Enzymes covalently immobilized on highly porous materials are demonstrated to have very high biocatalytic activity and good recyclability, exemplified by Candida antarctica Lipase B (CAL‐B). Polymerized high internal phase emulsions (PolyHIPEs, see figure) are developed for covalent grafting of proteins (enzymes) via the reaction of the protein surface lysine residues with active ester moieties in the monolithic material.
Virus particles are probably the most precisely defined nanometre-sized objects that can be formed by protein self-assembly. Although their natural function is the storage and transport of genetic material, they have more recently been applied as scaffolds for mineralization and as containers for the encapsulation of inorganic compounds. The reproductive power of viruses has been used to develop versatile analytical methods, such as phage display, for the selection and identification of (bio)active compounds. To date, the combined use of self-assembly and reproduction has not been used for the construction of catalytic systems. Here we describe a self-assembled system based on a plant virus that has its coat protein genetically modified to provide it with a lipase enzyme. Using single-object and bulk catalytic studies, we prove that the virus-anchored lipase molecules are catalytically active. This anchored biocatalyst, unlike man-made supported catalysts, has the capability to reproduce itself in vivo, generating many independent catalytically active copies.
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