Analysis of Amadori Compounds by High-Performance Cation Exchange Chromatography Coupled to Tandem Mass Spectrometry

Davídek, Tomáš; Kraehenbuehl, Karin; Devaud, Stéphanie; Robert, Fabien; Blank, Imre

doi:10.1021/ac048925a

Cited by 90 publications

(76 citation statements)

References 27 publications

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“…Furthermore, N-(1-deoxy-d-fructos-1-yl)-l-glutamic acid (41) was identified in sun-dried tomatos in yields of up to 1.5 % (on a weight basis), and confirmed to be generated by the Maillard reaction of lglutamic acid and glucose upon the drying of foods. [74] After independent synthesis, this Amadori product was found to exhibit an umami-like taste quality with a recognition threshold of 1.8 mmol L À1 . [75] Moreover, the previously not reported N-(1-carboxymethyl)-6-hydroxymethylpyridinium-3-ol inner salt, named alapyridaine (42), was discovered as a taste enhancer in beef bouillon by means of the sensomics approach.…”

Section: Natural Umami Compoundsmentioning

confidence: 98%

Sweet and Umami Taste: Natural Products, Their Chemosensory Targets, and Beyond

et al. 2011

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Much of our appreciation of food is due to the excitement of the perception of "sweet" and "umami" taste. With a special focus on natural products, this Review gives a summary of compounds that elicit and modulate "sweet" or "umami" taste responses. It will be discussed how the interaction of these molecules with the oral sweet and umami taste receptors stimulates receptor cells to secrete neurotransmitters to induce neural activity that is conveyed to the cerebral cortex to represent sweet and umami taste, respectively. Recent data also show that a sweet taste is metabolically relevant for fuel homeostasis and linked to appetitive ingestive behavior.

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Section: Natural Umami Compoundsmentioning

confidence: 98%

Sweet and Umami Taste: Natural Products, Their Chemosensory Targets, and Beyond

et al. 2011

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“…Aspergillus) grow. Glycated amino acids have been reported on dried fruits, but they are likely to be formed during the drying process itself (36). Identification of glycated amino acids in the environment might be difficult since those relatively unstable compounds may be present in very small ecological niches and, possibly, during a well defined period of time.…”

Section: Crystal Structure Of the Deglycating Enzyme Faox-iimentioning

confidence: 99%

Crystal Structure of the Deglycating Enzyme Fructosamine Oxidase (Amadoriase II)

Collard

Zhang

Nemet

et al. 2008

Journal of Biological Chemistry

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Fructosamine oxidases (FAOX) catalyze the oxidative deglycation of low molecular weight fructosamines (Amadori products). These proteins are of interest in developing an enzyme to deglycate proteins implicated in diabetic complications. We report here the crystal structures of FAOX-II from the fungi Aspergillus fumigatus, in free form and in complex with the inhibitor fructosyl-thioacetate, at 1.75 and 1.6 Å resolution, respectively. FAOX-II is a two domain FAD-enzyme with an overall topology that is most similar to that of monomeric sarcosine oxidase. Active site residues Tyr-60, Arg-112 and Lys-368 bind the carboxylic portion of the fructosamine, whereas Glu-280 and Arg-411 bind the fructosyl portion. From structure-guided sequence comparison, Glu-280 was identified as a signature residue for FAOX activity. Two flexible surface loops become ordered upon binding of the inhibitor in a catalytic site that is about 12 Å deep, providing an explanation for the very low activity of FAOX enzymes toward protein-bound fructosamines, which would have difficulty accessing the active site. Structure-based mutagenesis showed that substitution of Glu-280 and Arg-411 eliminates enzyme activity. In contrast, modification of other active site residues or of amino acids in the flexible active site loops has little effect, highlighting these regions as potential targets in designing an enzyme that will accept larger substrates.Fructosamines are formed by condensation of glucose with the amino group of amino acids or proteins. Fructosamines are formed spontaneously, i.e. non-enzymatically, at a rate that depends on temperature, sugar anomerization rate, concentration, and turnover rate of the target proteins. In medicine, protein-bound fructosamines (also named glycated proteins) have attracted much attention since their formation is increased in diabetes and taken to be in part responsible for diabetic complications. Fructosamines are relatively unstable compounds and are precursors for advanced glycation end products (AGEs), 5 some of which cause proteins cross-linking, extracellular matrix stiffening, and activation of the receptor for AGEs (RAGEs) (1, 2). As an example, the fructosamine-derived lysine-arginine cross-link glucosepane is to date the single major cross-link known to accumulate in human collagen in diabetes and aging (3).Several years ago our laboratory initiated a search for deglycating enzymes in soil organisms with the goal of finding enzymes that could deglycate proteins. In doing so we found enzymes with "amadoriase" activity toward low molecular weight substrates in soil samples, first in Pseudomonas sp. (4) and later in Aspergillus fumigatus (5-7). The latter turned out to have similar properties with the enzyme first published by Horiuchi et al. (8) under the name fructose amino acid oxidase (EC 1.5.3). Considerable work has since been published on these enzymes, which we are referring to in this work under the generic name fructosamine oxidases (FAOX).In addition to FAOX enzymes, two different families o...

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“…Nowadays, mass spectrometry (MS) has been adopted by many researchers attempting to reveal the details of Maillard chemistry (9,(15)(16)(17)(18). Whereas traditional mass analysis would provide the fragment ions resulting from all compounds contained within a sample, tandem mass spectrometry provides information regarding the fragment ions that originate from a single molecular ion (9).…”

Section: Introductionmentioning

confidence: 99%

Assessment of Feasibility of Maillard Reaction between Baclofen and Lactose by Liquid Chromatography and Tandem Mass Spectrometry, Application to Pre Formulation Studies

et al. 2009

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Abstract. The aim of this study was to determine any possible, baclofen-lactose Maillard reaction products. Granules and tablets of baclofen and lactose were prepared and maintained in heat ovens for a certain time period. The effects of lactose type, addition of magnesium stearate, and water were monitored. Heated lactose and baclofen were analyzed using reverse-phase HPLC. Liquid chromatography tandem mass spectroscopy revealed nominal mass values consistent with baclofen-lactose, earlystage Maillard reaction condensation products (ESMRP). Multiple reaction monitoring confirmed the presence of ESMRP as well. FTIR analysis proved the formation of imine bond. The results indicated that baclofen undergoes a Maillard-type reaction with lactose.

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Analysis of Amadori Compounds by High-Performance Cation Exchange Chromatography Coupled to Tandem Mass Spectrometry

Cited by 90 publications

References 27 publications

Sweet and Umami Taste: Natural Products, Their Chemosensory Targets, and Beyond

Sweet and Umami Taste: Natural Products, Their Chemosensory Targets, and Beyond

Crystal Structure of the Deglycating Enzyme Fructosamine Oxidase (Amadoriase II)

Assessment of Feasibility of Maillard Reaction between Baclofen and Lactose by Liquid Chromatography and Tandem Mass Spectrometry, Application to Pre Formulation Studies

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