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HEAT STABILITY OF CHICKEN ACTOMYOSIN
Author(s) -
YOUNG LOUIS L.
Publication year - 1974
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.1974.tb02902.x
Subject(s) - chemistry , heat stability , food science , thermal stability , sucrose , solvent , ionic bonding , chromatography , biochemistry , ion , organic chemistry , materials science , composite material
The heat sensitivity of chicken actomyosin was determined under varying conditions of the pH and ionic environment and in the presence and absence of various additives. The emulsifying capacity of the protein was used as the index of heat damage. As the pH of the solvent was increased above 8.5, the stability of the protein increased. It was more stable in 0.6M KC1 than in 0.2M KCl. Up to 6% sucrose significantly improved the stability. Polyphosphates were beneficial in stabilizing the actomyosin. This information should facilitate development of methods of heat pasteurizing mechanically deboned chicken meat.