Binding of Tris to Bacillus licheniformis α-amylase can affect its starch hydrolysis activity
Binding of Tris to Bacillus licheniformis α-amylase can affect its starch hydrolysis activity
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DOI：
10.2174/092986608783489616
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发表时间：
2008-02-01
影响因子：
1.6
通讯作者：
Ranjbar, Bijan
中科院分区：
文献类型：
--
作者：
Ghalanbor, Zahra;Ghaemi, Nasser;Ranjbar, Bijan
地衣芽孢杆菌α -淀粉酶（BLA）是生物化学研究中常用的耐热淀粉酶模型。近年来在Tris缓冲液中研究了其淀粉水解活性。在这里，我们解决了Tris缓冲液的应用是否会影响BLA活性分析结果的问题。基于抑制研究和对接模拟，我们认为Tris分子是BLA淀粉水解活性的竞争性抑制剂，具有较高的结合酶活性位点的倾向。因此，在解释Tris缓冲液中该酶的活性研究结果时，考虑这种效应是至关重要的。
Bacillus licheniformis alpha-amylase (BLA) is routinely used as a model thermostable amylase in biochemical studies. Its starch hydrolysis activity has recently been studied in Tris buffer. Here, we address the question that whether the application of Tris buffer may influence the results of BLA activity analyses. Based on the inhibition studies and docking simulations, we suggest that Tris molecule is a competitive inhibitor of starch-hydrolyzing activity of BLA, and it has a high tendency to bind the enzyme active site. Hence, it is critically important to consider such effect when interpreting the results of activity studies of this enzyme in Tris buffer.