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Please use this identifier to cite or link to this item: https://doi.org/10.1016/j.jcis.2007.08.012
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dc.titleAdsorption, desorption, and conformational changes of lysozyme from thermosensitive nanomagnetic particles
dc.contributor.authorShamim, N.
dc.contributor.authorLiang, H.
dc.contributor.authorHidajat, K.
dc.contributor.authorUddin, M.S.
dc.date.accessioned2014-10-09T06:43:06Z
dc.date.available2014-10-09T06:43:06Z
dc.date.issued2008-04-01
dc.identifier.citationShamim, N., Liang, H., Hidajat, K., Uddin, M.S. (2008-04-01). Adsorption, desorption, and conformational changes of lysozyme from thermosensitive nanomagnetic particles. Journal of Colloid and Interface Science 320 (1) : 15-21. ScholarBank@NUS Repository. https://doi.org/10.1016/j.jcis.2007.08.012
dc.identifier.issn00219797
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/88508
dc.description.abstractAdsorption of globular protein, lysozyme, on thermosensitive poly(N-isopropylacrylamide) coated nanomagnetic particles was studied at different temperatures and pHs. It was observed that a maximum amount of lysozyme was adsorbed at a temperature above the lower critical solution temperature (LCST) (32 °C ) of the polymer and at the isoelectric point (p I = 11) of lysozyme. Desorption was carried out using either NaH2PO4 (pH 4) or NaSCN (pH 6) as the desorbing agents. Conformational changes in lysozyme on desorption from nanomagnetic particles was studied by circular dichroism and intrinsic fluorescence spectroscopy. Lysozyme desorbed by NaH2PO4 showed very little conformational changes while lysozyme desorbed by NaSCN showed significant conformational changes, and 87% enzymatic activity was retained in the desorbed enzyme for desorption by NaH2PO4. © 2007 Elsevier Inc. All rights reserved.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1016/j.jcis.2007.08.012
dc.sourceScopus
dc.subjectConformational changes
dc.subjectIsoelectric point
dc.subjectLower critical solution temperature (LCST)
dc.subjectLysozyme
dc.subjectN-isopropylacrylamide
dc.typeArticle
dc.contributor.departmentCHEMICAL & BIOMOLECULAR ENGINEERING
dc.description.doi10.1016/j.jcis.2007.08.012
dc.description.sourcetitleJournal of Colloid and Interface Science
dc.description.volume320
dc.description.issue1
dc.description.page15-21
dc.description.codenJCISA
dc.identifier.isiut000254091000003
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