Immobilization of alpha-chymotrypsin on oxygen-RF-plasma functionalized PET and PP surfaces.
Immobilization of alpha-chymotrypsin on oxygen-RF-plasma functionalized PET and PP surfaces.
复制标题
将 α-胰凝乳蛋白酶固定在氧-射频-等离子体功能化 PET 和 PP 表面上。
DOI：
10.1080/09205063.1998.9753063
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发表时间：
1998
期刊：
影响因子：
--
通讯作者：
F. Denes
中科院分区：
文献类型：
--
作者：
R. Ganapathy;M. Sarmadi;F. Denes
在这方面的贡献，α-糜蛋白酶等离子体活化PET和PP表面的固定化进行了研究。在RF-O2-等离子体环境下，在聚合物表面上的“锚定”C=O基团被创建。等离子体产生的功能的身份和相对浓度进行了评价，使用调查和高分辨率X射线光电子能谱，和差分衰减全反射-FTIR光谱。用原子力显微镜分析了等离子体处理后基片表面形貌的变化。从经历固定化程序的原始样品和血浆改性样品进行酶测定。结果表明，冷等离子体技术是适合于产生功能，合成聚合物表面，可以引发酶偶联反应。还表明，固定化酶的活性比游离酶低。多点偶联过程导致的构象迁移率降低可能是导致这种行为的原因。
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.