A COMPARISON OF THE RHEOLOGICAL CHARACTERISTICS OF DIFFERENT FRACTIONS OF CHICKEN MYOFIBRILLAR PROTEINS

YOULING L. XIONG

doi:10.1111/j.1745-4514.1992.tb00447.x

A COMPARISON OF THE RHEOLOGICAL CHARACTERISTICS OF DIFFERENT FRACTIONS OF CHICKEN MYOFIBRILLAR PROTEINS

YOULING L. XIONG

Animal and Food Sciences

Research output: Contribution to journal › Article › peer-review

98 Scopus citations

Abstract

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.

Original language	English
Pages (from-to)	217-227
Number of pages	11
Journal	Journal of Food Biochemistry
Volume	16
Issue number	4
DOIs	https://doi.org/10.1111/j.1745-4514.1992.tb00447.x
State	Published - Aug 1992

ASJC Scopus subject areas

Food Science
Biophysics
Pharmacology
Cell Biology

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N2 - 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.

AB - 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.

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A COMPARISON OF THE RHEOLOGICAL CHARACTERISTICS OF DIFFERENT FRACTIONS OF CHICKEN MYOFIBRILLAR PROTEINS

Abstract

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