Effect of Malondialdehyde-Induced Oxidation Modification on Physicochemical Changes and Gel Characteristics of Duck Myofibrillar Proteins

Abstract

This paper focuses on the effect of malondialdehyde-induced oxidative modification (MiOM) on the gel properties of duck myofibrillar proteins (DMPs). DMPs were first prepared and treated with oxidative modification at different concentrations of malondialdehyde (0, 0.5, 2.5, 5.0, and 10.0 mmol/L). The physicochemical changes (carbonyl content and free thiol content) and gel properties (gel whiteness, gel strength, water holding capacity, rheological properties, and microstructural properties) were then investigated. The results showed that the content of protein carbonyl content increased with increasing MDA oxidation (p < 0.05), while the free thiol content decreased significantly (p < 0.05). Meanwhile, there was a significant decrease in gel whiteness; the gel strength and water-holding capacity of protein gels increased significantly under a low oxidation concentration of MDA (0–5 mmol/L); however, the gel strength decreased under a high oxidation concentration (10 mmol/L) compared with other groups (0.5–5 mmol/L). The storage modulus and loss modulus of oxidized DMPs also increased with increasing concentrations at a low concentration of MDA (0–5 mmol/L); moreover, microstructural analysis confirmed that the gels oxidized at low concentrations (0.5–5 mmol/L) were more compact and homogeneous in terms of pore size compared to the high concentration or blank group. In conclusion, moderate oxidation of malondialdehyde was beneficial to improve the gel properties of duck; however, excessive oxidation was detrimental to the formation of dense structured gels.

Protein oxidation‐induced changes in the physicochemical properties and quality of plant food

“…Studies have shown that oxidation treatment could promote the formation of oxidised aggregates with β1‐sheet structure through hydrophobic interaction, resulting in a reduction in the solubility, emulsification ability and interfacial activity of SPI (Zhao et al ., 2021). Generally, the greater the degree of oxidation, the worse the solubility of the protein (Zhu et al ., 2022). The solubility of peanut arachin decreased to a minimum of 65% when AAPH concentration is 10 mmol/L, which is due to the formation of soluble aggregates.…”

Effects of 2,2′-Azobis(2-methylpropionamidine) Dihydrochloride Stress on the Gel Properties of Duck Myofibrillar Protein Isolate

“…We revealed that excessive oxidation led to the explicit cross-linking of DMPs, which negatively affected the gel-forming capacities of DMPs by hydroxy radicals and malondialdehyde. However, the moderate oxidation of malondialdehyde was beneficial for improving its gel-forming properties [ 7 , 8 ]. 2,2′-azobis(2-methylpropionamidine) dihydrochloride (AAPH) generates alkylperoxyl radicals upon degradation, which preferentially oxidize their main targets, tryptophan, cysteine, methionine, tyrosine and, to a lesser extent, histidine residues, respectively, thereby causing protein oxidation [ 9 , 10 ].…”