Controlled immobilisation of active enzymes on the cowpea mosaic virus capsid

47Citations
Citations of this article
49Readers
Mendeley users who have this article in their library.

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. © The Royal Society of Chemistry 2012.

Cite

CITATION STYLE

APA

Aljabali, A. A. A., Barclay, J. E., Steinmetz, N. F., Lomonossoff, G. P., & Evans, D. J. (2012). Controlled immobilisation of active enzymes on the cowpea mosaic virus capsid. Nanoscale, 4(18), 5640–5645. https://doi.org/10.1039/c2nr31485a

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free