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The Maillard Reaction in Food and Medicine

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The Maillard Reaction in Food and Medicine COST - IMARS Joint Workshop Cost Action 927 - IMARS The Maillard Reaction in Food and Medicine Napoli, 2006 May 24-27 Centro Congressi Ateneo Federico II Via Partenope, 36 - Napoli Wednesday, May 24 13.30: Registration 14.00-18.00: “APPETIZER WORKSHOP” Three moderated debates about the question: “Are dietary AGEs/ALEs a risk to human health and, if they are, what is the mechanism of action?” Motion 1: Dietary AGEs are a risk to human health Chair: Thomas Henle For the motion: Katerina Sebekova Against the motion: Jenny Ames Motion 2: Dietary ALEs are a risk to human health Chair: Vincent Monnier For the motion: Joseph Kanner Against the motion: John Baynes Coffee break Motion 3: The mechanism by which dietary AGEs and ALEs pose a risk to human health is via their interaction with RAGE Chair: Paul Thornalley For the motion: Anne-Marie Schmidt Against the motion: Claus Heizmann Wednesday, May 24 COST927-IMARS WORKSHOP THE MAILLARD REACTION IN FOOD AND MEDICINE 18.15-19.15 Welcome addresses IMARS President: Vincent Monnier COST action 927 Chair: Vincenzo Fogliano Opening lecture: Helmut Erbersdobler Forty years of Furosine - Forty years of using markers for Maillard Reaction in Food and Nutrition Thursday, May 25 8.30: Registration 9.00-12.30: Exogenous and endogenous MRPs/AGEs: nutrition and toxicology Chairs: Karl Heinz Wagner & Veronika Somoza 9.00 T. Henle: Antimicrobial and cytotoxic effects of dicarbonyl compounds in honey - risk or benefit? 9.25 J. Ames: Effect of dietary heat treatment on the profile of human colonic bacteria in ulcerative colitis: in vitro and in vivo studies 9.50 T. Buetler: Mechanistic evaluation of biological effects of dietary AGEs 10.15 A. Simm: Influence of the Maillard reaction on ischemia reperfusion injury 10.40-11.00: Coffee Break 11.00 K.H. Wagner: Safety assessment of Glucose vs. Fructose based Maillard Reactions Products 11.15 L. Bravo: Coffee Melanoidin protects human hepatoma HepG2 against oxidative stress induced by tertbutyl hydroperoxide 11.30 F. Tessier: Protective effect of a diet rich in Maillard Reaction products on experimentally induced colitis in mice 11.45 P. O´Brien: Dietary AGE and thiamine deficiency increased plasma alpha-oxoaldehyde levels and colonic inflammation 12.00 M. Argirova: In vitro effects of model Maillard Reaction product on the mechanical activity of rat gastric smooth muscle 12.30 K. Kankova: Relationship between circulating levels of soluble RAGE (sRAGE) and genetic variability in the ager gene in subjects with diabetic nephropathy 12.45-13.45: Lunch 13.45-15.00 Poster session 14.30-18.30: The impact of new food technologies on the MR/AGE formation Chairs: Eyal Shimoni & Jenny Ames 15.00 P. Buera: Water and the kinetics of Maillard reaction: a new perspective 15.30 V. Gokmen: Modelling the Formation of Acrylamide in Glucose-Asparagine Model System Using Artificial Neural Network 16.00 N. Alt: Influence of new food processing techniques on protein glycation reactions 16.20-16.50: Coffee break 16.50 E. Shimoni: Reducing MRP's in liquid foods by ultra-high temperature ohmic heating 17.10 B. Cammerer: Shelf life of pea nuts with roasting degree 17.30 A. Arnoldi: Technological properties and non-enzymatic browning of lupin-based food products 17.50 R. Venkutonis: Effects of heating and natural antioxidants on the content of heterocyclic amines in meat 18.10 C. Billaud: Studies of the antioxidant activity of neoformed products from heated cysteine and aldehydes 20.30: Social dinner Friday, May 26 8.30-12.30: Formation pathways and detection of MRPs/AGEs in food and in vivo Chairs: Francisco Morales & Susan Thorpe 8.30 T. Hofmann: Taste-active glyco-conjugates and their formation upon thermal food processing 8.55 P. Thornalley: LC-MS/MS quantitation, hotspot site location and predicted structures of proteins glycated by dicarbonyls - a systems, information-rich approach 9.20 J. Baynes: Methionine Sulfoxide, a Sensitive Biomarker of Oxidative Damage to Proteins 9.45 R. Stadler: Recent advances in acrylamide analysis, formation and mitigation in foods 10.10-10.35: Coffee Break 10.35 S. Thorpe: S-(2-succinyl)cysteine: A novel chemical modification of tissue proteins 11.00 I. Blank: Formation of furan and methylfuran under roasting conditions 11.15 V. Yaylayan: Vinylogous Amadori rearrangement: consequences in food and in biological systems 11.30 I. Birlouez: Simultaneous analysis of reactive lysine, furosine and carboxymethyllysine by GC-MS: Application to a wide range of heat-treated foods 11.45 A. Jakas: Synthesis and stability of the early glycation products formed from d-fructose and endogenous opiod peptides 12.00 T. Fiedler: Carbohydrate based melanoidins, several alpha-dicarbonyl compounds as direct precursor for the formation of discrete molecular size domains 12.15 J. Hajslova: Study of "masked" acrylamide origin 12.30-13.30: Luncheon session The impact of food MRPs on human health Chairs: Simonetta Salvini & Josephine Forbes 12.35 S. Salvini: Problems in the assessment of MRP intake in humans 12.50 S. Tuijtelaars: Human exposure of acrylamide in food 13.10 N. Pellegrini: Coffee: a protective beverage? 13.30-15.00: Poster session 15.00-18.00: Monitoring and control of the Maillard Reaction in food and in vivo Chairs: Vincent Monnier & Vincenzo Fogliano 15.00 T. Miyata: Advanced glycation end products: Surrogate markers and therapeutic targets for diabetic renal injury 15.20 V. Monnier: Ascorbic acid as a Glycating Agent in Vivo 15.40 E. Van Schaftingen: Fructosamine-3-kinase and other enzymes involved in protein glycation 16.00 V. Fogliano: Amadoriase, a tool for inhibiting protein glycation and food browning 16.20-16.50: Coffee Break 16.50 T. Miyazawa: Amadori glycated phosphatidylethanolamine in food and human plasma 17.10 R. Nagai: Investigation of pathway for AGE formation in macrophages 17.30 Z. Ciesarova: Application of L-Asparaginase for acrylamide mitigation in potato products 17.50 S. Sivakami: The roles of dietary factors in preventing glycation mediated damage to DNA in a MG/LYS system 18.15 Report of IMARS activities 18.30-19.30: COST 927 Management Committee meeting (only for MC members) Saturday, May 27 8.30-12.30: AGE related pathologies: Diabetes, Lens and Renal Disease Chairs: Katerina Sebekova & Naoyuki Taniguchi 8.30 N. Taniguchi: Glycation and posttranslational modifications of antioxidative enzymes 9.00 A. Stitt: Pathogenic role of substrate-immobilized AGEs in diabetic retinopathy 9.25 M. Cooper: Tangled in a web of sugar: AGEs, their actions and reactions in diabetic complications 9.50 C. Schalkwijk: AGE/ALEs: non-traditional risk factors for vascular complications 10.15-10.45: Coffee break 10.45 G. Stein: Kidney and AGEs 11.10 J. De Groot: Advanced Glycation End products in the development of osteoarthritis 11.35 M. Pischetsrieder: Effects of Maillard reaction products on NFKB activation and expresion of proinflammatory markers - molecular mechanism 12.00 F. Facchiano: Sugar-induced modification of angiogenic growth factors: a structural and functional study 12.20: Meeting Closure 12.40: Lunch and tour to Pompei Oral programme S1 FORTY YEARS OF FUROSINE – FORTY YEARS OF USING MARKERS FOR MAILLARD REACTION IN FOOD AND NUTRITION Helmut F. Erbersdobler Institut für Humanernährung und Lebensmittelkunde, Düsternbrooker Weg 17, D-24105 Kiel Since about 60 years amino acid analysers were used in order to evaluate protein quality (1). However, soon it was known that this procedure was not reliable in heat damaged foods. It had to be recognized that in usually heated or stored foods especially lysine was less destroyed but nutritionally blocked, a fact which was not considered by the usual determination after acid hydrolysis. One of the first proposals for the determination of available lysine was labelling of the critical ε-amino group of lysine with fluoro- dinitrobenzene (2) which led to a worldwide application of this technique (e.g.3). However, to evaluate the intensity of the heating process it seems to be better to analyse new substances whose formation depends on different heating conditions. Moreover, meanwhile more sensitive indicators are wanted, suited to measuring also a low technical impact on protein quality e.g. in ultra high temperature treated milk. Since its detection forty years ago (4) as a stable indicator of the Amadori products (5,6,7) furosine was used as indicator of thermal damage in food science and medical biochemistry. Its use was enhanced by analytical improvements starting with the proposal of Schleicher et al. (8) and improved by Resmimi et al. (9). Especially after the commercial availability of a pure and stable standard the furosine analyses increased very much and are still in use (e.g.10). Furosine has the disadvantage that it is formed from the Amadori products only at a rate of 30-40%. However, this recovery is reproducible if constant analytical conditions are applied. Moreover, furosine increases not linearly with increasing heat damage since the Amadori products are only intermediates which react to further compounds in the advanced and late Maillard reaction. In more severely heated products furosine values reach a plateau or even decrease. On the other hand, furosine has the big advantage that it is a direct marker for a real existing reaction product of lysine, which is not only of analytical and technical but also of nutritional relevance. Furosine analyses were applied on many food items and especially on dairy products. Some items showed by this way a degree of inactivation up to one third, even to one half. In dairy products also hydroxymethylfurfural (HMF (11) is a common marker resulting also from the Maillard condensation. Data from the literature offer a wide range for this marker which suspect that the HMF determination is insufficiently reproducible between laboratories. However, several studies on UHT treated milks demonstrated the usefulness of the UHT-method as a rapid and simple measure of heat damage.
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