HEAT-INDUCED GELATION OF ACTOMYOSIN

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-degrees-C), but decreased with increasing pH (5.5-9.0). Low heating temperatures (50-55-degrees-C) favoured the formation of more cohesive actomyosin gels than the higher heating temperatures (60-75-degrees-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 mM) reduced gel strength but did not affect gel cohesiveness.