The role of sarcoplasmic protein in hydrostatic pressure-induced myofibrillar protein denaturation

Meat Sci. 2011 Mar;87(3):219-22. doi: 10.1016/j.meatsci.2010.10.012. Epub 2010 Nov 12.

Abstract

To observe the role of sarcoplasmic protein (SP) on myofibrillar protein (MP) denaturation under a hydrostatic pressure (HP), MP isolated from bovine muscle was treated with 300 MPa by increasing concentrations of SP (0, 0.8, 1.6, and 3.2 mg/ml) from bovine. SDS-PAGE patterns of soluble proteins in 0.1M NaCl (pH 7.4) indicated that a protein (about 100 kDa) from MP decreased with increasing concentrations of SP and that a 97 kDa protein from SP observed with 0.1 MPa was not observed with 300 MPa. SDS-PAGE patterns of soluble proteins in 0.6 M NaCl (pH 7.4) and Ca-ATPase activity showed that the denaturation of myosin heavy chain (MHC) was accelerated with increasing SP concentrations with the 300 MPa treatment. Thus, the addition of SP enhanced HP-induced denaturation of MHC and of a protein from MP of about 100 kDa.

Publication types

  • Comparative Study

MeSH terms

  • Actinin / chemistry
  • Animals
  • Ca(2+) Mg(2+)-ATPase / metabolism
  • Calcium-Transporting ATPases / metabolism
  • Cattle
  • Electrophoresis, Polyacrylamide Gel
  • Food Handling*
  • Gels
  • Glycogen Phosphorylase, Muscle Form
  • Hydrostatic Pressure / adverse effects
  • Meat Products / analysis
  • Molecular Weight
  • Muscle Proteins / analysis
  • Muscle Proteins / chemistry*
  • Myofibrils / chemistry*
  • Myosin Heavy Chains / chemistry
  • Protein Denaturation*
  • Sarcoplasmic Reticulum / chemistry*
  • Solubility

Substances

  • Gels
  • Muscle Proteins
  • Actinin
  • Glycogen Phosphorylase, Muscle Form
  • Ca(2+) Mg(2+)-ATPase
  • Myosin Heavy Chains
  • Calcium-Transporting ATPases