Changes in Shear Parameters, Protein Degradation and Ultrastructure of Pork Following Water Bath and Ohmic Cooking

Influence of stewing time on the texture, ultrastructure and in vitro digestibility of meat from the yellow‐feathered chicken breed

“…These results were consistent with reports in poultry and pork (Kong et al 2008a;Huang et al 2011;Dai et al 2014). The generation of gaps could be contributed to the denaturation of major component protein of Z lines and I bands, such as a-actinin, troponin T, titin and nebulin that are more sensitive to heat processing (Dai et al 2014). 1b), which agreed well with the results reported in beef and pork meat (Huang et al 2011;Li et al 2013).…”

“…Moreover, the connections between thin filaments and Z lines weakened, as evidenced by gaps formed on both sides of the Z lines (Fig. The connections near the Z lines continuously weakened, which could be attributable to the enhanced protein denaturation of Z lines and I bands (Dai et al 2014). The generation of gaps could be contributed to the denaturation of major component protein of Z lines and I bands, such as a-actinin, troponin T, titin and nebulin that are more sensitive to heat processing (Dai et al 2014).…”

“…These reactions generally consist of aggregation, denaturation, and degradation of myofibrillar and sarcoplasmic proteins, and solubilization and gel formation of connective tissues (Kong et al 2008a;Isleroglu et al 2014;Kaur et al 2014). During cooking, the myofibrils structure changes progressively, including that the I bands become shortened and more condensed and that the A bands appear slightly stretched (Huang et al 2011;Dai et al 2014). During cooking, the myofibrils structure changes progressively, including that the I bands become shortened and more condensed and that the A bands appear slightly stretched (Huang et al 2011;Dai et al 2014).…”

Cooking‐Induced Protein Modifications in Meat

“…MS analysis of the gel bands revealed that proteins exhibited various degrees of tolerance to heating: for example, myosin heavy chain (224 kDa) and myoglobin (17 kDa) being distinctively intolerant, glycogen phosphorylase (98 kDa) and actin and creatine kinase (42 kDa) being more tolerant, whereas triosephosphate isomerase (27 kDa) and myosin light chain 3 (22 kDa) were stable even at 100 °C (molecular masses listed in this sentence are based on the theoretical values). In another recent study on pork, Dai and others () reported that the myosin light‐chain bands of myofibrillar protein fraction became more intensely stained in meat cooked to the end point internal temperatures of 80 and 100 °C. The authors suggested that this might be a result of their comigration with degradation products of myosin.…”

Salt Intake from Processed Meat Products: Benefits, Risks and Evolving Practices

“…As the amount of myoglobin depends, among other factors, on the breed, the age, the weight, the sex of the animal, and the nature of the muscle fibers, PMP color is influenced by such intrinsic factors as the overall quality of the fresh meat (Cannon et al, 1995;Lee et al, 2012;Lewis, Brown & Heck, 1962;Nam et al, 2009;Pettigrew & Esnaola, 2001;Rosenvold & Andersen, 2003;Suman, Hunt, Nair, & Rentfrow, 2014). In addition, storage (Lien et al, 2002a(Lien et al, , 2002b, packaging system (De Santos, Rojas, Lockhorn, & Brewer, 2007;Wicklund et al, 2006), and cooking method (Chiavaro, Rinaldi, Vittadini, & Barbanti, 2009;Dai et al, 2013Dai et al, , 2014Vittadini, Rinaldi, Chiavaro, Barbanti, & Massini, 2005) can influence the internal cooked color of pork products. Technological processes (presalting, salting, steaming, temperature rising, cooking, cooling, thawing, storage conditions) influence pigment and then color (Lien et al, 2002a).…”