Controlled immobilisation of active enzymes on the cowpea mosaic virus capsid

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...

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Bibliographic Details
Published inNanoscale Vol. 4; no. 18; pp. 5640 - 5645
Main Authors Aljabali, Alaa A A, Barclay, J Elaine, Steinmetz, Nicole F, Lomonossoff, George P, Evans, David J
Format Journal Article
LanguageEnglish
Published England 21.09.2012
Subjects
Biocatalysis
Biosensing Techniques
Capsid Proteins - chemistry
Capsid Proteins - metabolism
Comovirus - metabolism
Cowpea mosaic virus
Enzymes, Immobilized - metabolism
Glucose Oxidase - chemistry
Glucose Oxidase - metabolism
Horseradish Peroxidase - chemistry
Horseradish Peroxidase - metabolism
Oxidation-Reduction
Periodic Acid - chemistry
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Summary: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.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
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ISSN:2040-3364
2040-3372
DOI:10.1039/c2nr31485a