High-pressure homogenization combined with sulfhydryl blockage by hydrogen peroxide enhance the thermal stability of chicken breast myofibrillar protein aqueous solution.

This study tested the potential of high-pressure homogenization (HPH, 69 MPa) combined with hydrogen peroxide (HO, at 0, 40, 80, 160 and 320 μmol/g protein) on enhancing the stability of myofibrillar protein (MP, 15 mg/mL) against thermal aggregation (95 °C for 10 min) in aqueous solution. The addition of HO blocked the sulfhydryl (SH) groups, inhibited the formation of disulfide bonds, and suppressed thermal aggregation of MP. HPH facilitated the blockage effect of HO by disrupting the intact myofibril structure and exposing buried -SH groups, and this resultedin stronger inhibition of thermal aggregation therefore improved solubility of MP. More than 75% of heated MP remained soluble after the treatment with HPH and 160 μmol/g HO, while untreated samples formed a gel upon heating. These results proved that HPH combined with HO is an effective strategy to promote heat stability of MP in the development of muscle protein-based beverages.