Disulfide Bonds Influence the Heat‐induced Gel Properties of Chicken Breast Muscle Myosin

Abstract

The functions of thiol groups in the denaturation, aggregation and gelation of chicken breast muscle myosin during heating in 0.6M NaCl, 50mM sodium phosphate buffer, pH 6.5, was investigated by inhibiting disulfide (SS) bond formation using dithiothreitol (DTT). The endotherm of myosin heated in the presence or absence of DTT had similar thermal transition temperatures. Preventing SS bond formation increased the onset temperature for aggregation and gelation and decreased the elastic-like properties of the final gel matrix. Results indicated that SS bond formation was not a prerequisite for the gelation of chicken breast myosin. However, intermolecular SS bonds, especially from thiol groups on subfragment-1, contributed to gel network formation.

Influence of pH on the solubility and conformational characteristics of muscle proteins from mullet (Mugil cephalus)

“…Similar trends were observed as a result of pH induced folding and unfolding of cod myosin [15]. In rabbit myosin it has been reported that only one fifth of its reactive sulphydryl groups is located in the myosin light chain while remaining in the head region [32]. The increased reactive sulphydryl groups indicated possible structural transitions in the head region of myosin [29].…”

Effects of Ionic Strength on Chemical Forces and Functional Properties of Heat-induced Myofibrillar Protein Gel

“…Previous literatures have showed the importance of chemical forces in heat-induced protein gels. Smyth et al (1998) found that hardness of myosin gel could be weakened by adding dithiothreitol (DTT) to prevent the formation of disulfide bonds.…”

“…Previous literatures have showed the importance of chemical forces in heat-induced protein gels. Smyth et al (1998) found that hardness of myosin gel could be weakened by adding dithiothreitol (DTT) to prevent the formation of disulfide bonds. Liu and Hsieh (2007) studied the molecular interactions of protein gels by adding DTT, urea and other reagents, and they concluded that non-covalent bonds played a more important role than disulfide bonds in the formation of heat-induced protein gels.…”

“…Previous literatures have showed the importance of chemical forces in heat-induced protein gels. Smyth et al (1998) found that hardness of myosin gel could be weakened by adding dithiothreitol (DTT) to prevent the formation of disulfide bonds.Liu and Hsieh (2007) studied the molecular interactions of protein gels by adding DTT, urea and other reagents, and they concluded that non-covalent bonds played a more important role than disulfide bonds in the formation of heat-induced protein gels. Hermansson (1979) found that when less net electric charge were distributed on the surface of protein molecules, the electrostatic repulsion, hydrophobic attractions and intermolecular hydrogen bonds could keep a better balance, which made it easier to form ordered gel network.…”

Accurate determination of endpoint temperature of cooked meat after storage by Raman spectroscopy and chemometrics

“…2B) indicates the involvement of intermolecular disulfide bonds in network formation at the higher cooking temperatures (Smyth, Smith, & O'Neill, 1998;Sugeta, Go, & Miyazawa, 1973). In summary, Raman spectroscopy revealed the structural changes in protein secondary structure and that this information is useful to predict the EPT even after storage time up to 8 days.…”