Effect of oxidation on the gel properties of porcine myofibrillar proteins and their binding abilities with selected flavour compounds.

In this work, the effect of oxidation induced by hydroxyl radicals on the binding abilities of myofibrillar protein (MP) gels to aldehydes and ketones and their relationship with MP gel properties were investigated. Mild oxidation (0-0.2 mM H2O2) could induce partial unfolding of MP, thus slightly increasing the salt solubility of MP and enhancing the hardness of MP gels. MP suffering a higher oxidative attack could undergo a reduction in water-holding capacity, with increased mobility of water in MP gels. Oxidation could make MP gel more disordered. The ability of oxidised MP gels to bind to flavours decreased as the carbon chain length of the flavour compound increased. MP oxidation only significantly affected the binding of MP gels to hexanal, heptanal, and 2-octanone, while other flavour compounds were not affected.