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dc.contributor.authorOswald, Paul R.
dc.contributor.authorEvans, Rachel A.
dc.contributor.authorHenderson, William
dc.contributor.authorDaniel, Roy M.
dc.contributor.authorFee, Conan J.
dc.date.accessioned2010-08-30T02:52:45Z
dc.date.available2010-08-30T02:52:45Z
dc.date.issued1998
dc.identifier.citationOswald, P.R., Evans, R.A., Henderson, W., Daniel, R.M. & Fee, C.J. (1998). Properties of a thermostable β-glucosidase immobilized using tris(hydroxymethyl)phosphine as a highly effective coupling agent. Enzyme and Microbial Technology, 23(1-2), 14-19.en_NZ
dc.identifier.urihttps://hdl.handle.net/10289/4465
dc.description.abstractA very stable b-glucosidase (EC 3.2.1.21) was immobilized to polyacrylamide-magnetite beads, aminopropyl silica, and chitosan using tris(hydroxymethyl)phosphine (THP) or glutaraldehyde as the coupling reagent. The use of THP on chitosan resulted in greater than 90% yields with respect to free enzyme activity compared with only 60% observed when using the more conventional glutaraldehyde coupling reagent. THP-immobilized enzyme also lost activity more slowly than both glutaraldehyde-immobilized and the free enzyme when incubated at 90°C. Repetitive assays of THP and glutaraldehyde-immobilized enzyme also showed that THP was more able to retain active enzyme on the silica-based support. The pH optimum and Km app were unchanged with respect to free enzyme.en_NZ
dc.language.isoen
dc.publisherElsevieren_NZ
dc.subjecttris(hydroxymethyl)phosphineen_NZ
dc.subjectenzyme immobilizationen_NZ
dc.subjectβ-glucosidaseen_NZ
dc.subjectpolyacrylamide-magnetite beadsen_NZ
dc.subjectaminopropyl silicaen_NZ
dc.subjectchitosanen_NZ
dc.titleProperties of a thermostable β-glucosidase immobilized using tris(hydroxymethyl)phosphine as a highly effective coupling agenten_NZ
dc.typeJournal Articleen_NZ
dc.identifier.doi10.1016/S0141-0229(98)00005-2en_NZ
dc.relation.isPartOfEnzyme and Microbial Technologyen_NZ
pubs.begin-page14en_NZ
pubs.elements-id39716
pubs.end-page19en_NZ
pubs.issue1-2en_NZ
pubs.volume23en_NZ


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