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Keywords:

  • myosin;
  • glycinin;
  • aggregation;
  • a-helix;
  • pale soft exudative

ABSTRACT The pale, soft, and exudative (PSE) condition in pork meat has been associated with protein dena-turation that leads to loss of functional properties. The effect of soy glycinin addition to model systems of actomyosin from PSE or normal meat on biophysical properties was evaluated. Although the functional properties depended on actomyosin concentration, a 75% actomyosin/25% glycinin mixture presented acceptable properties with both types of actomyosin. This combination was used to investigate protein-protein interactions. Gel strength correlated with intermediate a-helical content and protein aggregation. Changes in protein secondary structure probably added to protein denaturation appear to be necessary to improve gelation and water retention in PSE actomyosin-glycinin combinations.