Heat-induced gelation of actomyosin

E O'Neill; P A Morrissey; D M Mulvihill

doi:10.1016/0309-1740(93)90094-X

Heat-induced gelation of actomyosin

Meat Sci. 1993;33(1):61-74. doi: 10.1016/0309-1740(93)90094-X.

Authors

E O'Neill¹, P A Morrissey, D M Mulvihill

Affiliation

¹ Department of Food Chemistry, University College, Cork, Ireland.

PMID: 22059944
DOI: 10.1016/0309-1740(93)90094-X

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 mM) reduced gel strength but did not affect gel cohesiveness.