Biosurfactant-Protein Interaction: Influences of Mannosylerythritol Lipids-A on beta-Glucosidase

文献类型： 外文期刊

第一作者： Wang, Ying

作者： Wang, Ying;Huang, Zisu;Zhou, Jianzhong;Xie, Pujun

作者机构：

关键词： protein biosurfactant;beta-glucosidase;mannosylerythritol lipids;isothermal titration calorimetry;docking simulation

期刊名称：JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY （ 影响因子：5.279； 五年影响因子：5.269 ）

ISSN： 0021-8561

年卷期： 2018 年 66 卷 1 期

页码：

收录情况： SCI

摘要： In this work, the influences of a biosurfactant, mannosylerythritol lipids-A (MEL-A) toward beta-glucosidase activity and their molecular interactions were studied by using differential scanning calorimetry (DSC), circular dichroism spectroscopy (CD), isothermal titration calorimetry (ITC), and docking simulation. The enzyme inhibition kinetics data showed that MEL-A at a low concentration (< critical micelle concentration (CMC), 20.0 +/- 5.0 mu M) enhanced beta-glucosidase activity, whereas it inhibited the enzyme activity at higher concentrations more than 20.0 mu M, followed by a decreased V-max and K-m of beta-glucosidase. The thermodynamics and structural data demonstrated that the midpoint temperature (T-m) and unfolding enthalpy (Delta H) of beta-glucosidase was shifted to high values (76.6 degrees C, 126.3 J/g) in the presence of MEL-A, and the secondary structure changes of beta-glucosidase, including the increased alpha-helix, beta-turn, or random coil contents, and a decreased beta-sheet content were caused by MEL-A at a CMC concentration. The further ITC and docking simulations suggested the bindings of MEL-A toward beta-glucosidase were driven by weak hydrophobic interactions happened between the amino acid residues of beta-glucosidase and the fatty acid residues of MEL-A, in addition to hydrogen bonds between amino acids and hydroxyl in glycosyl residues of this biosurfactant.

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