ABSTRACT
Enzymes endowed by nature are ubiquitous and versatile as catalysts that span some nanometers in size. Their paramount activity and specicity under mild and physiologically friendly conditions are most benecial, which allow them to be applicable to various elds, including synthesis of chemicals and pharmaceuticals, integration to biosensors, biofuel cells, and many others. However, enzymes are inherently proteins that are sensitive, unstable, and incompatible in most cases with organic media. In order to make them more useful in industrial processes, a tremendous number of efforts has been dedicated to circumventing the drawbacks in stability and compatibility with various organic media. One traditional strategy is to immobilize them on solid supports comprising inorganic or organic materials. Through immobilization, their solubility and stability can be signicantly improved and the catalytic reactions can be more precisely controlled to meet high standards and tricky regulations in industry. An additional advantage of their immobilization includes facile recovery of the catalytic system from the reaction mixture at the end of the reactions so that the recovered exorbitant enzymes can be reused in the next run. Enzyme immobilization was rst reported on inorganic support materials through covalent linkage in 1969.1 Obviously, it is the most important factor to consider for enzyme immobilization that support materials should be chemically and mechanically benign and
6.1 Introduction ..................................................................................................225 6.2 Nanomaterials for Biocatalyst Immobilization ............................................226
