Negative impactsofin-vitrooxidative stress on the quality of heat-induced myofibrillar protein gelation during refrigeration

Abstract

To investigate the effects of pre-oxidized myofibrillar protein (MP) on stability of heat-induced MP gelation throughout 28 days of refrigeration, a hydroxyl radical generating system (10 μM FeCl 3 , 0.1 mM ascorbic acid, with 10 mM H 2 O 2) was employed. Results demonstrated that an increase of carbonyl content followed a similar trend in both pre-oxidized and nonoxidized protein gels. Unexpectedly, pre-oxidized protein gels yielded increased (P < 0.05) hardness at 14 days of storage compared to the initial day of storage. The water holding capacity (WHC) had a significant positive correlation with gel hardness, percentage of immobile water, and T 22 , while having a negative correlation with carbonyl group content and T 23 (P < 0.01). These results suggest that the pre-oxidation treatment increases the susceptibility of MP gel matrices to undergo oxidation and thus provides a better comprehension of the consequences that in vitro pre-oxidation treatments have on protein matrix systems.

Comparison between lipid and protein oxidation progress in the tail and claw muscles of signal crayfish (Pacifastacus leniusculus)

“…By contrast, protein oxidation especially, myofibrillar proteins during storage has a key role on the flesh quality and can decrease its tenderness and water holding capacity (WHC) (Xia et al, 2018). The alteration of seafood muscle texture during the post-mortem period has been previously confirmed by Fu et al (2014); and can be attributed to the degradation of myofibrillar proteins (Ouali et al, 2013).…”

Coating Effects of ε-Polylysine and Rosmarinic Acid Combined with Chitosan on the Storage Quality of Fresh Half-Smooth Tongue Sole (Cynoglossus semilaevis Günther) Fillets

“…LF-NMR has been perceived as an efficient technique to evaluate the freshness of fish, and MRI is also a complementary technology for understanding water migration [39]. In the present study, the shortest relaxation time T21 representing the bound water varied, ranging from 0.79% to 1.01% during storage (Table 4), which was due to the water entrapped within highly organized myofibril structures [40]. T22 with intermediate population of relaxation time was considered as immobile water within the myofibril and diminished progressively during storage (p ＜ 0.05).…”

Covalent chemical modification of myofibrillar proteins to improve their gelation properties: A systematic review

“…Loss of functionality might be induced by the polymerization and attenuated SH, causing reduced hydrogen bonding in the protein matrix (Li et al., 2013). Other studies on the effects of oxidation in chicken MPs proved that white muscle‐derived myosin was more susceptible to hydroxyl radicals than red muscle (Liu & Xiong, 2015), and oxidized MPs (10 mM H 2 O 2 ) did not maintain their gel‐forming ability during refrigeration storage (Xia et al., 2018).…”

“…The structure of pork MPs is more easily altered at high ferric ion concentrations, and the pattern of changes is independent from the content of FeCl 3 (Park, Xiong, & Alderton, 2007). Different sources of MPs have been subjected to the Fenton system with various concentrations of H 2 O 2 and evaluated for covalent modification and their effects on gelation properties, including pork (Xia et al., 2019; Xiong et al., 2010), chicken (Liu & Xiong, 2015; Xia et al., 2018), beef (Fu et al., 2019), and fish (Li, Kong, Xia, Liu, & Diao, 2013; Lu, Zhang, Li, & Luo, 2017).…”