treatment with Dowex 50 W X8 cation exchanger and converted into N(O)-perfluoroacyl amino acid propyl esters. In all honeys d-Ala, ranging from 2.2–6.2% d-Ala, was detected. Other d-amino acids were also found, albeit not in all honeys and approached 5.9% d-Glx, 5.4% d-Lys, 3.0% d-Phe, 2.1% d-Orn, 1.7% d-Asx, 1.5% d-Ser, 0.1% d-Pro, and 0.4% d-Val in certain honeys. Quantities of d-amino acids increased very much on experimental heating of honeys in an oven and on a microwave treatment. Conventional heating of a forest honey (no. 1) at 65 °C for 450 h leads to an increase of d-Ala (2.2–12.5%), d-Pro (0.0–5.0%), d-Ser (1.5–9.1%), d-Asx (1.7–9.8%), d-Phe (0.4–5.0%) and d-Glx (1.5–5.8%); first numbers in parentheses refer to unheated honeys. Relative quantities of other d-amino acids also increased. Experimental heating of another forest honey (no. 2) in a microwave oven for 3 min at 180 W leads to an increase of d-Ala (3.7–11.0%), d-Glx (1.5–13.7%), d-Asx (0.7–10.2%), d-Phe (0.3–4.8%), d-Val (0–4.2%), and d-Pro (0.1–2.3%). Microwave treatment at 700 W for 1 min of a blossom honey (no. 3) leads to an increase of d-Ala (6.2–26.7%) and of d-Phe (3.0–10.9%). Microwave treatments were accompanied by intensive destruction of amino acids. Heating of a model mixture mimicking the major components of honey (d-glucose, d-fructose, and l-amino acids at 20% water content) at pH 2.6–9.0 and at 180 W for 1–3 min leads to the generation of d-amino acids and was also accompanied by intensive decay of amino acids. From the data it is concluded that d-amino acids are formed in honeys in the course of the Maillard reaction. A mechanism is presented based on amino acid racemization of reversibly formed Heyns and Amadori compounds (fructose-amino acids).

RAPID HIGH PERFORMANCE LIQUID CHROMATOGRAPHIC DETECTION OF FUROSINE (ε‐N‐2‐FUROYLMETHYL‐L‐LYSINE) IN YOGURT AND CHEESE MARKETED IN TURKEY*

ABSTRACT Furosine (ε‐N‐2‐furoylmethyl‐L‐lysine) content determination in the yogurt and different cheese types (pickled white, kasar, processed, canned tulum, blue‐veined and mozzarella cheeses) marketed in Turkey was performed using ion‐pair reversed‐phase high performance liquid chromatography (RP‐HPLC). Calibration study (R2 = 0.9999), analytical method validation and recovery studies gave satisfactory results. The lowest furosine values were observed in pickled white cheeses (5.35 ± 0.01 to 7.28 ± 0.02 mg/100 g protein). All cheeses except pickled white showed furosine values between 182.16 ± 0.12 (canned tulum) and 261.32 ± 0.10 mg/100 g protein (ripened kasar). The highest content of furosine was observed in whole yogurt (316.47 ± 0.17 mg/100 g protein) which could be because of severe heat treatment and the addition of milk powder during the manufacturing process. The method provides a rapid, reproducible and accurate determination of this Amadori compound (ε‐deoxy‐fructosyl‐lysine) in yogurt and cheese samples.

ε-Glycation, APP and Aβ in ageing and Alzheimer disease: A hypothesis

The post-translational modifications of protein molecules include glycation, which may not only occur enzymatically controlled in N and O position, but also wherever proteins meet reducing sugars non-enzymatically in epsilon position at lysines (non-enzymatic (epsilon) glycation (NEG)). The formation of keto-amines from the amine-sugar compounds (Amadori re-arrangement) and further processing of the largely undigestible Amadori compounds eventually results in insoluble advanced glycation end products (AGEs). The latter can induce or favour disease including mental disorders. Preferential targets of NEG include large cell surface proteins. Ample evidence has been provided that NEG also occurs in the brain where cross-linking of epsilon-glycated proteins, induction of oxidative stress and signalling of AGEs through their specific receptor (RAGE) likely play a role in (brain) ageing and Alzheimer disease (AD). This is underscored by the demonstration of particular interactions between AGE/RAGE and amyloid-beta (Abeta) that favour the aggregation and deposition of Abeta and, perhaps, the formation of Abeta itself. The close relationship between NEG and Abeta, as well as other facts foster the hypothesis that NEG of the large trans-membrane amyloid precursor protein (APP) might be a significant factor in the induction of aberrant APP cleavage with production of Abeta, not only in normal ageing, but also in AD. Blockade of lysine cleavage sites on APP by sugar chains or marker effects induced by NEG akin to ubiquitination of proteins for degradation at lysines could be expected to contribute to altered processing of APP. The hypothesis of epsilon-glycation in APP proposed here and the review of evidences for the significance of NEG in brain ageing and AD are aimed at the stimulation of investigations into the still open question which role NEG plays with respect to APP and its abnormal processing in AD. It can be rendered likely that such research might open new avenues towards decreasing the risk of AD and/or slowing its progression through the prevention of NEG in APP with aberrant APP processing, increased generation of Abeta and the formation of AGEs from epsilon-glycated APP.

Mass Spectrometric Detection and Formation of d-Amino Acids in Processed Plant Saps, Syrups, and Fruit Juice Concentrates

Liquid and syrupy dietary saps and juices of plant origin, characterized by the presence of large quantities of saccharides (glucose, fructose, or sucrose) and containing amino acids, were analyzed for the presence of D-amino acids using enantioselective gas chromatography-mass spectrometry. D-amino acids were detected in processed saps and juices of trees (maple, palm, birch), fruits (grape, apple, pear, pomegranate, date), and various other plants (agave, beetroot, sugar cane, carob). D-Ala was detected in all plant products and amounted to approximately 34% D-Ala (relative to L-Ala + D-Ala) in Canadian maple syrups, to approximately 13% in palm saps, and to 48 and 13% D-Ala, respectively, in concentrated grape juices (Spanish Arrope and Turkish Pekmez). Varying amounts and kinds of other D-amino acids were also detected. To test the hypothesis that racemization, that is, partial conversion of L-amino acids into their corresponding D-enantiomers, occurs at reversible stages of the Maillard reaction, the Amadori compound fructose-L-phenylalanine was synthesized. On heating at 200 degrees C for 5 (20) min, release of 10.8% (24.2%) D-Phe was detected. From the data it is concluded that the Amadori compounds formed in the course of the Maillard reaction are pecursors of D-amino acids in foodstuffs.

Elucidating the Secrets of the Maillard Reaction Cascade – The Role of Amadori Compounds

Elucidating the Secrets of the Maillard Reaction Cascade – The Role of Amadori Compounds

Assessment of Initial Stages of Maillard Reaction in Dehydrated Onion and Garlic Samples

The initial steps of the Maillard reaction in freshly laboratory-freeze-dried and commercial dehydrated onion and garlic samples have been assessed by quantitative determination of 2-furoylmethylamino acids, obtained after acid hydrolysis of the corresponding Amadori compound. In freshly prepared samples, hardly any presence of 2-furoylmethylamino acids was detected, whereas in commercial samples, onion contained much more important levels of 2-furoylmethylamino acids as compared to garlic species. 2-Furoylmethyl-gamma-aminobutyric acid (1), 2-furoylmethyl-lysine (furosine; 2), and 2-furoylmethylarginine (3) were identified in all commercial dehydrated onion samples, with compound 3 being the most abundant. All garlic samples presented slightly higher levels of 2 than 3 with no presence of 1. The observed differences between onion and garlic commercial samples may be due to their very different content of reducing sugars. Moreover, some variations found in 2-furoylmethyl derivatives within both onion and garlic species could be also attributed to different processing and storage conditions during the manufacture of these products. The findings of this study show the first evidence of important levels of Amadori compounds in dehydrated garlic and onion samples, as well as the usefulness of 2-furoylmethyl derivatives as quality indicators for the early detection of the Maillard reaction in onion and garlic products.