兔腰大肌肌球蛋白三磷酸酶的纯化与特性研究：研究报告。

Purification and characterization of myosin-tripolyphosphatase from rabbit Psoas major muscle: research note.

机构信息

Department of Food Science and Technology, Nanjing Agricultural University, Nanjing, 210095, PR China.

出版信息

Meat Sci. 2011 Dec;89(4):372-6. doi: 10.1016/j.meatsci.2010.10.014. Epub 2010 Oct 23.

DOI:10.1016/j.meatsci.2010.10.014

Abstract

In this study, we investigated the tripolyphosphatase (TPPase) activity responsible for the hydrolysis of tripolyphosphates (TPP) in rabbit Psoas major muscle tissue. After a series of extraction and purification steps, myosin was identified to be a TPPase. Optimum pH and temperature for myosin-TPPase activity were 6.0 and 35°C, respectively. We also found that myosin-TPPase activity was significantly influenced by Mg(2+) and Ca(2+) levels, whose optimal concentrations were determined to be 3 and 6mM, respectively. Furthermore, myosin-TPPase was strongly inhibited by EDTA-4Na(+) and KIO(3), and was slightly activated by EDTA-2Na(+). These results suggest that it may be useful to regulate tripolyphosphate hydrolysis to enhance its function in meat processing.

摘要

在这项研究中，我们研究了三磷酸酶（TPPase）活性，该活性负责水解兔腰肌组织中的三聚磷酸（TPP）。经过一系列的提取和纯化步骤，肌球蛋白被鉴定为 TPPase。肌球蛋白-TPPase 活性的最佳 pH 值和温度分别为 6.0 和 35°C。我们还发现，肌球蛋白-TPPase 活性受 Mg(2+)和 Ca(2+)水平的显著影响，其最佳浓度分别确定为 3mM 和 6mM。此外，肌球蛋白-TPPase 被 EDTA-4Na(+)和 KIO(3)强烈抑制，而被 EDTA-2Na(+)轻微激活。这些结果表明，调节三聚磷酸水解以增强其在肉品加工中的功能可能是有用的。