The Effects of Lipid Oxidation Product Acrolein on the Structure and Gel Properties of Rabbit Meat Myofibrillar Proteins

Variation in the structure and emulsification of egg yolk high‐density lipoprotein by lipid peroxide

“…With the increasing concentration of AAPH, the content of the α‐helix decreased at 0–0.2 mmol/L AAPH and then increased at 0.2–10 mmol/L AAPH, the change in the β‐sheet content was exactly the opposite to that of the α‐helix content, while the β‐turn content and random coil content were increased significantly. Normally, the oxidation of AAPH causes the ordered α‐helix and β‐sheet structure in EYHDL to transform into a disordered random coil and β‐turn structure, and the increased α‐helix content in EYHDL under high‐oxidant conditions was different from that reported in previous related studies (Huang, Sontag‐Strohm, Stoddard, & Kato, ; Wang, He, Gan, & Li, ). Moderate oxidation can induce partial unfolding of the proteins, thereby exposing certain sites that are normally hidden within proteins (Estévez, ) and leading to a reduction in the intramolecular hydrogen bonds.…”

“…Normally, the oxidation of AAPH causes the ordered α-helix and β-sheet structure in EYHDL to transform into a disordered random coil and β-turn structure, and the increased α-helix content in EYHDL under high-oxidant conditions was different from that reported in previous related studies (Huang, Sontag-Strohm, Stoddard, & Kato, 2017;Wang, He, Gan, & Li, 2018). Moderate oxidation can induce partial unfolding of the proteins, thereby exposing certain sites that are normally hidden within proteins (Estévez, 2011) and leading to a reduction in the intramolecular hydrogen bonds.…”

Intake of Oxidized Proteins and Amino Acids and Causative Oxidative Stress and Disease: Recent Scientific Evidences and Hypotheses

“…The covalent linkage of malondialdehyde (MDA) or 4-hydroxy-2-nonenal (4-HNE) to food proteins, such as soy (Zhao, Chen, Zhu, & Xiong, 2012), meat (Zhou, Sun, & Zhao, 2015), fish (Hu et al, 2017;Wang, Zhang, Fang, & Bhandari, 2017), and dairy (Gürbüz & Heinonen, 2015) proteins, as well as myoglobin (Maheswarappa, Rani, Kumar, Kulkarni, & Rapole, 2016) has been found to cause impairment of the functionality and digestibility of the latter. A recent study by Wang, He, Gan, and Li (2018) proved the ability of acrolein, a potentially toxic lipid oxidation product, to impair the native structure and gel properties of rabbit meat myofibrillar proteins.…”

Oxidized Milk Induces Spatial Learning and Memory Impairment by Altering Gut Microbiota in Offspring Mice during Pregnancy and Lactation

“…The Organization for Economic Cooperation and Development (OECD) and the Food and Agriculture Organization of the United Nations (FAO) clearly stated in the ″Agricultural Outlook Report 2019-2028″ that the production and consumption of dairy products are expected to increase in the coming years. Raw milk and dairy products contain more unsaturated fatty acids, radiation, free radicals, and metal catalysts, they may induce milk to oxidize during processing and storage, causing changes in its physicochemical properties, such as gelling and emulsification, and changes in functions, such as hydration and digestion, affecting nutritional quality. − In addition, if dairy oxidatively modified products accumulate in the body, they may induce pathological changes such as aging, diabetes, and chronic kidney disease. − Over the past decades, researchers have reported various oxidants during food processing and storage, for instance, radiation, free radicals, and high oxygen, not only easily cause lipid oxidation rancidity but also induce protein oxidation. − Proteins, peptides, and amino acids undergo oxidative damage when subjected to ·OH and O 2– environments. , In addition, proteins and amino acids are strongly oxidized when placed in metal refinement oxidation systems, and proteins were mainly affected by ·OH. , Protein oxidation can produce a variety of chemical modifications resulting in oxidation products, including the formation of carbonyl derivatives, amino acid side-chain modifications, protein backbone cleavage, and formation of protein cross-linkages. , Some studies highlight that potentially toxic products can be ingested through food that is absorbed across the intestines and distributed in blood. , In the gastrointestinal tract and various internal organs, cellular responses to molecular changes in oxidative modification of proteins often involve specific signaling pathways . Our previous studies showed that oxidized casein damages the antioxidant defense system and causes oxidative stress and inflammation through the accumulation of protein oxidation products, such as dityrosine (Dityr), 3-nitrotyrosine (3-NT), and advanced oxidation protein products (AOPPs) .…”