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作 者:李晶晶[1] 张瑞红[1] 韩冬雪[1] 俞龙浩[1]
机构地区:[1]黑龙江八一农垦大学食品学院,黑龙江大庆163319
出 处:《食品科学》2015年第15期240-244,共5页Food Science
基 金:国家自然科学基金面上项目(31171712)
摘 要:目前普遍认为参与宰后肌肉嫩化的相关蛋白酶主要有溶酶体组织蛋白酶、蛋白酶体、钙激活蛋白酶、钙激活酶抑制蛋白和半胱天冬酶5种,然而对于成熟过程中肉的嫩化程度及机理颇具有争议。大量的研究表明,上述5种嫩化酶在参与肉嫩化过程中其自身生理生化特性在宰后也发生变化。本文综述5种参与宰后肉嫩化酶的分子质量、存在部位、作用底物、作用位点、激活条件、最适pH值以及对其活性具有一定影响的抑制剂,并就其影响宰后肉嫩度的作用机理及其自身状态的变化进行分析与阐述,旨在为后续研究嫩化酶在宰后改善肉嫩度方面的应用条件提供参考。The mechanism of postmortem tenderization of muscle has been controversial for years. It is generally accepted that the improvement of meat tenderness mainly results from five endogenous proteolytic enzymes, including lysosomal cathepsin, proteasome, calpain, calpastatin and caspase. Calpains were widely considered to be a major contributor; however the latest studies reveal the role of caspases in muscle tenderness. The molecular weights, distribution, substrates, action sites, activation conditions, optimum pH and inhibitors of five enzymes involved in meat tenderization are briefly reviewed in this paper. The possible activation pathways and transformation ways of the enzymes are also discussed with the aim of providing a guideline for the application of these proteolytic enzymes to improve meat tenderness.
分 类 号:R337.1[医药卫生—人体生理学]
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