HEAT-INDUCED GELATION AND PROTEIN-PROTEIN INTERACTION OF ACTOMYOSIN1

Authors

  • J. C. ACTON,

    1. Food Protein Research Grou Department of Food Science and Technology University of Nebraska—Lincoln Lincoln, Nebraska 68583
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    • 2

      Department of Food Science, Clemson University, Clemson, SC 29631.

  • M. A. HANNA,

    1. Food Protein Research Grou Department of Food Science and Technology University of Nebraska—Lincoln Lincoln, Nebraska 68583
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  • L. D. SATTERLEE

    1. Food Protein Research Grou Department of Food Science and Technology University of Nebraska—Lincoln Lincoln, Nebraska 68583
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  • 1

    Published as Paper No. 6153, Journal Series, Nebraska Agricultural Experiment Station, Lincoln, NE.

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.

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