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dc.contributor.authorYenenler, Aslı
dc.contributor.authorKurt, Hasan
dc.contributor.authorSezerman, Osman Uğur
dc.date.accessioned10.07.201910:49:13
dc.date.accessioned2019-07-10T19:51:03Z
dc.date.available10.07.201910:49:13
dc.date.available2019-07-10T19:51:03Z
dc.date.issued2019en_US
dc.identifier.citationYenenler, A., Kurt, H. ve Sezermen, O. U. (2019). Enhancing enzymatic properties of endoglucanase i enzyme from trichoderma reesei via swapping from cellobiohydrolase i enzyme. Catalysts, 9(2). https://dx.doi.org/10.3390/catal9020130en_US
dc.identifier.issn2073-4344
dc.identifier.urihttps://dx.doi.org/10.3390/catal9020130
dc.identifier.urihttps://hdl.handle.net/20.500.12511/2137
dc.descriptionWOS: 000460702200024en_US
dc.description.abstractUtilizing plant-based materials as a biofuel source is an increasingly popular attempt to redesign the global energy cycle. This endeavour underlines the potential of cellulase enzymes for green energy production and requires the structural and functional engineering of natural enzymes to enhance their utilization. In this work, we aimed to engineer enzymatic and functional properties of Endoglucanase I (EGI) by swapping the Ala43-Gly83 region of Cellobiohydrolase I (CBHI) from Trichoderma reesei. Herein, we report the enhanced enzymatic activity and improved thermal stability of the engineered enzyme, called EGI_swapped, compared to EGI. The difference in the enzymatic activity profile of EGI_swapped and the EGI enzymes became more pronounced upon increasing metal-ion concentrations in the reaction media. Notably, the engineered enzyme retained a considerable level of enzymatic activity after thermal incubation for 90 min at 70 degrees C while EGI completely lost its enzymatic activity. Circular Dichroism spectroscopy studies revealed distinctive conformational and thermal susceptibility differences between EGI_swapped and EGI enzymes, confirming the improved structural integrity of the swapped enzyme. This study highlights the importance of swapping the metal-ion coordination region in the engineering of EGI enzyme for enhanced structural and thermal stability.en_US
dc.description.sponsorshipScientific and Technological Research Council of Turkey [112T901]en_US
dc.description.sponsorshipThe Scientific and Technological Research Council of Turkey supported this work with grant number 112T901. The authors have special thanks to Yusuf Tutus (Sabanci University) for contribution to ICP-OES readings.en_US
dc.language.isoengen_US
dc.publisherMDPIen_US
dc.rightsinfo:eu-repo/semantics/openAccessen_US
dc.rightsAttribution 4.0 International*
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/*
dc.subjectEndoglucanese Ien_US
dc.subjectCellbiohydrolase Ien_US
dc.subjectTrichoderma Reeseien_US
dc.subjectSwappingen_US
dc.subjectProtein Engineeringen_US
dc.subjectDivalent Metal Ionen_US
dc.titleEnhancing enzymatic properties of endoglucanase i enzyme from trichoderma reesei via swapping from cellobiohydrolase i enzymeen_US
dc.typearticleen_US
dc.relation.journalCatalystsen_US
dc.departmentİstanbul Medipol Üniversitesi, Mühendislik ve Doğa Bilimleri Fakültesi, Biyomedikal Mühendisliği Bölümüen_US
dc.authorid0000-0002-1677-644Xen_US
dc.identifier.volume9en_US
dc.identifier.issue2en_US
dc.relation.ecinfo:eu-repo/grantAgreement/TUBITAK/SOBAG/112T901en_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.identifier.doi10.3390/catal9020130en_US


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