食品科学

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小分子热应激蛋白与肉嫩度的关系研究进展

李 鑫,邢 通,徐幸莲   

  1. 南京农业大学 肉品加工与质量控制教育部重点实验室,江苏 南京 210095
  • 出版日期:2016-07-15 发布日期:2016-07-26
  • 通讯作者: 徐幸莲
  • 基金资助:

    国家现代农业(肉鸡)产业技术体系建设专项(CARS-42)

Relationship between Small Heat Shock Proteins and Meat Tenderness

LI Xin, XING Tong, XU Xinglian   

  1. Key Laboratory of Meat Processing and Quality Control, Ministry of Education, Nanjing Agricultural University, Nanjing 210095, China
  • Online:2016-07-15 Published:2016-07-26
  • Contact: XU Xinglian

摘要:

肉嫩度的形成与动物宰后肌肉成熟过程中发生的复杂生理生化变化密切相关。动物宰杀放血后,氧气和营养物质供应终止,细胞凋亡程序启动,因此,调控该过程的凋亡因子可能最终影响到肌肉品质。小分子热应激蛋白(small heat shock proteins,sHSPs)作为肌肉嫩度的潜在生物标记,在许多蛋白组学的研究中得到证实。sHSPs由于其抗细胞凋亡和分子伴侣功能特性,在保护肌原纤维蛋白、干扰凋亡通路信号、延缓内源性蛋白酶对其的降解、延长肉的成熟时间等方面起到重要作用,与肉嫩度密切相关。本文综述了sHSPs作为肌肉向食用肉转变过程中的分子伴侣和其抗凋亡作用对肉嫩度的影响及其作用机理。

关键词: 小分子热应激蛋白, 嫩度, 分子伴侣, 细胞凋亡

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

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