Abstract
Rheological properties of actomyosin gels were markedly affected by protein concentration, pH and heating temperature. Gel strength increased with increasing protein concentration (30–60 mg ml −1) and heating temperature (55–75°C), but decreased with increasing pH (5·5–9·0). Low heating temperatures (50–55°C) favoured the formation of more cohesive actomyosin gels than the higher heating temperatures (60–75°C). Gels formed at low pH (5·5 and 6·0) were less cohesive than those formed at high pH (7·5–9·0). Addition of ATP and pyrophosphate (10 mm) prior to heating decreased gel strength and cohesiveness, whereas EDTA (1–5 m M) reduced gel strength but did not affect gel cohesiveness.
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