dc.contributor.author | Ekinci, Arife Pınar | |
dc.contributor.author | Dinçer, Barbaros | |
dc.contributor.author | Baltaş, Nimet | |
dc.contributor.author | Adıgüzel, Ahmet | |
dc.date.accessioned | 2020-12-19T19:55:36Z | |
dc.date.available | 2020-12-19T19:55:36Z | |
dc.date.issued | 2016 | |
dc.identifier.citation | Ekinci, A. P., Dinçer, B., Baltaş, N., & Adıgüzel, A. (2016). Partial purification and characterization of lipase from Geobacillus stearothermophilus AH22. Journal of enzyme inhibition and medicinal chemistry, 31(2), 325–331. https://doi.org/10.3109/14756366.2015.1024677 | en_US |
dc.identifier.issn | 1475-6366 | |
dc.identifier.issn | 1475-6374 | |
dc.identifier.uri | https://doi.org/10.3109/14756366.2015.1024677 | |
dc.identifier.uri | https://hdl.handle.net/11436/2558 | |
dc.description | Adiguzel, Ahmet/0000-0001-8848-6647 | en_US |
dc.description | WOS: 000368719800018 | en_US |
dc.description | PubMed: 25798692 | en_US |
dc.description.abstract | The lipase was partially purified by ion exchange chromatography and gel filtration column chromatography, and was characterized from Geobacillus stearothermophilus AH22 strain. the lipase was purified 18.3-folds with 19.7% recovery. the lipase activity was determined by using p-nitrophenyl esters (C-2-C-12) as substrates. the K-m values of the enzyme for these substrates were found as 0.16, 0.02, 0.19 and 0.55mM, respectively, while V-max values were 0.52, 1.03, 0.72 and 0.15 Umg(-1). the enzyme showed maximum activity at 50 degrees C and between pH 8.0 and 9.0. the enzyme was found to be quite stable at pH range of 4.0-10.0, and thermal stability between 50 and 60 degrees C. It was found that the best inhibitory effect of the enzyme activity was of Hg2+. the inhibitory effect as orlistat, catechin, propyl paraben, p-coumaric acid, 3,4-dihydroxy hydro-cinnamic acid was examined. These results suggest that G. stearothermophilus AH22 lipase presents very suitable properties for industrial applications. | en_US |
dc.description.sponsorship | Research Fund of Recep Tayyip Erdogan UniversityRecep Tayyip Erdogan University [2010.102.02.3] | en_US |
dc.description.sponsorship | This work was financially supported by Research Fund of Recep Tayyip Erdogan University (Project No: 2010.102.02.3). | en_US |
dc.language.iso | eng | en_US |
dc.publisher | Taylor & Francis Ltd | en_US |
dc.rights | info:eu-repo/semantics/closedAccess | en_US |
dc.subject | Characterization | en_US |
dc.subject | Geobacillus stearothermophilus AH22 | en_US |
dc.subject | Lipase | en_US |
dc.subject | Partial purification | en_US |
dc.title | Partial purification and characterization of lipase from Geobacillus stearothermophilus AH22 | en_US |
dc.type | article | en_US |
dc.contributor.department | RTEÜ, Fen - Edebiyat Fakültesi, Kimya Bölümü | en_US |
dc.contributor.institutionauthor | Ekinci, Arife Pınar | |
dc.contributor.institutionauthor | Dinçer, Barbaros | |
dc.contributor.institutionauthor | Baltaş, Nimet | |
dc.identifier.doi | 10.3109/14756366.2015.1024677 | |
dc.identifier.volume | 31 | en_US |
dc.identifier.issue | 2 | en_US |
dc.identifier.startpage | 325 | en_US |
dc.identifier.endpage | 331 | en_US |
dc.ri.edit | oa | en_US |
dc.relation.journal | Journal of Enzyme Inhibition and Medicinal Chemistry | en_US |
dc.relation.publicationcategory | Makale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanı | en_US |