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 (H ₂ O ₂ , 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 H ₂ O ₂ blocked the sulfhydryl (SH) groups, inhibited the formation of disulfide bonds, and suppressed thermal aggregation of MP. HPH facilitated the blockage effect of H ₂ O ₂ 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 H ₂ O ₂ , while untreated samples formed a gel upon heating. These results proved that HPH combined with H ₂ O ₂ is an effective strategy to promote heat stability of MP in the development of muscle protein-based beverages.