This paper reviews some of the research designed to lead to an increased understanding of the chemistry of the Maillard reaction, based on recent developments, and its influence on food properties like colour, flavour and nutritional value A critical analysis is given on how quality attributes associated with Maillard reaction can be predicted and controlled by kinetic modelling Multiresponse modelling (taking more than one reactant and product into consideration in the modelling process) is a powerful tool to model complicated consecutive and parallel reactions, like the Maillard reaction Such a multiresponse approach provides a major guidance in understanding the reaction mechanism An illustrative example is given

/pdf/a-review-of-maillard-reaction-in-food-and-implications-to-4jgu3amkqv.pdf

A review of Maillard reaction in food and implications to kinetic modelling

Enzymatic and nonenzymatic browning reactions of amino acids and proteins with carbohydrates, oxidized lipids, and oxidized phenols cause deterioration of food during storage and processing. The loss in nutritional quality and potentially in safety is attributed to destruction of essential amino acids, decrease in digestibility, inhibition of proteolytic and glycolytic enzymes, interaction with metal ions, and formation of antinutritional and toxic compounds. Studies in this area include influence of damage to essential amino acids on nutrition and food safety, nutritional damage as a function of processing conditions, and simultaneous formation of deleterious and beneficial compounds. These compounds include kidney-damaging Maillard reaction products, mutagens, carcinogens, antimutagens, antioxidants, antibiotics, and antiallergens. This overview covers the formation, nutrition, and safety of glycated proteins, characterized browning products, and heterocyclic amines. Possible approaches to inhibiting browning reactions and preventing adverse effects of browning during food processing and food consumption, including protection against adverse effects of heterocyclic amines by N-acetylcysteine, caffeine, chlorophyll, conjugated linoleic acid, lignin, and tea extracts, are also described. This research subject covers a complex relationship of the chemistry, biology, and pathology of browning products and the impact on human nutrition and health. Future study should differentiate antinutritional and toxicological relationships, define individual and combined potencies of browning products, and develop means to prevent the formation and to minimize the adverse manifestations of the most antinutritional and toxic compounds. Such studies should lead to better and safer foods and improved human health.

http://nfscfaculty.tamu.edu/talcott/courses/FSTC605/Papers%20Reviewed/Food%20Browning.pdf

Food browning and its prevention: an overview

http://depa.fquim.unam.mx/amyd//archivero/GRUPO5_25541.pdf

Effect of heating on Maillard reactions in milk.

Smokers have a significantly higher risk for developing coronary and cerebrovascular disease than nonsmokers Advanced glycation end products (AGEs) are reactive, cross-linking moieties that form from the reaction of reducing sugars and the amino groups of proteins, lipids, and nucleic acids AGEs circulate in high concentrations in the plasma of patients with diabetes or renal insufficiency and have been linked to the accelerated vasculopathy seen in patients with these diseases Because the curing of tobacco takes place under conditions that could lead to the formation of glycation products, we examined whether tobacco and tobacco smoke could generate these reactive species that would increase AGE formation in vivo Our findings show that reactive glycation products are present in aqueous extracts of tobacco and in tobacco smoke in a form that can rapidly react with proteins to form AGEs This reaction can be inhibited by aminoguanidine, a known inhibitor of AGE formation We have named these glycation products “glycotoxins” Like other known reducing sugars and reactive glycation products, glycotoxins form smoke, react with protein, exhibit a specific fluorescence when cross-linked to proteins, and are mutagenic Glycotoxins are transferred to the serum proteins of human smokers AGE-apolipoprotein B and serum AGE levels in cigarette smokers were significantly higher than those in nonsmokers These results suggest that increased glycotoxin exposure may contribute to the increased incidence of atherosclerosis and high prevalence of cancer in smokers

https://www.pnas.org/content/pnas/94/25/13915.full.pdf

Tobacco Smoke is a Source of Toxic Reactive Glycation Products

Meat products can be contaminated with carcinogenic N-nitrosamines, which is ascribed to the reaction between a nitrosating agent, originating from nitrite or smoke, and a secondary amine, derived from protein and lipid degradation. Although in model systems it is demonstrated that many amine containing compounds can be converted to N-nitrosamines, the yield is dependent of reaction conditions (e.g., low pH and high temperature). In this article, the influence of the composition of the meat products (e.g., pH, aw, spices) and processing (e.g., ageing, ripening, fermentation, smoking, heat treatment and storage) on the presence and availability of the amine precursors and the N-nitrosamine formation mechanism is discussed. In addition, this article explores the current N-nitrosamine mitigation strategies in order to obtain healthier and more natural meat products.

Volatile N-nitrosamines in meat products: Potential precursors, influence of processing, and mitigation strategies.

The degradation of nitrite and the inhibition towards formation of carcinogenic nitrosamines by melanoidins, produced from the glucose-glycine system were investigated at various conditions. The degradation of nitrite was highest at pH 1.2 (29%), when the ratio of melanoidins to nitrite was 1: 3. The inhibition towards formation of nitrosamines by melanoidins had the same tendency as the degradation of nitrite, the inhibition also being highest at pH 1.2 (99%). In addition, melanoidins after nitrite treatment exhibited a little higher mutagenicity and much stronger desmutagenicity than those of the original melanoidins. The change of the structure of melanoidins after treating with nitrite was also investigated by HPLC and CP-MAS NMR.

Inhibition of Nitrosamine Formation by Nondialyzable Melanoidins

The desmutagenic activities of low-molecular weight melanoidins (LM-MEL, MW 500–1000) and nondialyzable melanoidins (ND-MEL, MW above 1000) prepared from a glucose–glycine reaction system were examined by Ames’ test on such mutagens/carcinogens as nitro or amino compounds of aromatics or heterocycles, azo compounds, nitroso compounds, and epoxides.ND-MEL and LM-MEL exhibited a desmutagenic activity of 25–75% against mutagenic aromatic or heterocyclic compounds such as aflatoxin B1, B[α]P, 2-aminofluorene, 4-aminobiphenyl, and 2-aminonaphthalene, as well as heterocyclic amines, using S. typhimurium TA98 in the presence of S9 mix. In the case of using S. typhimurium TA100 in the absence of S9 mix, ND-MEL and LM-MEL showed a desmutagenic activity of 20–50% against 2-nitrofluorene, 4NQO and 2-nitronaphthalene. The strong desmutagenic activity of MEL from various kinds of amino acids, peptides, or egg albumin hydrolyzates with glucose was also observed against Trp-P-1. Furthermore, MEL had marked desmutagenic ...

Desmutagenicity of Melanoidins against Various Kinds of Mutagens and Activated Mutagens.

Two kinds of melanoidins formed between glucose and glycine with average molecular weights of 800 (low-MW MEL) and 3000 (high-MW MEL) were investigated for their absorption and distribution in rats. Seven hours after its oral administration, [14C] low-MW MEL underwent absorption by 12.8%, which was distributed in liver, kidney, urine, blood, and breath (CO2) with percentages of 2.2, 0.5, 5.7, 1.2, and 3.1, respectively. On the other hand, [14C] high-MW MEL was absorbed to a lesser extent (less than 1% of the initial administration). The results of gel permeation chromatography analyses for melanoidins showed that [14C] high-MW MEL and [14C] low-MW MEL with average MWs of 2000 and 500, respectively, were excreted into the urine, and that 80% of [14C] low-MW MEL was present in a form bound to protein in the plasma. The protein-bound MEL had a desmutagenic activity against Trp-P-1. It thus is reasonable to consider that absorbed MEL (MW above 500) and protein-bound MEL may actually act as desmu-tagens in vivo.

Absorption and Distribution of [14C]Melanoidins in Rats and the Desumtagenicity of Absorbed Melanoidins against Trp-P-1

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Inhibition of Nitrosamine Formation by Nondialyzable Melanoidins

Desmutagenicity of Melanoidins against Various Kinds of Mutagens and Activated Mutagens.

Absorption and Distribution of [14C]Melanoidins in Rats and the Desumtagenicity of Absorbed Melanoidins against Trp-P-1