TY - JOUR
T1 - Myosin sensitivity to thermal denaturation explains differences in water loss and shrinkage during cooking in muscles of distinct fibre types
AU - Vaskoska, Rozita
AU - Ha, Minh
AU - Ong, Lydia
AU - Chen, George
AU - White, Jason
AU - Gras, Sally
AU - Warner, Robyn
N1 - Funding Information:
R. Vaskoska would like to thank Dr. Annie Venien and Dr. Thierry Astruc from INRAE France for ATPase staining training. The assistance of Michelle LeMaster with staining is acknowledged. The authors are grateful for the provision of meat samples by Westside Meats, Victoria, Australia. A consultation with Associate Prof. Graham Hepworth in deciding the fixed and random factors structure of the statistical analysis is also acknowledged. R. Vaskoska would like to acknowledge the receiving of Research Training Scholarship from the Australian Government. The myosin figure in graphical abstract is prepared with Biorender.com.
Funding Information:
R. Vaskoska would like to thank Dr. Annie Venien and Dr. Thierry Astruc from INRAE France for ATPase staining training. The assistance of Michelle LeMaster with staining is acknowledged. The authors are grateful for the provision of meat samples by Westside Meats, Victoria, Australia. A consultation with Associate Prof. Graham Hepworth in deciding the fixed and random factors structure of the statistical analysis is also acknowledged. R. Vaskoska would like to acknowledge the receiving of Research Training Scholarship from the Australian Government. The myosin figure in graphical abstract is prepared with Biorender.com .
Publisher Copyright:
© 2021 Elsevier Ltd
PY - 2021/9
Y1 - 2021/9
N2 - The effect of thermal protein denaturation on the structure and quality of muscles of different fibre types is not well understood. Unaged masseter (100% type I fibres) and cutaneous trunci (93% type II fibres) muscles (N = 10) were assessed for their characteristics, protein denaturation, cooking loss, Warner- Bratzler shear force (WBSF) and shrinkage after heating at 50 °C - 85 °C with a rate of 5 °C/ min. Raw masseter had a higher pH, collagen and water content, shorter sarcomere, comparable fibre diameter, and shorter and wider fragments upon homogenization, than cutaneous trunci. In cutaneous trunci, at 55 °C - 60 °C, the lower transition temperature of myosin and the greater cumulative enthalpy resulted in greater cooking loss in muscle cuboids, and greater transverse, longitudinal and volume shrinkage in fibres and fibre fragments, than in masseter. Protein denaturation explained 71% variability in fibre fragment volume and 58% in cooking loss of both muscles, as well as 47% variability in WBSF of masseter.
AB - The effect of thermal protein denaturation on the structure and quality of muscles of different fibre types is not well understood. Unaged masseter (100% type I fibres) and cutaneous trunci (93% type II fibres) muscles (N = 10) were assessed for their characteristics, protein denaturation, cooking loss, Warner- Bratzler shear force (WBSF) and shrinkage after heating at 50 °C - 85 °C with a rate of 5 °C/ min. Raw masseter had a higher pH, collagen and water content, shorter sarcomere, comparable fibre diameter, and shorter and wider fragments upon homogenization, than cutaneous trunci. In cutaneous trunci, at 55 °C - 60 °C, the lower transition temperature of myosin and the greater cumulative enthalpy resulted in greater cooking loss in muscle cuboids, and greater transverse, longitudinal and volume shrinkage in fibres and fibre fragments, than in masseter. Protein denaturation explained 71% variability in fibre fragment volume and 58% in cooking loss of both muscles, as well as 47% variability in WBSF of masseter.
KW - Cooking
KW - Cooking loss
KW - Meat
KW - Protein conformation
KW - Shear force
KW - Shrinkage
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U2 - 10.1016/j.meatsci.2021.108521
DO - 10.1016/j.meatsci.2021.108521
M3 - Article
C2 - 33964804
AN - SCOPUS:85105319470
VL - 179
SP - 1
EP - 15
JO - Meat Science
JF - Meat Science
SN - 0309-1740
M1 - 108521
ER -