Premium
Myofibrillar Protein Gelation: Viscoelastic Changes Related to Heating Procedures
Author(s) -
XIONG YOULING L.,
BLANCHARD SUZANNE P.
Publication year - 1994
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.1994.tb08115.x
Subject(s) - myofibril , rheology , viscoelasticity , isothermal process , dynamic mechanical analysis , chemistry , dynamic modulus , phase transition , protein aggregation , solubility , biophysics , crystallography , materials science , thermodynamics , biochemistry , composite material , polymer , organic chemistry , biology , physics
Dynamic Theological properties were investigated during gelation of chicken myofibrillar protein as influenced by heating procedures, Thermal scan (1°C/min) of myofibril suspensions in 0.6M NaCl (pH 6.0) induced a major transition in storage modulus (G′, peak 48°C), preceded by a transition in protein‐protein aggregation (46°C) and accompanied by a marked reduction in actomyosin solubility. Preheating at 50°C diminished the transition and resulted in increased final G′value. Isothermal heating produced complex, temperature‐dependent Theological changes (G′and phase angles), particularly within 43–58°C. The rheological transitions of myofibrillar protein were probably related to kinetic changes during formation of elastic gel networks. Such Theological data on gel formation can help predict and control muscle food responses to specific thermal processes.