Comparative study on the stability of fish actomyosin and pork actomyosin.

Effects of temperature, pH and ionic strength on the stability of actomyosin (AM) from fish and pork were studied using UV spectra, solubility, turbidity, and sulfhydryl group content measurement for comparison. Pork AM exhibited higher stability to cold storage and heating than fish AM. The unfolding rate of AM increased with increasing temperature. Intense aggregation occurred over 30 °C for fish AM and 40 °C for pork AM. New disulfide bonds mainly formed over 40 °C for fish AM and 60 °C for pork AM. Pork AM exhibited the higher turbidity than fish AM in the range of 50-90 °C, suggesting the higher extent of aggregation of pork AM. Ionic strength mainly influenced solubility of AM, but there was no effect on cleavage and formation of disulfide bond. The lowest solubility of both AM was at pH 5.42. Additionally, fish AM was more sensitive to pH changes than pork AM. Crown