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Effect of Heating Rate on Thermally Formed Myosin, Fibrinogen and Albumin Gels
Author(s) -
FOEGEDING E.A.,
ALLEN C.E.,
DAYTON W.R.
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.tb10846.x
Subject(s) - fibrinogen , chemistry , myosin , albumin , solubility , phosphate buffered saline , turbidity , chromatography , biochemistry , organic chemistry , biology , ecology
ABSTRACT Myosin, fibrinogen and albumin gels were formed by heating in pH 6.0 phosphate buffer at three heating rates. Turbidity (A 660nm ) and solubility were monitored along with gel strength, as measured with an annular pump. Myosin and fibrinogen suspensions became turbid and solubility decreased as temperatures preceding the development of gel strength. Linearly increasing heating rates of 12°C/hr and 50°C/hr produced the strongest myosin and fibrinogen gels at 70°C, whereas albumin gels formed at 95°C by heating at 12°C/hr or constant heating for 20 min did not differ in strength.