Enzymes are protein catalysts that have many useful functions in industrial and technological applications, however the stability of enzymes is often a major barrier for greater utilization in many advanced applications. One approach toward enhancing the stability of enzymes is to encapsulate them in a biological protein cage derived from viruses, called a virus-like particle (VLP), which can provide a protective structure around the enzyme that is predicted to enhance overall stability and provide a molecular scaffold that can be chemically modified without direct modification of the enzymes entrapped inside. For our studies, we investigate the encapsulation of enzymes inside the Hong Kong 97 (HK-97) bacteriophage derived VLP, which forms a unique molecular chain mail catenane protein cage structure in its mature head form. The research presented focuses on encapsulation of GFP to determine optimal methods for enzyme encapsulation inside the HK-97 VLP and the investigation of encapsulation of the CelB enzyme. The enzyme CelB is a beta-galactosidase that is of interest for biofuels and synthesis of pharmaceuticals and has properties that make it a useful “model” enzyme for initial studies.

Examination of the encapsulation of protein cargoes inside the HK97 virus-like particle

Macromolecular Chemistry: The Second Century

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ACS Spring 2020 National Meeting & Expo

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.