Enzymatic degradation of plant polysaccharide networks is a complex process that involves disrupting an intimate assembly of cellulose and hemicelluloses in fibrous matrices. To mimic this assembly and to elucidate the efficiency of enzymatic degradation in a rapid way, models with physicochemical equivalence to natural systems are needed. Here, we employ xylan-coated cellulose thin films to monitor the hydrolyzing activity of an endo-1,4-β-xylanase. In situ surface plasmon resonance spectroscopy (SPRS) revealed a decrease in xylan areal mass ranging from 0.01 ± 0.02 to 0.52 ± 0.04 mg·m⁻². The extent of digestion correlates to increasing xylanase concentration. In addition, ex situ determination of released monosaccharides revealed that incubation time was also a significant factor in degradation (P > 0.01). For both experiments, atomic force microscopy confirmed the removal of xylans from the cellulose thin films. We provide a new model platform that offers nanoscale sensitivity for investigating biopolymer interactions and their susceptibility to enzymatic hydrolysis.

植物多糖网络的酶促降解是一个复杂的过程，涉及破坏纤维基质中纤维素和半纤维素的紧密组装。为了模拟这种组装并快速阐明酶降解的效率，需要与自然系统具有物理化学等效性的模型。在这里，我们使用木聚糖涂层的纤维素薄膜来监测 endo-1,4-β-xylanase 的水解活性。原位表面等离子共振光谱 (SPRS) 显示木聚糖面积质量减少，范围从 0.01 ± 0.02 到 0.52 ± 0.04 mg·m ^-2. 消化的程度与增加的木聚糖酶浓度相关。此外，释放的单糖的异位测定表明，孵育时间也是降解的重要因素（P > 0.01）。对于这两个实验，原子力显微镜证实了木聚糖从纤维素薄膜中的去除。我们提供了一个新的模型平台，该平台为研究生物聚合物相互作用及其对酶水解的敏感性提供了纳米级的灵敏度。