Heat‐induced gelation of myofibrillar proteins and myosin (0.6M; pH 6.0) from rabbit fast‐ and slow‐twitch muscles was analyzed by thermal scanning rheometry. Proteins from slow‐twitch muscle exhibited higher thermostability and lower gel strength than those from fast‐twitch muscle. Purifying myosin from myofibrillar proteins changed heat‐gelation profiles and generally increased gel rigidity at 80°C. However, the effect of some proteins on the gelation of myosin was muscle dependent. Complete elimination of actin decreased the heat‐gelling ability of slow myosin and increased that of fast myosin. Also, elimination of C‐protein led to a greater increase in rigidity of gels from slow myosin than from fast myosin. The heat‐behavior of the different protein fractions was related to the degree and type of aggregation in the gel.
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Boyer et al. (1996) studied this question.
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