Inverse relationships between biomarkers and beef tenderness according to contractile and metabolic properties of the muscle

J Agric Food Chem. 2014 Oct 8;62(40):9808-18. doi: 10.1021/jf501528s. Epub 2014 Sep 23.

Abstract

Previous proteomic analyses established a list of proteins biomarkers of beef tenderness. The present study quantified the relative abundance of 21 of these proteins by dot-blot technique in the Longissimus thoracis and Semitendinosus muscles of 71 young bulls from three breeds: Aberdeen Angus (AA), Limousin (LI), and Blond d'Aquitaine (BA). For both muscles overall tenderness was estimated by sensory analysis; shear force was measured with a Warner-Bratzler instrument, and an index combining sensory and mechanical measurements was calculated. Multiple regressions based on relative abundances of these proteins were used to propose equations of prediction of the three evaluations of tenderness. Hsp70-1B appeared to be a good biomarker of low tenderness in the three breeds and in the two muscles. Proteins such as lactate dehydrogenase-B, myosin heavy chain IIx, and small heat shock proteins (Hsp27, Hsp20, and αB-crystallin) were related to tenderness but inversely according to the muscle and breed. The results demonstrate that prediction of tenderness must take into account muscle characteristics and animal type.

Keywords: beef tenderness; biomarkers; dot-blot; heat shock proteins; prediction; skeletal muscle.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Biomarkers / metabolism*
  • Cattle
  • Food Quality*
  • HSP27 Heat-Shock Proteins / metabolism
  • HSP72 Heat-Shock Proteins / metabolism
  • Heat-Shock Proteins / metabolism*
  • Male
  • Meat*
  • Muscle Contraction
  • Muscle, Skeletal / metabolism
  • Muscle, Skeletal / physiology*
  • Regression Analysis
  • alpha-Crystallin B Chain / metabolism

Substances

  • Biomarkers
  • HSP27 Heat-Shock Proteins
  • HSP72 Heat-Shock Proteins
  • Heat-Shock Proteins
  • alpha-Crystallin B Chain