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Interaction of Myosin‐Albumin and Myosin‐Fibrinogen to Form Protein Gels
Author(s) -
FOEGEDING E.A.,
DAYTON W.R.,
ALLEN C.E.
Publication year - 1986
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.1365-2621.1986.tb10847.x
Subject(s) - myosin , albumin , fibrinogen , chemistry , phosphate buffered saline , chromatography , biochemistry , biophysics , biology
Myosin, fibrinogen, albumin, myosin‐fibrinogen and myosin‐albumin gels were formed by heating in pH 6.0 phosphate buffer at two heating rates. Gel strength was measured with an annular pump and soluble protein was determined. Myosin and fibrinogen interacted to form a gel which was stronger than the sum of the gel strengths for the two individual proteins. The strength of myosin‐fibrinogen gels formed at 50°C was not affected by heating method; however, the strength of gels developed between 55°C and 70°C was related to heating method. Myosin and albumin did not interact to form a gel matrix until 80°C where sufficient thermal alteration of albumin had occurred.