A COMPARISON OF THE RHEOLOGICAL CHARACTERISTICS OF DIFFERENT FRACTIONS OF CHICKEN MYOFIBRILLAR PROTEINS
Author:
- 1 August 1992
- journal article
- Published by Hindawi Limited in Journal of Food Biochemistry
- Vol. 16 (4) , 217-227
Abstract
Suspensions of myofibrils and salt-soluble (SSP) or insoluble (SIP) proteins of chicken breast muscle in 0.6 M NaCl at pH 6.0 were heated to induce gels. Dynamic oscillating measurements showed multiple transitions in the shear storage modulus and loss modulus for all three protein fractions in the temperature range of 40–65C. However, changes in these viscoelasticities were most pronounced for SSP and least appreciable for SIP. Gel penetration test also revealed a descending order of SSP < myofibrils < SIP in gel strength. The three fractions of myofibrillar proteins appeared to follow a similar gelation mechanism but vary in the density of the gel networks.Keywords
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