Thesis (MTech (Food Technology))--Cape Peninsula University of Technology, 2016. / The Maillard reaction (MR) involves the condensation reaction between amino acids or proteins with reducing sugars, which occurs commonly in food processing and storage. Maillard reaction products (MRPs) were prepared from glucose-casein model system at pH 8, heated at 60, 75 and 90°C for 6, 12 and 24 h, respectively. Browning intensity (BI) of MRPs, as monitored by absorbance at 420 nm increased with an increase in reaction temperature. The reducing power (RP) of MRPs increased (p < 0.05) as the reaction time increased at 60 and 75°C, while at 90°C an increase in RP was observed from 6 to 12 h and thereafter a slight decrease was observed up to 24 h. The 2,2-Azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) radical scavenging activity (ABTS-RS) and Peroxyl radical scavenging (PRS) activity of glucose-casein MRPs produced at 90°C decreased as the reaction time increased. In this study, the ferrous chelation activity of MRPs was higher than that of tert-butylhydroquinone (TBHQ) (0.02%) and Trolox (1 mM), respectively. Moreover, the 1, 1-diphenyl-2-picryl-hydrazil radical scavenging (DPPH-RS) of MRPs increased (p < 0.05) as the reaction time increased irrespective of the heating temperature. The primary and secondary lipid oxidation products were measured using the Peroxide value (PV) and Thiobarbituric acid reactive substance (TBARs) assay in sunflower oil-in-water emulsion, respectively. MRPs derived at 90°C for 12 h had the lowest peroxide value, while the TBARs inhibitory by MRPs ranged from 39.05 – 88.66%. Glucose-casein MRPs displayed superior antioxidant activity than TBHQ (0.02%) and Trolox (1 mM), respectively, as measured by the TBARs assay. The differential scanning calorimetry (DSC) and Rancimat techniques set at 110°C were used to evaluate the oxidative stability the lipid-rich media containing MRPs. At the same temperature program, DSC gave significantly lower reduction times than the Rancimat. Furosine (N-ε-Fructosyl-lysine) and Pyrraline (2-amino-6-(2-formyl-5-hydroxymethyl-1-pyrrolyl)-hexanoic acid) were determined using high pressure liquid chromatography to evaluate the extent of the MR. Furosine concentration of glucose-casein MRPs ranged between 0.44 – 1.075 mg.L-1 in MRPs derived at 60°C, while at 75°C an increase as function of time was observed. MRPs derived at 60 and 75°C exhibited a varied concentration of pyrraline as the reaction time increased with higher temperatures resulted in higher concentrations (0.39 mg.L-1). The results of this study clearly indicated that MRPs possess antioxidant activity and can be used as natural antioxidants in the food industry.

The role of redox reactions in the formation of aroma volatiles, colour and other non-volatiles in the Maillard Reaction was investigated. The electrochemical properties of individual reactants and Maillard model mixtures were monitored via ORP (oxidation-reduction potential) and oxygen electrodes. All models exhibited unique electrochemical activities represented by their corresponding ORP profiles. Investigation into the redox potentials of several model systems demonstrated that the increased negative value of a redox potential is not necessarily correlated with its browning potential. An optimal redox potential range, where browning is favoured, was found to represent a balance between carbonyl and hydroxyl moieties in the structure. Adjustment of this redox potential by introducing reducing or oxidizing species can shift this balance resulting in modifications in browning capacities. However, it was concluded that there is a clear relationship between browning ability and reducing capacity of the model systems. Furthermore, a novel oxidative pyrolysis technique was developed to study the role of oxidative environment on the product distribution during pyrolysis and to investigate the mechanism of formation of non-volatiles through 13C and 15N-label incorporation. Application of this technique to glucoselglycine model system have indicated that most non-volatile Maillard reaction products can arise from glucose oxidation intermediates such as glucosone, gluconic acid and deoxyglucosones. To study the specific role of redox reactions in the formation of non-volatiles, a post-pyrolytic derivatization technique was developed and optimized. Several non-volatile end products were identified and mechanistically confirmed to involve oxidation and reduction reactions for their formation, such as lactones, hydroxylated benzenes and hydroxylated pyrazine. The latter was identified and confirmed to be generated via the dimerization of glycine and subsequent oxidation. In addition, the formation of different volatiles such as pyrazole, imidazole and oxazole was mechanistically confirmed to depend on redox reactions.

Diss.--Philosophie--New York--City Univ. of NY, 1981. / Catalogue raisonné des oeuvres de J. Maillard p. 169-203. Réunit la musique de messes, motets et autres oeuvres vocales sacrées p. 204-281. Bibliogr. p. 289-309.

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Les produits de glycation avancée (AGEs) sont trouvés en excès dans le plasma et les tissus au cours du diabète, de l'insuffisance rénale et du vieillissement. Ils se forment aussi pendant la cuisson domestique et industrielle des aliments. Actuellement, la plus forte consommation de denrées alimentaires transformées contenant des quantités importantes des AGEs augmente le risque d'exposition de la population aux AGEs et à leurs effets biologiques. C'est ainsi que l'étude de la biodisponibilité des AGEs devient un sujet d'actualité dans la compréhension de la pathogenèse de certaines maladies chroniques, particulièrement le diabète. Deux études cliniques ont été menées dans le but d'étudier l'impact de l'ingestion des AGEs alimentaires sur les fluctuations des concentrations de ces mêmes molécules retrouvées dans les fluides biologiques des individus sains étudiés. Une première étude qui compare la teneur des AGEs ingérés à travers deux régimes alimentaires administré à 62 jeunes adultes. Une deuxième étude qui évalue la teneur en AGEs d'une alimentation basée sur du lait maternel ou du lait de formules infantiles donné à 161 bébés. La quantification de la carboxyméthyllysine (CML) et des AGEs fluorescents comme indicateurs de la réaction de Maillard a été effectuée dans les aliments administrés aux sujets de l'étude ainsi que dans leurs matrices biologiques : plasma, urine et fèces. Les résultats montrent qu'un régime contenant 2,5 fois moins de CML et 1,7 fois moins des AGEs fluorescents, en comparaison avec un régime courant ou standard, peut provoquer des baisses importantes de ces indicateurs dans le plasma, l'urine et la matière fécale des individus sains. Ces diminutions sont plus accentuées au niveau de l'excrétion urinaire. D'autre part, une plus forte présence de la CML dans le lait de formules infantiles correspond à une plus forte quantité de CML dans le plasma et dans l'urine des enfants ayant ingéré cet aliment, à la différence des enfants nourris avec le lait maternel, caractérisé par de faibles quantités de la CML. Chez les adultes soumis au régime bas en AGEs ainsi que les bébés nourris avec le lait maternel, les niveaux de certains paramètres métaboliques tels que le stress oxydatif, les antioxydants importants et des facteurs de l'inflammation cellulaire et systémique ont été normaux mais inférieurs à ceux des adultes et des enfants ayant ingéré de plus fortes quantités d'AGEs. Ces effets indiquent que de plus faibles quantités de produits de Maillard alimentaires pourraient avoir un impact sur la prévention des maladies chroniques. / Advanced Glycation End Products (AGEs) are found in excess in plasma and tissus during diabetes, renal diseases and aging. AGEs are known to form in foods during industrial processes or home cooking. Nowadays, an excessive intake of technologically transformed foods riches in AGEs, increase the risk of the population to their possible pathophysiological effects. In this contexte, the study of bioavailability of AGEs formed in foods may have a significant impact in understanding the pathogenesis of some chronic diseases as diabetes.Two clinical studies were conducted to study the impact of dietary intake of AGEs on fluctuating levels of these same molecules found in biological fluids of healthy individuals studied. A first study that compared the content of AGEs ingested through two diets administered to 62 young adults. A second study evaluates the AGE content of a diet based on breast milk or infant formula milk given to 161 babies. Quantification of CML and fluorescent AGEs as indicators of the Maillard reaction was performed in the food administered to the subjects and their biological matrices: plasma, urine and feces. The results show that a diet containing less than 2.5 times and 1.7 times of CML and fluorescent AGEs respectively, compared with a current or standard diet, can cause significant declines in these indicators in plasma, urine and fecal matter of healthy individuals. These decreases are more pronounced at the level of urinary excretion. A stronger presence of CML in the milk of infant formula is a higher amount of CML in plasma and urine of children who ingested this food, unlike the children fed with milk breast, characterized by low levels of CML. In adults subjected to diet low in AGEs and babies fed breast milk, the levels of some metabolic parameters such as oxidative stress, antioxidants and important factors of cellular and systemic inflammation, were lower than normal levels of adults and children who ingested higher amounts of AGEs. These effects indicate that lower amounts of dietary Maillard products could have an impact on chronic disease prevention

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No description available.

Pour répondre aux attentes des consommateurs, l'industrie agro-alimentaire mise sur l'innovation qui reste le vecteur principal de croissance et de différenciation des entreprises. Celles-ci sont en permanence à la recherche de nouveaux ingrédients. Elles visent ainsi la production d'aliments innovants dotés de structures complexes, dont les émulsions font partie. Ces dernières sont d’ailleurs largement répandues dans le domaine de l’agro-alimentaire. Cependant, au cours de leur fabrication ou de leur stockage, ces émulsions sont soumises à des phénomènes concomitants de déstabilisation et d’oxydation, palliés par la présence d’additifs le plus souvent d’origine chimique. Or, les consommateurs recherchent désormais des produits alimentaires contenant des substances naturelles, voire exempts d’additifs (clean label). La recherche de nouveaux ingrédients d'origine naturelle est donc un défi majeur pour les industriels de l’agro-alimentaire, et suscite un intérêt croissant. Les pistes explorées sont nombreuses, et parmi celles-ci, la réaction de glycation ou réaction de Maillard (RM) appliquée à des protéines ou des mélanges peptidiques. En effet, la RM peut s’avérer potentiellement intéressante pour renforcer la capacité antioxydante et/ou les propriétés technofonctionnelles, dont les propriétés émulsifiantes, de substrats protéiques. Dans ce contexte, nous avons cherché à optimiser les propriétés émulsifiantes et antioxydantes de deux substrats protéiques par la RM en conditions contrôlées et en présence de différents glucides. Du caséinate de sodium et un hydrolysat de coproduits de crevette ont été choisis. Le premier substrat est utilisé comme protéine de référence, car il est couramment employé dans l’industrie comme agent émulsifiant, et le second est étudié dans l’optique d’une valorisation des co-produits de la pêche. En effet, l'hydrolyse enzymatique constitue une approche d'un intérêt stratégique majeur pour réhabiliter la fraction protéique des coproduits marins. Nous avons réalisé des RM entre l’hydrolysat de crevette et trois concentrations différentes de xylose. Nous avons ainsi montré que l’augmentation de la concentration en xylose entraîne une diminution logarithmique du nombre de fonctions aminées restantes après RM. Ceci indique que la concentration en xylose initialement utilisée était limitante. Des analyses chromatographiques montrent que l’utilisation de concentrations plus importantes en xylose semble privilégier l’apparition de composés aromatiques de faible poids moléculaire(< 250 Da). Par ailleurs, l’augmentation de la concentration en xylose lors de la RM avec l’hydrolysat de crevette modifie les propriétés rhéologiques des émulsions à 0,5 % et pH 7. Enfin, la capacité antioxydante des hydrolysats de crevette issus de la RM augmente lorsque la concentration en xylose utilisée est croissante dans le milieu réactionnel. En conclusion, notre étude a permis de produire, à partir de deux substrats protéiques modifiés par RM en conditions contrôlées à 50°C, des ingrédients potentiellement bifonctionnels, montrant à la fois des propriétés émulsifiantes et antioxydantes. / No

The reactions of reducing sugars with primary amino groups are the most common nonenzymatic modifications of proteins. Subsequent rearrangements, oxidations, and dehydrations yield a heterogeneous group of mostly colored and fluorescent compounds, termed "Maillard products" or advanced glycation end products (AGEs). AGE formation has been observed on long-lived proteins such as collagen, eye lens crystalline, and in pathological protein deposits in Alzheimer's (AD) and Parkinson's disease (PD) and dialysis-related amyloidosis. AGE-modified proteins are also involved in the complications of diabetes. AGEs accumulate in the the ß-amyloid plaques and neurofibrillary tangles (NFT) associated with AD and in the Lewy bodies characteristic of PD. Increasing evidence supports a role for oxidative stress in neurodegenerative disorders such as AD and PD. AGEs have been shown to contribute towards oxidative damage and chronic inflammation, whereby activated microglia secrete cytokines and free radicals, including nitric oxide (NO). Roles proposed for NO in the pathophysiology of the central nervous system are increasingly diverse and range from intercellular signaling, through necrosis of cells and invading pathogens, to the involvement of NO in apoptosis. Using in vitro experiments, it was shown that AGE-modified bovine serum albumin (BSA-AGE) and AGE-modified ß-amyloid, but not their unmodified proteins, induce NO production in N-11 murine microglia cells. This was mediated by the receptor for AGEs (RAGE) and upregulation of the inducible nitric oxide synthase (iNOS). AGE-induced enzyme activation and NO production could be blocked by intracellular-acting antioxidants: Ginkgo biloba special extract EGb 761, the estrogen derivative, 17ß-estradiol, R-(+)-thioctic acid, and a nitrone-based free radical trap, N-tert.-butyl-*-phenylnitrone (PBN). Methylglyoxal (MG) and 3-deoxyglucosone (3-DG), common precursors in the Maillard reaction, were also tested for their ability to induce the production of NO in N-11 microglia. However, no significant changes in nitrite levels were detected in the cell culture medium. The significance of these findings was supported by in vivo immunostaining of AD brains. Single and double immunostaining of cryostat sections of normal aged and AD brains was performed with polyclonal antibodies to AGEs and iNOS and monoclonal antibodies to Aß and PHF-1 (marker for NFT) and reactive microglia. In aged normal individuals as well as early stage AD brains (i.e. no pathological findings in isocortical areas), a few astrocytes showed co-localisation of AGE and iNOS in the upper neuronal layers of the temporal (Area 22) and entorhinal (Area 28, 34) cortices compared with no astrocytes detected in young controls. In late AD brains, there was a much denser accumulation of astrocytes co-localised with AGE and iNOS in the deeper and particularly upper neuronal layers. Also, numerous neurons with diffuse AGE but not iNOS reactivity and some AGE and iNOS-positive microglia were demonstrated, compared with only a few AGE-reactive neurons and no microglia in controls. Finally, astrocytes co-localised with AGE and iNOS as well as AGE and ß-amyloid were found surrounding mature but not diffuse ß-amyloid plaques in the AD brain. Parts of NFT were AGE-immunoreactive. Immunohistochemical staining of cryostat sections of normal aged and PD brains was performed with polyclonal antibodies to AGEs. The sections were counterstained with monoclonal antibodies to neurofilament components and a-synuclein. AGEs and a-synuclein were colocalized in very early Lewy bodies in the substantia nigra of cases with incidental Lewy body disease. These results support an AGE-induced oxidative damage due to the action of free radicals, such as NO, occurring in the AD and PD brains. Furthermore, the involvement of astrocytes and microglia in this pathological process was confirmed immunohistochemically in the AD brain. It is suggested that oxidative stress and AGEs participate in the very early steps of Lewy body formation and resulting cell death in PD. Since the iNOS gene can be regulated by redox-sensitive transcription factors, the use of membrane permeable antioxidants could be a promising strategy for the treatment and prevention of chronic inflammation in neurodegenerative disorders. / Die Glykierung oder Maillard-Reaktion ist neben der oxidativen Modifikation die bekannteste nicht-enzymatische posttranslationale Modifikation von Proteinen. Glykierung startet mit der Reaktion von reduzierenden Zuckern mit primären Aminogruppen. Nachfolgenden Umlagerungen, Oxidationen und Dehydra- tionen führen zu einer heterogenen Gruppe von farbigen und fluoreszierenden Verbindungen, den sogenannten "Maillard products" oder "advanced glycation end products" (AGEs). Diese Vorgänge werden besonders an langlebigen Proteinen wie Kollagen und Kristallin der Augenlinsen sowie in pathologischen Proteinab- lagerungen bei der Alzheimer-Demenz (AD), der Parkinson-Krankheit (PD) und bei Hämodialyse beobachtet. AGE-modifizierte Proteine sind auch aktiv beteiligt an den Spätkomplikationen des Diabetes mellitus. AGEs reichern sich im Alzheimer Gehirn in den ß-Amyloid-Plaques und den neurofibrillären Bündeln (tangles, NFT), sowie in den für PD charakteristisch- en Lewi-Körpern an. Immer mehr Befunde belegen die Rolle von oxidativem Stress in neurodegenerativen Erkrankungen wie AD und PD. Es konnte gezeigt werden, dass AGEs an oxidativer Schädigung und chronischer Entzündung Anteil haben, wobei aktivierte Mikroglia Cytokine und freie Radikale, inklusive Stickstoffmonoxid (NO) sezernieren. Vermutungen über die Rolle von NO in der Pathophysiologie des Zentralnervensystems gehen weit auseinander und reichen von interzellulärer Signalübertragung über nekrotischen Zelltod und eindringende pathogene Substanzen bis zur Beteiligung von NO an der Apoptose. In einem Zellkultur Modell konnte in vitro gezeigt werden, dass AGE- modifiziertes Albumin (BSA-AGE) und AGE-modifiziertes ß-Amyloid, aber nicht die unmodifizierten Proteine, die Synthese von NO in N-11 Maus-Mikrogliazellen induzieren. Diese wird möglicherweise vom Rezeptor für AGE (RAGE) und durch eine Steigerung der Expression der induzierbaren Stickstoffmonoxid-Synthase (iNOS) vermittelt. AGE-induzierte Enzymexpression und NO-Produktion konnten durch folgende intrazellulär wirkende Antioxidantien blockiert werden: Ginkgo biloba Spezialextrakt EGb 761, das Östrogenderivat 17ß-Estradiol, alpha- Liponsäure, und ein Radikalfänger, N-tert.-butyl-*-phenylnitrone (PBN). Neben AGEs wurden auch reaktive Dicarbonyle wie Methylglyoxal (MG) und 3- Deoxyglucosone (3-DG), Vorläufer der Maillard-Reaktion, auf ihre Fähigkeit untersucht, die Synthese von NO in N-11 Mikroglia zu induzieren. Es konnten jedoch keine Induktion der NO-Produktion festgestellt werden. Die Bedeutung dieser in vitro-Ergebnisse wurden durch in vivo Immunohisto- chemischen Untersuchungen an AD Gehirnen bestätigt. Einfache und doppelte Immunfärbungen wurden an Gefrierschnitten von normal gealterten Gehirnen und AD-Gehirnen mit polyklonalen Antikörpern gegen AGEs und iNOS und monoklonalen Antikörpern gegen Aß, PHF-1 (zur spezifischen Markierung der NFT) und reaktive Mikroglia angefertigt. Bei normal gealterten Personen sowie bei AD Erkrankten im Frühstadium (d.h. keine pathologischen Veränderungen in iso- kortikalen Gebieten) wiesen wenige Astrozyten eine Kolokalisation von AGE und iNOS in den oberen Neuronenschichten des temporalen (Area 22) und entorhinalen (Area 28, 34) Kortex auf. Im Vergleich dazu wurden keine Astrozyten in jungen Kontrollgehirnen gefunden. In fortgeschrittenen Alzheimergehirnen wurde eine viel dichtere Anreicherung von Astrozyten, kolokalisiert mit AGE und iNOS in den tieferen, und insbesondere in den oberen Neuronenschichten gefunden. Weiterhin konnten zahlreiche Neurone mit diffuser AGE-Reaktivität, aber ohne iNOS-Reaktivität, sowie einige AGE- und iNOS-positive Mikroglia gezeigt werden, im Vergleich zu nur wenigen AGE-reaktiven Neuronen und keinen Mikroglia in den Kontrollen. Schliesslich wurden in Astrozyten, die reife, aber nicht diffuse ß-Amyloid-Plaques im AD-Gehirn umlagern, AGE mit iNOS sowie mit ß-Amyloid kolokalisiert gefunden. Teile der NFT waren AGE-immunoreaktiv. Immunhistochemische Färbung an Gefrierschnitten von normal gealterten und PD- Gehirnen wurden mit polyklonalen Antikörpern gegen AGEs durchgeführt. Die Schnitte wurden mit monoklonalen Antikörpern gegen Neurofilamentkomponenten und a-Synuclein gegengefärbt. AGEs und a-Synuclein waren kolokalisiert in sehr frühen Lewi-Körpern der Substantia nigra in Gehirnen mit vorhandener Lewi-Körper-Demenz. Diese Ergebnisse unterstützen die These AGE-induzierter oxidativer Schädigung mittels freier Radikale wie z.B. NO in AD- und PD- Gehirnen. Ausserdem wurde die Beteiligung von Astrozyten und Mikroglia an diesem pathologischen Prozess immunhistochemisch im Alzheimergehirn bestätigt. Es liegt nahe, dass oxidativer Stress und AGEs an den sehr frühen Stufen der Lewi-Körper-Bildung und dem daraus resultierenden Zelltod in PD beteiligt sind. Da das iNOS-Gen durch redoxsensitive Transkriptionsfaktoren reguliert werden kann, könnte die Verwendung membranpermeabler Antioxidantien eine erfolgversprechende Strategie für die Behandlung und Prävention chronischer Entzündungen bei neurodegenera- tiven Erkrankungen darstellen.

Amadori rearrangement product (ARP) of tryptophan with glucose was synthesized according to a published procedure, and its decomposition was studied at two different concentrations and at two temperatures, 110$ sp circ$C and 140$ sp circ$C over a period of 6 hrs. A RP-HPLC system was developed to separate and quantitate the decomposition products of the ARP. The results indicated that, the ARP can decompose to form the following products, hydroxymethylfurfural (HMF), maltol, indole, $ beta$-carbolines (norharman and harman) and tryptophan. Further, using the same analytical method, the following systems were also analyzed for the presence of the above mentioned products (a) D-glucose and D-mannose with tryptophan; (b) D-glucose; and (c) tryptophan. In addition, rate constants and activation energies for the decomposition and formation reaction were calculated. Plausible mechanisms for the formation of the decomposition products are suggested.