Relationship between Small Heat Shock Proteins and Meat Tenderness

doi:10.7506/spkx1002-6630-201613042

Abstract

Abstract:

The development of meat eating quality is closely related to complex biochemical processes during postmortem aging. Oxygen and nutrient withdrawal following exsanguination is known to induce apoptosis, so that muscle cells inevitably engage towards apoptotic cell death. Thus, factors that regulate the process of apoptotic cell death of muscle cells are believed to influence the ultimate meat quality. Small heat shock proteins (sHSPs), as biomarkers for meat quality attributes, have been confirmed by many proteomic studies. Due to the anti-apoptotic and molecular chaperone functions, sHSPs can protect myofibrillar proteins from degradation, interfere with cellular signal transduction pathways, delay myofibrillar protein degradation by endogenous enzymes and extend the process of meat aging. In this review, we discuss the mechanism of their possible chaperone and anti-apoptotic roles involved in meat tenderness during the conversion of muscle to meat

Key words: small heat shock proteins, tenderness, chaperone, apoptosis

CLC Number:

TS251.1

LI Xin, XING Tong, XU Xinglian. Relationship between Small Heat Shock Proteins and Meat Tenderness[J]. FOOD SCIENCE, doi: 10.7506/spkx1002-6630-201613042.

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