Work

Controlled immobilisation of active enzymes on the cowpea mosaic virus capsid

Year: 2012

Type: article

Abstract: Immobilisation of horseradish peroxidase (HRP) and glucose oxidase (GOX) via covalent attachment of modified enzyme carbohydrate to the exterior of the cowpea mosaic virus (CPMV) capsid gave high retention of enzymatic activity. The number of enzymes bound per virus was determined to be about eleven for HRP and 2-3 for GOX. This illustrates that relatively large biomacromolecules can be readily coupled to the virus surface using simple conjugation strategies. Virus-biomacromolecule hybrids have great potential for uses in catalysis, diagnostic assays or biosensors.

Source: Nanoscale

DOI: 10.1039/c2nr31485a

Authors: Alaa A. A. Aljabali, J. Elaine Barclay, Nicole F. Steinmetz, George P. Lomonossoff, David J. Evans

Institutions: John Innes Centre, Norwich Research Park, Case Western Reserve University

Language: English

Topic: Enzyme Catalysis and Immobilization

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: hybrid

Funders: Directorate for Biological Sciences, Biotechnology and Biological Sciences Research Council

Award: G5277250144