HEAT-INDUCED GELATION AND PROTEIN-PROTEIN INTERACTION OF ACTOMYOSIN

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Abstract
Natural actomyosin (NAM) and “crude” actomyosin formed gels yielding maximum strengths (from back extrusion force) at pH 5.0 and 5.5, respectively. At pH 6.0, NAM gels had a least protein concentration endpoint (LCE) value of 6 mg/ml. Gel strength increased exponentially with an increase of NAM concentration from 3.75–10 mg/ml. With constant time (30 min)-temperature heating, NAM gel forces increased by 20.5% (NS, P>0.05) in the 30–80°C range. Arrhenius plots of NAM interaction in solution and in gelation at pH 6.0 indicated two different reaction mechanisms within the temperature zones above and below approximately 35°C for solutions and 40°C for gels. Similarity of interaction slopes above the 35–40°C region suggested one reaction mechanism for NAM molecular aggregation in solution and gelation.