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EMULSION CAPACITY AND TIMED EMULSIFICATION OF CHICKEN BREAST MUSCLE MYOSIN

EMULSION CAPACITY AND TIMED EMULSIFICATION OF CHICKEN BREAST MUSCLE MYOSIN ABSTRACT 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. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Journal of Food Science Wiley

EMULSION CAPACITY AND TIMED EMULSIFICATION OF CHICKEN BREAST MUSCLE MYOSIN

GALLUZZO, S. J.; REGENSTEIN, J. M.
Journal of Food Science , Volume 43 (6) – Nov 1, 1978
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References (16)

Publisher
Wiley
Copyright
Copyright © 1978 Wiley Subscription Services, Inc., A Wiley Company
ISSN
0022-1147
eISSN
1750-3841
DOI
10.1111/j.1365-2621.1978.tb07407.x
Publisher site
See Article on Publisher Site

Abstract

ABSTRACT 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.

Journal

Journal of Food Science – Wiley

Published: Nov 1, 1978

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