Investigating lignin from Canna edulis ker residues induced activation of alpha-amylase: Kinetics, interaction, and molecular docking
Investigating lignin from Canna edulis ker residues induced activation of alpha-amylase: Kinetics, interaction, and molecular docking
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研究美人蕉残基中的木质素诱导的 α-淀粉酶激活：动力学、相互作用和分子对接
DOI：
10.1016/j.foodchem.2018.07.153
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发表时间：
2019
期刊：
影响因子：
8.8
通讯作者：
Wang Zhengwu
中科院分区：
文献类型：
--
作者：
Xie Fan;Zhang Wei;Gong Shengxiang;Gu Xinzhe;Lan Xiaohong;Wu Jinhong;Wang Zhengwu
木质素是从C。刺激剂残留物对α-淀粉酶有明显的激活作用。进一步的研究表明，分离的木质素通过氢键与α-淀粉酶形成1：1的络合物，并通过静态猝灭过程猝灭α-淀粉酶的荧光。与木质素结合导致α-淀粉酶的构象和颗粒大小发生变化。2D-NOE-SY谱表明G单元中的单键OH和β-O-4结构是木素在α-淀粉酶分子上的主要结合部位。分子对接研究表明，α-淀粉酶与木质素的结合残基不同于与氯离子的结合残基，主要结合力为氢键。此外，对接结果还显示了α-淀粉酶对木质素结构的影响。因此，本工作为研究美人蕉渣木质素与α-淀粉酶的相互作用提供了新的视角，为木质素在食品工业中的应用提供了新的思路。
The lignin isolated fromC. edulisker residues showed a significant activating effect on α-amylase. Further studies revealed that the isolated lignin formed a 1:1 complex with α-amylase through hydrogen bonding and quenched fluorescence of α-amylase with a static quenching procedure. Binding with lignin led to conformational and granular size changes of α-amylase. Two-dimensional nuclear Overhauser spectroscopy (2D-NOESY) spectra suggested that single bondOH in G units and β-O-4 structure were the major binding sites of lignin on the α-amylase molecule. Molecular docking studies indicated that the binding residue on α-amylase for lignin was not the same as for chloride ions, and the major binding force was hydrogen bonding. Furthermore, the docking results also showed the structural change of lignin induced by α-amylase. Thus, this work provided a new insight into the interaction between lignin fromCanna edulisker residues and α-amylase, which may be beneficial to apply lignin in the food industry.