Please use this identifier to cite or link to this item: https://hdl.handle.net/11147/5526
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dc.contributor.authorCeylan, Çağatay-
dc.contributor.authorKaraçiçek, Bilge-
dc.date.accessioned2017-05-16T13:26:13Z-
dc.date.available2017-05-16T13:26:13Z-
dc.date.issued2015-
dc.identifier.citationCeylan, Ç., and Karaçiçek, B. (2015). Structural and functional characterization of solution, gel, and aggregated forms of trypsin in organic solvent-assisted and pH-induced phase changes. Turkish Journal of Biochemistry, 40(1), 81-87. doi:10.5505/tjb.2015.65002en_US
dc.identifier.issn0250-4685-
dc.identifier.issn1303-829X-
dc.identifier.urihttp://doi.org/10.5505/tjb.2015.65002-
dc.identifier.urihttp://hdl.handle.net/11147/5526-
dc.identifier.urihttps://search.trdizin.gov.tr/yayin/detay/206316-
dc.description.abstractIn this study the effect of three different physicochemical parameters on pHtriggered gelation and aggregation of bovine pancreatic trypsin changes and structural and functional changes in these changes in alcohol-water mixtures were studied. Methods: Trypsin gelation times were studied using inverted tube method. Trypsin stability was studied using trypsin enzyme assay. Protein secondary structural changes were monitored using FTIR spectroscopy. Gel and aggregate macrostructures and morphologies were viewed using Scanning Electron Microscopy. Results: The solution phase was observed in the absence of both NaOH and CaCl2. The gel phase was observed in the absence of the either. The aggregate phase was observed in the presence of the both agents all depending on trypsin concentrations used. Trypsin stability studies showed that there were a nearly 53 and 32% specific activity losses after the gelation and aggregation processes. According to FTIR studies β–sheet structure in 1637 cm-1 band disappeared in trypsin gel and trypsin aggregates. Increases in α–helix structure in 1651 cm-1 in trypsin gel and aggregates were observed. Iodoacetamide delayed the gelation and prevented the aggregation indicating the importance of intermolecular disulfides in the both processes. Conclusion: Trypsin gelation was caused by the denaturation of the protein three dimensional structures. The gel and aggregate formation indicates a secondary structural change towards α–helix structure formation at the expense of β–sheet structure and formation of intermolecular disulfide bonds.en_US
dc.description.abstractAmaç: Bu çalışmada alkol-su karışımlarında pH tarafından tetiklenen sığır pankreatik tripsin jelleşmesi ve agregasyonu faz değişiklikleri üzerine üç değişik fizikokimyasal değişkenin yapısal ve fonksiyonel etkileri çalışılmıştır. Metod: Tripsin jelleşmesi ters tüp metodu ile çalışılmıştır. Tripsin stabilitesi tripsin enzim aktivitesi tayiniyle çalışılmıştır. Protein ikinci yapı değişiklikleri FTIR spektroskopisi metodu ile gözlenmiştir. Jel ve agregat makroyapıları ve morfolojileri taramalı elektron mikroskopisi yöntemiyle incelenmiştir.en_US
dc.description.sponsorshipIZTECH Scientific Research Council (BAP) (2011IYTE11--2008IYTE22)en_US
dc.language.isoenen_US
dc.publisherTürk Biyokimya Derneğien_US
dc.relation.ispartofTurkish Journal of Biochemistryen_US
dc.rightsinfo:eu-repo/semantics/openAccessen_US
dc.subjectAggregationen_US
dc.subjectFTIRen_US
dc.subjectGelationen_US
dc.subjectTrypsinen_US
dc.subjectPhase transitionen_US
dc.titleStructural and functional characterization of solution, gel, and aggregated forms of trypsin in organic solvent-assisted and pH-induced phase changesen_US
dc.title.alternativeTrpsinin çözelti, jel ve agregat formlarının organik çözgen içeren ve pH-tektiklenmiş faz geçişlerinde yapısal ve fonksiyonel incelenmesien_US
dc.typeArticleen_US
dc.authoridTR45775en_US
dc.institutionauthorCeylan, Çağatay-
dc.institutionauthorKaraçiçek, Bilge-
dc.departmentİzmir Institute of Technology. Food Engineeringen_US
dc.identifier.volume40en_US
dc.identifier.issue1en_US
dc.identifier.startpage81en_US
dc.identifier.endpage87en_US
dc.identifier.wosWOS:000351543800009en_US
dc.identifier.scopus2-s2.0-84923030165en_US
dc.relation.publicationcategoryMakale - Ulusal Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.identifier.doi10.5505/tjb.2015.65002-
dc.relation.doi10.5505/tjb.2015.65002en_US
dc.coverage.doi10.5505/tjb.2015.65002en_US
dc.identifier.trdizinid206316en_US
dc.identifier.wosqualityQ4-
dc.identifier.scopusqualityQ3-
item.openairetypeArticle-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.grantfulltextopen-
item.fulltextWith Fulltext-
item.languageiso639-1en-
item.cerifentitytypePublications-
crisitem.author.dept03.08. Department of Food Engineering-
Appears in Collections:Food Engineering / Gıda Mühendisliği
Scopus İndeksli Yayınlar Koleksiyonu / Scopus Indexed Publications Collection
TR Dizin İndeksli Yayınlar / TR Dizin Indexed Publications Collection
WoS İndeksli Yayınlar Koleksiyonu / WoS Indexed Publications Collection
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