Abstract
The Maillard reaction is a simple but ubiquitous reaction that occurs both in vivo and ex vivo during the cooking or processing of foods under high-temperature conditions, such as baking, frying, or grilling. Glycation of proteins is a post-translational modification that forms temporary adducts, which, on further crosslinking and rearrangement, form permanent residues known as advanced glycation end products (AGEs). Cooking at high temperature results in various food products having high levels of AGEs. This review underlines the basis of AGE formation and their corresponding deleterious effects on the body. Glycated Maillard products have a direct association with the pathophysiology of some metabolic diseases, such as diabetes mellitus type 2 (DM2), acute renal failure (ARF), Alzheimer’s disease, dental health, allergies, and polycystic ovary syndrome (PCOS). The most glycated and structurally abundant protein is collagen, which acts as a marker for diabetes and aging, where decreased levels indicate reduced skin elasticity. In diabetes, high levels of AGEs are associated with carotid thickening, ischemic heart disease, uremic cardiomyopathy, and kidney failure. AGEs also mimic hormones or regulate/modify their receptor mechanisms at the DNA level. In women, a high AGE diet directly correlates with high levels of androgens, anti-Müllerian hormone, insulin, and androstenedione, promoting ovarian dysfunction and/or infertility. Vitamin D3 is well-associated with the pathogenesis of PCOS and modulates steroidogenesis. It also exhibits a protective mechanism against the harmful effects of AGEs. This review elucidates and summarizes the processing of infant formula milk and the associated health hazards. Formulated according to the nutritional requirements of the newborn as a substitute for mother’s milk, formula milk is a rich source of primary adducts, such as carboxy-methyl lysine, which render an infant prone to inflammation, dementia, food allergies, and other diseases. We therefore recommend that understanding this post-translational modification is the key to unlocking the mechanisms and physiology of various metabolic syndromes.
Highlights
A Brief Glance at Advanced Glycation End Products (AGEs)Cooking practices have evolved, along with the evolution of man, from eating raw meat to cooking on low flame and later modernized to high flame cooking, such as baking, caramelizing, or preserving meats with sugar and spices
A-ApoA-II protein depositions were in the range 1.1 ± 0.2 A.U., which were lower in Receptor of AGE (RAGE)-l, compared to wild types having
Commonly known as protein glycation, normally occurs in vivo as well as during the preparation of foods at high temperatures. Though it is a simple reaction, elevated serum levels of AGE are risk factors associated with the physiology of various metabolic disorders
Summary
Along with the evolution of man, from eating raw meat to cooking on low flame and later modernized to high flame cooking, such as baking, caramelizing, or preserving meats with sugar and spices. Biomolecules 2019, 9, 888 and deep-frying, enhance the flavor of food and the desired texture in the final cooked product This is attributable to a unique chemical reaction known as the Maillard reaction [1]. Reducing sugars (glucose, galactose, and fructose) readily bind with the amino group of free lysine, arginine, and sometimes cysteine, tryptophan, and histidine, resulting in the formation of the Maillard reaction glycated products These products undergo conformational changes (such as rearrangement of the molecules), which stabilizes them into the final heterogeneous products, abbreviated as AGEs (Figure 2) Following their conformational changes, the products bind tightly with proteins available in the vicinity [6] and further crosslink with long-lived proteins, such as collagen, lens protein [4], hemoglobin [7], lysozyme, alkaline phosphatase, elastin, etc. Enzyme-linked immunosorbent assay (ELISA)-based immunochemical detection [9,21]; High-performance liquid chromatography (HPLC) [22]; Fluorescence detection, as some AGEs emit characteristic fluorescence [9]; Mass spectrometry; Gas chromatography with mass spectrometry [23]; MALDI-TOF mass spectrometry [24]; Western or dot-blot assays [18]
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