The preparation and enzyme immobilization of hydrophobic polysiloxane supports

Enzymes are versatile biocatalysts and find increasing applications in many areas. The major advantages of using enzymes in biocatalytic transformations are their chemo-, regio-, and stereospecificity, as well as the mild reaction conditions that can be used. However, even when an enzyme is identified as being useful for a given reaction, its application is often hampered by its lack of long-term stability under process conditions, and also by difficulties in recovery and recycling. For ease of application and stabilization purposes, enzymes are often immobilized on solid supports. Among support matrices, hydrophobic biomaterials have been extensively used as supports for enzyme immobilization because the hydrophobic interactions not only can effectively increase the amount of enzyme immobilization, but also exhibit higher activity and retention of activity compared with hydrophilic supports. On the other hand, polysiloxane can evidently increase the amount of enzyme immobilization because of its hydrophobicity and strong affinity with enzyme. Therefore, this research details the first preparation and use of a hydrophobic polysiloxane support for enzyme immobilization in which the structural and functional characteristics of new supports have been investigated by using glucose oxidase (GOD) and a simple Fenton's assay method, and extremely interesting features were revealed. The results showed that the amount of GOD immobilization and the stability of GOD loaded, which are fundamental properties for enzyme separation and purification, can be significantly improved by adsorption. Moreover, the results indicated that hydrophobic polysiloxane supports can effectively increase the enzymatic affinity and durability of GOD, and decrease the rate of GOD desorbed.