Department of Bioproducts and Biosystems , Aalto University , Espoo, FI-00076 Aalto , Finland.
Department of Experimental Physics , Saarland University , Saarbrücken 66123 , Germany.
Biomacromolecules. 2019 Feb 11;20(2):769-777. doi: 10.1021/acs.biomac.8b01346. Epub 2019 Jan 31.
In this study, the interaction forces between different cellulosic nanomaterials and a protein domain belonging to cellulose binding modules family 1 (CBM1) were investigated at the molecular scale. Cellulose binding modules are protein domains found in carbohydrate active enzymes having an affinity toward cellulosic materials. Here, the binding force of a fusion protein containing a cellulose binding module (CBM1) produced recombinantly in E. coli was quantified on different cellulose nanocrystals immobilized on surfaces. Adhesion of the CBM on cellulose with different degrees of crystallinity as well as on chitin nanocrystals was examined. This study was carried out by single molecule force spectroscopy using an atomic force microscope, which enables the detection of binding force of individual molecules. The study contains a preliminary quantification of the interactions at the molecular level that sheds light on the development of new nanocellulose-based nanocomposites with improved strength and elasticity.
在这项研究中，我们在分子尺度上研究了不同纤维素纳米材料与属于纤维素结合模块家族 1（CBM1）的蛋白质结构域之间的相互作用力。纤维素结合模块是在具有纤维素亲和力的碳水化合物活性酶中发现的蛋白质结构域。在这里，我们对在表面固定的不同纤维素纳米晶体上重组产生的含有纤维素结合模块（CBM1）的融合蛋白的结合力进行了定量。我们研究了 CBM 在不同结晶度的纤维素以及壳聚糖纳米晶体上的粘附。这项研究是通过原子力显微镜的单分子力谱进行的，该技术可以检测单个分子的结合力。该研究初步量化了分子水平上的相互作用，为开发具有更高强度和弹性的新型纳米纤维素基纳米复合材料提供了思路。
