Myofibrillar protein gel properties are influenced by oxygen concentration in modified atmosphere packaged minced beef

Abstract

Minced beef was stored for 8days and myofibrillar protein (MP) was extracted to investigate the effect of oxygen concentration (0, 20, 40, 60, and 80%) in modified atmosphere packaging (MAP) on heat-induced gel properties. Compression force of gels was lower when prepared from beef packaged in 0% oxygen, intermediate in 20 to 60% oxygen and greater in 80% oxygen. Total water loss of gels prepared from beef packaged with oxygen (20-80%) was higher and rheology measurements presented higher G' and G″ values. Additionally, gels from beef packaged without oxygen exhibited higher J (t) values during creep and recovery tests, demonstrating that oxygen exposure of meat during storage in MAP affect MP in such a way that heat-induced protein gels alter their characteristics. Generally, storage with oxygen in MAP resulted in stronger and more elastic MP gels, which was observed already at a relative low oxygen concentration of 20%.

Role of protein oxidation in the nutritional loss and texture changes in ready‐to‐eat chicken patties

“…The relationship between protein oxidation and texture changes in meat products has been documented in numerous studies (Lund et al, 2007;Ganhão et al, 2010;Smaoui et al, 2017;Wang et al, 2017). Protein cross-linking in meat products is typically identified as responsible for the texture deterioration by promoting the strengthening of the protein structure in the muscle tissue, which leads in turn to meat toughening (Lund et al, 2011).…”

“…In addition to the loss of their nutritional value, protein oxidation also affects the gelling properties of meat proteins and the texture of meat products (Smaoui et al, 2017). During the oxidative process, protein cross-links are formed, which increases the hardness of meat and meat products (Lund et al, 2007;Wang et al, 2017). Additionally, the accumulation of particular protein oxidation products during processing and digestion of muscle foods may also involve certain health risks due to the potential toxicity of these species (Soladoye et al, 2015;Est evez & Luna, 2017).…”

Myofibrillar protein oxidation affects filament charges, aggregation and water-holding

“…Recently, decreased water-holding of myofibril gels prepared from beef packaged with oxygen (20 -80%) has been reported (Wang, Luo, & Ertbjerg, 2017).…”

Effect of peroxyl radicals on the structure and gel properties of isolated rabbit meat myofibrillar proteins

“…) and protein cross‐linking (Fig. ) promoted the generation of large protein aggregates, hindering the ordered interactions of reactive functional groups, but this phenomenon was contrary to the generation of a three‐dimensional gel network (Wang et al ., 2017c). Furthermore, as a result of protein oxidation, excessive carbonylation also relatively weakens the gelling capacities of MPs to some extent (Utrera & Estévez, ).…”