pH stability and influence of salts on activity of a milk-clotting enzyme from Solanum dubium seeds and its enzymatic action on bovine caseins
pH stability and influence of salts on activity of a milk-clotting enzyme from Solanum dubium seeds and its enzymatic action on bovine caseins
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DOI：
10.1016/j.lwt.2009.12.011
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发表时间：
2010-06-01
影响因子：
6
通讯作者：
Mori, Nobuhiro
中科院分区：
文献类型：
--
作者：
Ahmed, Isam A. Mohamed;Babiker, Elfadil E.;Mori, Nobuhiro
在这项研究中，我们研究了pH的稳定性和盐的影响，部分纯化的酶的活性从梭伦瓮dubium种子，以及其水解能力的酪蛋白和酪蛋白组分的混合和提取的种子S dubium用50 g/L的NaCl在50 mmol/L的乙酸缓冲液，pH 5 0，然后用硫酸铵部分纯化酶。结果表明，NaCl和CaCl_2均能增强酶的蛋白水解活性，其中以NaCl的增强作用最为显著，而且这种增强作用具有浓度依赖性。结果表明，K-酪蛋白和β-酪蛋白比α-酪蛋白更易水解。酪蛋白的三种主要组分α-、β-和κ-酪蛋白对酶的作用敏感，水解顺序为κ-酪蛋白、β-酪蛋白和α-酪蛋白。(C)2010爱思唯尔有限公司版权所有
In this study we investigated the pH stability and effect of salts on the activity of a partially purified enzyme from Solon urn dubium seeds as well as its hydrolytic power on caseins and caseins components The seeds of S dubium were blended and extracted using 50 g/L NaCl in 50 mmol/L acetate buffer, pH 5 0 The enzyme was then partially purified using ammonium sulfate. The results obtained showed that both NaCl and CaCl2 enhanced the proteolytic activity of the enzyme and the enhancement was found to be significant when NaCl was used Moreover, the stimulatory effect was found to be concentration dependent. The proteolysis of bovine whole casein and casein subunits by the enzyme during incubation was studied by SDS-PAGE The results obtained revealed that both K-casein and beta-casein are the most susceptible to hydrolysis than alpha-casein The three main casein components alpha-, beta-, and kappa-casems were sensitive to the action of the enzyme and the order of hydrolysis obtained was kappa-casein, beta-casein, and alpha-caseins. (C) 2010 Elsevier Ltd. All rights reserved