Premium
A COMPARISON OF THE RHEOLOGICAL CHARACTERISTICS OF DIFFERENT FRACTIONS OF CHICKEN MYOFIBRILLAR PROTEINS 1
Author(s) -
XIONG YOULING L.
Publication year - 1992
Publication title -
journal of food biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.507
H-Index - 47
eISSN - 1745-4514
pISSN - 0145-8884
DOI - 10.1111/j.1745-4514.1992.tb00447.x
Subject(s) - myofibril , rheology , chemistry , dynamic mechanical analysis , penetration (warfare) , dynamic modulus , salt (chemistry) , chromatography , biochemistry , materials science , composite material , organic chemistry , operations research , engineering , polymer
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.