Abstract

ABSTRACTWe analyzed the influence of temperature and heating time on rheological properties, and types of proteins involved in the gelation process of natural actomyosin from pork, chicken, and hake. At low temperatures (40–50°C) hake gels were stiffer than chicken or pork gels (due to setting); at higher temperatures (60°C), actomyosin from all three formed gels with similar rheological characteristics. Types of protein in the different fractions (analyzed by electrophoresis) were consonant with the rheological behavior of the AM gels for each heat treatment and species.

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