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THE EMULSIFYING PROPERTIES OF PURIFIED MUSCLE PROTEINS

THE EMULSIFYING PROPERTIES OF PURIFIED MUSCLE PROTEINS University THE EMULSIFYING PROPERTIES O F PURIFIED MUSCLE PROTEINS INTRODUCTION PROCEDURES have been developed for the study of emulsifying capacity of muscle proteins in model systems (Swift et al., 1961; Carpenter and Saffle, 1964). Many workers have demonstrated with light microscopy that the structure of meat emulsions is similar to classical emulsions to the extent of fat globules being surrounded by a limiting membrane (Hansen, 1960; Swift et al., 196 1; Helmer and Saffle, 1963; Carpenter and Saffle, 1964; Meyer et al., 1964). Borchert et al. (1967) used electron microscopy to study emulsions and showed that the fat was distributed as globules of different sizes ranging from O.l-50~ and was encapsulated by a matrix of protein. The functionality of individual muscle proteins (myosin, actin, sarcoplasmic, tropomyosin, etc.) in meat emulsions is still not entirely clear. Hansen (1960) described the protein matrix that surrounds the fat globules and stated that the salt soluble proteins, myosin and actomyosin appear to concentrate at the fat globule surfaces and form a stabilizing membrane. Baliga and Madaiah (1970) also emphasize the importance of myosin in stabilizing meat emulsions. Ivey et al. (1970) found that the stability of emulsions made from dilute protein extracts http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Journal of Food Science Wiley

THE EMULSIFYING PROPERTIES OF PURIFIED MUSCLE PROTEINS

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References (14)

Publisher
Wiley
Copyright
Copyright © 1972 Wiley Subscription Services, Inc., A Wiley Company
ISSN
0022-1147
eISSN
1750-3841
DOI
10.1111/j.1365-2621.1972.tb05837.x
Publisher site
See Article on Publisher Site

Abstract

University THE EMULSIFYING PROPERTIES O F PURIFIED MUSCLE PROTEINS INTRODUCTION PROCEDURES have been developed for the study of emulsifying capacity of muscle proteins in model systems (Swift et al., 1961; Carpenter and Saffle, 1964). Many workers have demonstrated with light microscopy that the structure of meat emulsions is similar to classical emulsions to the extent of fat globules being surrounded by a limiting membrane (Hansen, 1960; Swift et al., 196 1; Helmer and Saffle, 1963; Carpenter and Saffle, 1964; Meyer et al., 1964). Borchert et al. (1967) used electron microscopy to study emulsions and showed that the fat was distributed as globules of different sizes ranging from O.l-50~ and was encapsulated by a matrix of protein. The functionality of individual muscle proteins (myosin, actin, sarcoplasmic, tropomyosin, etc.) in meat emulsions is still not entirely clear. Hansen (1960) described the protein matrix that surrounds the fat globules and stated that the salt soluble proteins, myosin and actomyosin appear to concentrate at the fat globule surfaces and form a stabilizing membrane. Baliga and Madaiah (1970) also emphasize the importance of myosin in stabilizing meat emulsions. Ivey et al. (1970) found that the stability of emulsions made from dilute protein extracts

Journal

Journal of Food ScienceWiley

Published: Mar 1, 1972

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