L‐histidine inhibits the heat‐induced gelation of actomyosin in a low ionic strength solution

Abstract

AbstractThe heat‐induced gelation of actomyosin plays a key role in meat processing. Our previous study showed that L‐histidine could affect the characteristics of a heat‐induced gel of myosin on a low ionic strength. To apply the specific effect of L‐histidine to meat processing, the heat‐induced gel properties of actomyosin in the presence of L‐histidine were investigated. Actomyosin in a low ionic strength solution containing L‐histidine did not form a gel upon heating. The dynamic rheological properties of actomyosin in low ionic strength solutions were distinct depending on the presence or absence of L‐histidine. Electron microscopy showed that, heated at 50°C, actomyosin in a low ionic strength solution containing L‐histidine remained a filamentous structure. The surface hydrophobicity of actomyosin was stable up to 50°C in a low ionic strength solution containing L‐histidine. In conclusion, L‐histidine might suppress the aggregation of actomyosin and inhibit heat‐induced gelation in a low ionic strength solution.