Intense efforts have been directed at the stabilization of proteins because of their potential uses in organic synthesis, diagnostics, and the pharmaceutical industry. These efforts have resulted in a number of methods to stabilize enzymes including adsorbtion on inert supports or ion exchange resins, entrapment within a gel (with or without crosslinking of the gel or protein), covalent attachment to beads or polymeric supports, inclusion in micelles, chemical derivatization of the protein and mutagenesis. However, these methods do not provide a general approach to solving the problem of protein stability. We believed that the multi-site attachment of a carbohydrate-based macromolecule to the surface of a protein would provide structural stability and a water-like microenvironment for the protein under harsh reaction conditions.