Baroroh Umi, Chantika Nindi Salma, Firdaus Ade R R, Tohari Taufik Ramdani, Subroto Toto, Ishmayana Safri, Safari Agus, Rachman Saadah Diana, Yusuf Muhammad
Department of Biotechnology, Indonesia School of Pharmacy, Bandung, Indonesia.
Department of Chemistry, Faculty of Mathematics and Natural Sciences, Universitas Padjadjaran, Sumedang, Indonesia.
J Biomol Struct Dyn. 2025 Feb;43(2):571-581. doi: 10.1080/07391102.2023.2283152. Epub 2023 Nov 18.
The thermostability of enzymes plays a significant role in the starch hydrolysis process in the industry. The structural difference between thermostable α-amylase (BLA) and thermolabile α-amylase (ANA) is interesting to be explored. This work aimed to study the thermostability-determining factor of BLA as compared to a non-thermostable enzyme, ANA, using molecular dynamics (MD) simulation at a high temperature. A 100 ns of classical MD, which was followed by 200 ns accelerated MD was conducted to explore the conformational changes of the enzyme. It is revealed that the intramolecular interactions through salt bridge interactions and the presence of calcium ions dominates the stability effect of BLA, despite the absence of a disulfide bond in the structure. These results should be useful in designing a thermostable enzyme that can be used in industrial processes.Communicated by Ramaswamy H. Sarma.
酶的热稳定性在工业淀粉水解过程中起着重要作用。热稳定α-淀粉酶（BLA）和热不稳定α-淀粉酶（ANA）之间的结构差异值得探索。这项工作旨在通过高温下的分子动力学（MD）模拟，研究与非热稳定酶ANA相比，BLA的热稳定性决定因素。进行了100纳秒的经典分子动力学模拟，随后进行200纳秒的加速分子动力学模拟，以探索酶的构象变化。结果表明，尽管该结构中不存在二硫键，但通过盐桥相互作用的分子内相互作用和钙离子的存在主导了BLA的稳定性效应。这些结果对于设计可用于工业过程的热稳定酶应该是有用的。由拉马斯瓦米·H·萨尔马传达。
