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dc.contributor.authorLiao, Y. H.
dc.contributor.authorMartin, Gary P.
dc.contributor.authorBrown, Marc
dc.date.accessioned2013-06-24T09:15:54Z
dc.date.available2013-06-24T09:15:54Z
dc.date.issued2004-07
dc.identifier.citationLiao , Y H , Martin , G P & Brown , M 2004 , ' Investigation of the stabilisation of freeze-dried lysozyme and the physical properties of the formulations ' European Journal of Pharmaceutics and Biopharmaceutics , vol. 58 , no. 1 , pp. 15-24 . https://doi.org/10.1016/j.ejpb.2004.03.020
dc.identifier.issn0939-6411
dc.identifier.otherPURE: 628659
dc.identifier.otherPURE UUID: aa3e023a-1309-4d35-9aca-41d51197fb94
dc.identifier.otherWOS: 000222726000004
dc.identifier.otherScopus: 2942685201
dc.identifier.urihttp://hdl.handle.net/2299/10911
dc.description.abstractThe long-term stability of a protein formulation requires that the glass transition temperature (T-g) of the formulation should be maximised and the perturbation of the protein native structure in the dried form after processing minimised. In the present study, the stabilisation of lysozyme structure conferred by excipients was monitored using second derivative Fourier transform infrared spectroscopy and the physical properties of protein formulations were investigated using differential scanning calorimetry. The results showed that the preservation of protein native structure during freeze-drying and the T-g of freeze-dried formulations were excipient- and excipient to enzyme mass ratio-dependent. The freeze-dried lysozyme appeared to be less effectively stabilised compared with the spray-dried enzyme when the excipients and the excipient to enzyme mass ratios were the same. In terms of the preservation of the secondary structure of lysozyme, glycerol and sucrose seemed to be more efficient than trehalose, although the T-g of trehalose-containing formulations were found to be higher than the T-g of the equivalent sucrose-based ones. With adding either trehalose or dextran to sucrose-containing formulations, the stabilisation of lysozyme native structure could be as effective as with sucrose alone, whilst the T-g could be enhanced. The results in this study suggested that lysozyme, processed by freeze-drying, is stabilised primarily by the water substitution mechanism. (C) 2004 Elsevier B.V. All rights reserved.en
dc.format.extent10
dc.language.isoeng
dc.relation.ispartofEuropean Journal of Pharmaceutics and Biopharmaceutics
dc.subjectfreeze-drying/lyophilisation
dc.subjectspray-drying
dc.subjectprotein formulation
dc.subjectprotein unfolding
dc.subjectprotein aggregation
dc.subjectphysical stability
dc.subjectGLASS-TRANSITION TEMPERATURE
dc.subjectSTORAGE STABILITY
dc.subjectMOLECULAR MOBILITY
dc.subjectPROTEIN CONFORMATION
dc.subjectMONOCLONAL-ANTIBODY
dc.subjectAMORPHOUS STATE
dc.subjectSYSTEMS
dc.subjectLYOPHILIZATION
dc.subjectAGGREGATION
dc.subjectADDITIVES
dc.titleInvestigation of the stabilisation of freeze-dried lysozyme and the physical properties of the formulationsen
dc.contributor.institutionDepartment of Pharmacy
dc.contributor.institutionSchool of Life and Medical Sciences
dc.contributor.institutionHealth & Human Sciences Research Institute
dc.contributor.institutionCentre for Research into Topical Drug Delivery and Toxicology
dc.contributor.institutionPharmaceutics
dc.contributor.institutionSkin and Nail Group
dc.contributor.institutionAirway Group
dc.contributor.institutionBioadhesive Drug Delivery Group
dc.contributor.institutionNanopharmaceutics
dc.contributor.institutionPharmaceutical Analysis and Product Characterisation
dc.description.statusPeer reviewed
dc.relation.schoolSchool of Life and Medical Sciences
rioxxterms.versionofrecordhttps://doi.org/10.1016/j.ejpb.2004.03.020
rioxxterms.typeJournal Article/Review
herts.preservation.rarelyaccessedtrue
herts.rights.accesstyperestrictedAccess


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