Ganapathy R, Sarmadi M, Denes F
Engineering Research Center for Plasma-Aided Manufacturing and School of Human Ecology, University of Wisconsin-Madison 53706, USA.
J Biomater Sci Polym Ed. 1998;9(4):389-404. doi: 10.1080/09205063.1998.9753063.
In this contribution the immobilization of alpha-chymotrypsin on plasma activated PET and PP surfaces is investigated. The 'anchoring' C=O groups on polymer surfaces were created under RF-O2-plasma environments. The identity and relative concentrations of plasma-created functionalities were evaluated using survey and high resolution X-ray photoelectron spectroscopy, and differential attenuated total reflectance-FTIR spectroscopy. Surface morphology changes of plasma-exposed substrates were analyzed by atomic force microscopy. Enzyme assays were performed from both virgin and plasma modified samples which underwent the immobilization procedure. It was demonstrated that cold-plasma technique is suitable for generating functional, synthetic polymeric surfaces which can initiate enzyme coupling reactions. It also has been shown that the activity of the immobilized enzyme is lower in comparison to the free enzyme. Reduced conformational mobility resulting from multiple-point coupling process might be responsible for this behavior.
在本论文中，研究了α-糜蛋白酶在等离子体活化的聚对苯二甲酸乙二酯（PET）和聚丙烯（PP）表面的固定化。聚合物表面的“锚定”羰基（C=O）基团是在射频氧等离子体环境下产生的。利用扫描和高分辨率X射线光电子能谱以及差示衰减全反射傅里叶变换红外光谱（ATR-FTIR）对等离子体产生的官能团的特性和相对浓度进行了评估。通过原子力显微镜分析了等离子体处理后基材的表面形态变化。对经过固定化处理的原始样品和等离子体改性样品都进行了酶活性测定。结果表明，冷等离子体技术适用于生成能够引发酶偶联反应的功能性合成聚合物表面。研究还表明，与游离酶相比，固定化酶的活性较低。多点偶联过程导致的构象流动性降低可能是造成这种现象的原因。
