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dc.contributor.CRUESPUniversidade Estadual de Campinaspt_BR
dc.typeArtigo de periódicopt_BR
dc.titleRaman spectroscopic monitoring and control of aprotinin supersaturation in hanging-drop crystallizationpt_BR
dc.contributor.authorTamagawa, REpt_BR
dc.contributor.authorMiranda, EApt_BR
dc.contributor.authorBerglund, KApt_BR
unicamp.authorLulea Univ Technol, Div Chem Engn Design, SE-97187 Lulea, Sweden Campinas State Univ, Sch Chem Engn, Dept Bioproc, Campinas, SP, Brazil Michigan State Univ, Dept Chem, E Lansing, MI 48824 USA Michigan State Univ, Dept Chem Engn & Mat Sci, E Lansing, MI 48824 USApt_BR
dc.subject.wosPancreatic Trypsin-inhibitorpt_BR
dc.subject.wosBpti Moleculespt_BR
dc.subject.wosPrenucleationpt_BR
dc.subject.wosFormpt_BR
dc.description.abstractFiber optic Raman spectroscopy is used for in situ monitoring of supersaturation during the hanging-drop crystallization of aprotinin. Schwartz and Berglund (1999) previously demonstrated this technique for lysozyme crystallization and showed it combines two critical elements for protein crystallization studies: real-time monitoring/ control of supersaturation and small amounts of sample. Experiments were carried out using 10 muL of protein solution. A partial-least-squares (PLS) calibration based on Raman spectra of standard solutions allowed an accurate measurement of aprotinin in a range of 2-100 mg/mL with a standard error of 0.54 mg/mL determined by a leave-one-out cross validation. A 10x microscope attached to a Raman fiber optic probe allowed the monitoring of the hanging-drop liquid phase in a noninvasive and real-time mode. Aprotinin solubility determined by measuring the protein concentration of drop solution at equilibrium decreased with increase in NaCl concentration. By continuously collecting Raman spectra of the liquid phase in the drop, the protein concentration was monitored in real time during the whole process. Control of supersaturation by manipulating the evaporation rate of the drop solution allowed the optimization of the process, leading to an increase in the resulting crystal size.pt
dc.relation.ispartofCrystal Growth & Designpt_BR
dc.relation.ispartofabbreviationCryst. Growth Des.pt_BR
dc.publisher.cityWashingtonpt_BR
dc.publisher.countryEUApt_BR
dc.publisherAmer Chemical Socpt_BR
dc.date.issued2002pt_BR
dc.date.monthofcirculationJUL-AUGpt_BR
dc.identifier.citationCrystal Growth & Design. Amer Chemical Soc, v. 2, n. 4, n. 263, n. 267, 2002.pt_BR
dc.language.isoenpt_BR
dc.description.volume2pt_BR
dc.description.issuenumber4pt_BR
dc.description.firstpage263pt_BR
dc.description.lastpage267pt_BR
dc.rightsfechadopt_BR
dc.sourceWeb of Sciencept_BR
dc.identifier.issn1528-7483pt_BR
dc.identifier.wosidWOS:000176925900004pt_BR
dc.identifier.doi10.1021/cg025524kpt_BR
dc.date.available2014-11-18T20:29:20Z
dc.date.available2015-11-26T16:58:39Z-
dc.date.accessioned2014-11-18T20:29:20Z
dc.date.accessioned2015-11-26T16:58:39Z-
dc.description.provenanceMade available in DSpace on 2014-11-18T20:29:20Z (GMT). No. of bitstreams: 1 WOS000176925900004.pdf: 118705 bytes, checksum: f8609844f39729a0789de4df539a0214 (MD5) Previous issue date: 2002en
dc.description.provenanceMade available in DSpace on 2015-11-26T16:58:39Z (GMT). No. of bitstreams: 2 WOS000176925900004.pdf: 118705 bytes, checksum: f8609844f39729a0789de4df539a0214 (MD5) WOS000176925900004.pdf.txt: 20071 bytes, checksum: 7dad7244890ac42f9b0ac6e2e3452981 (MD5) Previous issue date: 2002en
dc.identifier.urihttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/58839pt_BR
dc.identifier.urihttp://www.repositorio.unicamp.br/handle/REPOSIP/58839
dc.identifier.urihttp://repositorio.unicamp.br/jspui/handle/REPOSIP/58839-
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