Abstract

The influence of heat-shock protein (HSP) concentrations at 45 min and 24 h postmortem on meat quality and sensory quality characteristics of longissimus thoracis muscle from highly marbled Hanwoo steers (beef marbling standard grade 6–8) was investigated. Muscle samples were segregated into three groups based on Warner–Bratzler shear force (WBSF) value. The low group exhibited a lower WBSF value compared to the medium and high groups (37.8 vs. 48.9 and 64.3 N, p < 0.001). Muscle pH at 45 min and 24 h postmortem was not different (p > 0.05), and all groups exhibited low ultimate pH value (pH < 5.8). Beef steaks from the low group were significantly easier to pierce and chew, and they left less perceptible residue than the high group (p < 0.05). These differences in tenderness attributes were associated with differences in small HSPs at 45 min postmortem, with the low group exhibiting a lower level of αβ-crystallin and higher levels of HSP20 and HSP27 compared with the high group (p < 0.05). No differences were observed for small HSPs, HSP70, and HSP90 at 24 h postmortem (p > 0.05). Therefore, the expression levels of small HSPs at 45 min postmortem seems to have the potential to be an indicator of tenderness in highly marbled Hanwoo beef with low ultimate pH.

Highlights

  • Heat-shock proteins (HSPs) are well known as molecular chaperones that assist in the normal folding of various polypeptides, help misfolded polypeptides regain their proper configuration, and regulate proteolysis [1,2]

  • The expression levels of small HSPs at 45 min postmortem seems to have the potential to be an indicator of tenderness in highly marbled Hanwoo beef with low ultimate pH

  • The objective of this study was to investigate the relationship between HSP expressions, including αβ-crystallin, HSP20, HSP27, HSP70, and HSP90, and meat quality and sensory quality characteristics of highly marbled Hanwoo steers to identify factors that are associated with tenderness variation in highly marbled beef

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Summary

Introduction

Heat-shock proteins (HSPs) are well known as molecular chaperones that assist in the normal folding of various polypeptides, help misfolded polypeptides regain their proper configuration, and regulate proteolysis [1,2]. These chaperone properties of HSPs are expressed under a variety of conditions including normal, stressed, and apoptotic, but HSPs do not remain as part of the final protein structure [2]. To maintain cell homeostasis against apoptosis, pro- and anti-apoptotic proteins are released from mitochondria [4]. The levels of HSPs at the early postmortem period are associated with the rate and extent of apoptosis, and they can influence structural and metabolic changes of skeletal muscle during the postmortem period [4,5]

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