期刊
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
卷 243, 期 -, 页码 -出版社
ELSEVIER
DOI: 10.1016/j.ijbiomac.2023.125131
关键词
& alpha;-Amylase; Allosteric regulation; Fluorescence quenching; Conformational change
The study systematically investigated the conformational changes in α-amylase induced by different ligands including metal ions, substrates, and aromatic compounds in liquor production. The results showed that interactions with active metal cations increased the exposure of active sites in α-amylase, while interactions with substrates reduced the degree of exposure and made the enzyme more rigid and compact. Inhibitory metal cations and aromatic compounds increased the exposure of active sites but reduced the enzymatic activity. These findings provide valuable insights for controlling conditions and improving production efficiency.
The conformational changes in a-amylase induced by different ligands, including metal ions, substrates, and aromatic compounds in liquor production, were systematically studied using spectroscopy. Fluorescence acrylamide quenching analysis showed that the interaction with active metal cations (K+, Na+, and Ca2+) led to higher exposure of the active sites in a-amylase. In contrast, interactions with substrates (soluble starch, amylose, amylopectin, wheat starch, and dextrin) reduced the degree of exposure of active sites, and the conformation of the enzyme became more rigid and compact. Although the interaction with inhibitory metal cations (Mg2+, Zn2+) and aromatic compounds generated in the brewing process (guaiacol, eugenol, thymol, and vanillin) increased the exposure of active site with a relatively low amplitude, it reduced the enzymatic activity. This finding may be due to the overall structure of the enzyme becoming looser. Structural stability showed that the active cations and substrates increased the stability of the secondary structure of the a-amylase backbone, whereas the inhibitory cations and aromatic compounds reduced the stability of the backbone but increased the compact of domain A and B. Enzymatic assays and molecular docking experiments strongly supported these conclusions. The experimental results may provide a valuable reference for controlling related conditions and improving production efficiency.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据