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EMULSION CAPACITY AND TIMED EMULSIFICATION OF CHICKEN BREAST MUSCLE MYOSIN
Author(s) -
GALLUZZO S. J.,
REGENSTEIN J. M.
Publication year - 1978
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.1365-2621.1978.tb07407.x
Subject(s) - chromatography , emulsion , chemistry , creaming , myosin , sodium dodecyl sulfate , centrifugation , mixing (physics) , sodium , biochemistry , organic chemistry , physics , quantum mechanics
Methods are described for the study of the role of muscle proteins in meat emulsion formation. Chicken myosin was used to optimize emulsifying capacity (E.C.) and timed emulsification conditions for a Sorvall Omni‐mixer equipped with 50 ml polycarbonate tubes. Optimal conditions for E.C. were a 0.9–1.2 ml sample volume, 6,000 rpm mixing rate and 0.25 ml oil/set addition rate. The oil (colored with 0.3g Oil Red 0/liter oil) was kept below 6°C, and the E.C. test was done in an ice bath. Emulsifying capacity was fairly constant over the 0.3–1.0M NaCl range, decreasing when salt concentration fell to 0.10M. Optimal conditions for timed emulsification were 3 ml sample:6 ml oil, and a 6,000 rpm mixing rate for up to 5 min. Creaming of the emulsions was accomplished by centrifugation at 30,000 XG for 15 min. The aqueous phase was then analyzed via the Lowry method and by SDS (sodium dodecyl sulfate) gel electrophoresis. Myosin exhibited four bands, namely the heavy chain and the three light chains, which could be monitored by using both 6% and 12% SDS gels and an actin internal standard. Densitometric areas were converted to mole: mole ratios using a dye‐binding factor of 1.0.