On the water-holding of myofibrils: Effect of sarcoplasmic protein denaturation

Meat Sci. 2016 Sep:119:32-40. doi: 10.1016/j.meatsci.2016.04.020. Epub 2016 Apr 19.

Abstract

The role of heat-denatured sarcoplasmic proteins in water-holding is not well understood. Here we propose a new hypothesis that in PSE-like conditions denatured sarcoplasmic proteins aggregate within and outside myofilaments, improving the water-holding of denatured myofibrils. The process is compartmentalized: 1) within the filaments the denatured sarcoplasmic proteins shrink the lattice space and water is expelled; and 2) between the myofibrils and in the extracellular space, the coagulated sarcoplasmic proteins trap the expelled water from interfilamental space. The effect of sarcoplasmic proteins on the water-holding of myofibrils following incubation for 1h at 21 to 44°C was investigated. Our results were consistent with the new hypothesis. Myofibrils without sarcoplasm had the poorest water-holding. With increasing amount of denatured sarcoplasmic proteins, the water-holding of heat-denatured myofibrils improved proportionally. X-ray diffraction was used to measure the lattice space between the filaments. Precipitated sarcoplasmic proteins shrank (P<0.001) the lattice spacing by 6.3% at 44°C.

Keywords: Heat denaturation; PSE; Protein aggregation; Water-holding capacity; X-ray diffraction.

MeSH terms

  • Animals
  • Hot Temperature
  • Hydrogen-Ion Concentration
  • Hydrophobic and Hydrophilic Interactions
  • Meat*
  • Muscle Proteins / chemistry*
  • Myofibrils / chemistry*
  • Protein Denaturation*
  • Sarcoplasmic Reticulum / chemistry*
  • Water / chemistry
  • X-Ray Diffraction

Substances

  • Muscle Proteins
  • Water