Myosin sensitivity to thermal denaturation explains differences in water loss and shrinkage during cooking in muscles of distinct fibre types

Meat Sci. 2021 Sep:179:108521. doi: 10.1016/j.meatsci.2021.108521. Epub 2021 Apr 10.

Abstract

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.

Keywords: Cooking; Cooking loss; Meat; Protein conformation; Shear force; Shrinkage.

MeSH terms

  • Animals
  • Cattle
  • Cooking*
  • Hot Temperature
  • Muscle Fibers, Fast-Twitch
  • Muscle Fibers, Slow-Twitch
  • Muscle, Skeletal / chemistry*
  • Myosins / chemistry*
  • Red Meat / analysis*
  • Shear Strength
  • Water

Substances

  • Water
  • Myosins