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

•Enhanced heat stability of myofibrillar protein (MP) aqueous solution is warranted.•H2O2 blocked its sulfhydryl group and inhibited disulfide mediated cross-linking.•High-pressure homogenization (HPH) facilitated the blockage effect of H2O2.•Thermal aggregation was suppressed, leading to an improved solubility of MP.•HPH combined with H2O2 is an effective strategy to promote its heat stability. This study tested the potential of high-pressure homogenization (HPH, 69 MPa) combined with hydrogen peroxide (H2O2, 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 H2O2 blocked the sulfhydryl (SH) groups, inhibited the formation of disulfide bonds, and suppressed thermal aggregation of MP. HPH facilitated the blockage effect of H2O2 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 H2O2, while untreated samples formed a gel upon heating. These results proved that HPH combined with H2O2 is an effective strategy to promote heat stability of MP in the development of muscle protein-based beverages.