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STUDIES ON THE EMULSIFYING CHARACTERISTICS OF SOME INTRACELLULAR TURKEY MUSCLE PROTEINS

STUDIES ON THE EMULSIFYING CHARACTERISTICS OF SOME INTRACELLULAR TURKEY MUSCLE PROTEINS SUMMARY Myosin, actin, actomyosin, myofibrils and sarcoplasmic proteins were isolated from the breast muscle of Broad‐breasted White breeder turkeys. The different proteins were evaluated for their emulsifying capacity (EC) and emulsion‐stabilizing capacity (ESC) at pH 7.0 and 6.0. Actin was evaluated both in the presence and in the absence of salt. A procedure for determination of ESC, which simulates commercial sausage conditions, was developed. The over‐all performance of the proteins was better at pH 7.0 than at 6.0 Myosin at both pH values had the highest EC but lacked ESC when compared to the other fractions. Actomyosin also possessed excellent emulsifying capacity second only to myosin at both pH 6.0 and 7.0. Although sarcoplasmic proteins had the lowest EC and ESC at pH 7.0, they performed better than actin, intact meat and myofibrils at pH 6.0. There was no difference between the performances of actin in the presence and in the absence of salt either in EC or ESC. Actin produced the most stable emulsions at pH 6.0, followed by sarcoplasmic proteins. Higher pH and the existence of “free” myosin and actin seem to be responsible for the better emulsifying characteristics of prerigor muscle. Sarcoplasmic proteins appear to contribute to emulsion stability in the post‐rigor state. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Journal of Food Science Wiley

STUDIES ON THE EMULSIFYING CHARACTERISTICS OF SOME INTRACELLULAR TURKEY MUSCLE PROTEINS

Journal of Food Science , Volume 36 (4) – May 1, 1971

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References (22)

Publisher
Wiley
Copyright
Copyright © 1971 Wiley Subscription Services, Inc., A Wiley Company
ISSN
0022-1147
eISSN
1750-3841
DOI
10.1111/j.1365-2621.1971.tb15142.x
Publisher site
See Article on Publisher Site

Abstract

SUMMARY Myosin, actin, actomyosin, myofibrils and sarcoplasmic proteins were isolated from the breast muscle of Broad‐breasted White breeder turkeys. The different proteins were evaluated for their emulsifying capacity (EC) and emulsion‐stabilizing capacity (ESC) at pH 7.0 and 6.0. Actin was evaluated both in the presence and in the absence of salt. A procedure for determination of ESC, which simulates commercial sausage conditions, was developed. The over‐all performance of the proteins was better at pH 7.0 than at 6.0 Myosin at both pH values had the highest EC but lacked ESC when compared to the other fractions. Actomyosin also possessed excellent emulsifying capacity second only to myosin at both pH 6.0 and 7.0. Although sarcoplasmic proteins had the lowest EC and ESC at pH 7.0, they performed better than actin, intact meat and myofibrils at pH 6.0. There was no difference between the performances of actin in the presence and in the absence of salt either in EC or ESC. Actin produced the most stable emulsions at pH 6.0, followed by sarcoplasmic proteins. Higher pH and the existence of “free” myosin and actin seem to be responsible for the better emulsifying characteristics of prerigor muscle. Sarcoplasmic proteins appear to contribute to emulsion stability in the post‐rigor state.

Journal

Journal of Food ScienceWiley

Published: May 1, 1971

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