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

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.

• Authors: D Lomiwes, M M Farouk, E Wiklund, O A Young
• Journal: Meat science (Meat Sci) Vol. 96 Issue 1 Pg. 26-40 (Jan 2014) ISSN: 1873-4138 [Electronic] England
• PMID: 23896134 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't, Review)
• Copyright: Copyright © 2013 Elsevier Ltd. All rights reserved.

Chemical References

• Heat-Shock Proteins, Small
• Muscle Proteins

Topics

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