Small heat shock proteins and their role in meat tenderness: a review

Meat Sci. 2014 Jan;96(1):26-40. doi: 10.1016/j.meatsci.2013.06.008. Epub 2013 Jun 16.

Abstract

The eating quality of meat is a result of complex interactions between the biological traits and biochemical processes during the conversion of muscle to meat. It was hypothesised that muscles inevitably engage towards apoptotic cell death due to the termination of oxygen and nutrient supply to the muscle following exsanguination. Thus, factors that regulate the process of apoptotic cell death of muscle cells are believed to ultimately influence meat quality. Proteomic studies have associated the regulation of small heat shock proteins (sHSPs) with various meat quality attributes including tenderness, colour, juiciness and flavour. Due to the anti-apoptotic and chaperone functions of sHSPs, they are proposed to be involved with the eating quality of meat. In this review, we discuss the possible chaperone and anti-apoptotic role of sHSPs during the conversion of muscle to meat and consider the repercussions of this on the development of meat tenderness.

Keywords: Apoptosis; Chaperone; Intermediate pH; Meat quality; Small heat shock proteins; Tenderness.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Apoptosis
  • Cattle
  • Food Quality*
  • Gene Expression Regulation
  • Heat-Shock Proteins, Small / chemistry*
  • Heat-Shock Proteins, Small / genetics
  • Meat / analysis*
  • Muscle Proteins / chemistry
  • Muscle, Skeletal / chemistry
  • Postmortem Changes
  • Proteomics
  • Stress, Physiological
  • Swine
  • Taste / physiology

Substances

  • Heat-Shock Proteins, Small
  • Muscle Proteins