dc.contributor.author | Sarı, Bilge | |
dc.contributor.author | Faiz, Özlem | |
dc.contributor.author | Genç, Berna | |
dc.contributor.author | Şişecioğlu, Melda | |
dc.contributor.author | Adıgüzel, Ahmet | |
dc.contributor.author | Adıgüzel, Gülşah | |
dc.date.accessioned | 2020-12-19T19:41:09Z | |
dc.date.available | 2020-12-19T19:41:09Z | |
dc.date.issued | 2018 | |
dc.identifier.citation | Sari, B., Faiz, O., Genc, B., Sisecioglu, M., Adiguzel, A., & Adiguzel, G. (2018). New xylanolytic enzyme from Geobacillus galactosidasius BS61 from a geothermal resource in Turkey. International journal of biological macromolecules, 119, 1017–1026. https://doi.org/10.1016/j.ijbiomac.2018.07.166 | en_US |
dc.identifier.issn | 0141-8130 | |
dc.identifier.issn | 1879-0003 | |
dc.identifier.uri | https://doi.org/10.1016/j.ijbiomac.2018.07.166 | |
dc.identifier.uri | https://hdl.handle.net/11436/1734 | |
dc.description | Adiguzel, Ahmet/0000-0001-8848-6647; GENC, BERNA/0000-0002-2790-9578 | en_US |
dc.description | WOS: 000447682100113 | en_US |
dc.description | PubMed: 30059740 | en_US |
dc.description.abstract | In this study, isolation, conventional and molecular characterizations of ten thermophilic bacteria from Rize/Ayder were carried out. Xylanase from Geobacillus galactosidasius BS61 (GenBank number: 10(447660) was purified by acetone precipitation, Diethylaminoethyl-cellulose and Sephadex G-100 chromatographies. the xylanase of G. galactosidasius BS61 in clarifying fruit juice was also investigated. Enzyme was purified 29.80-fold with 75.18% yield; and molecular weight was determined as 78.15 kDa. the optimum temperature of xylanase was 60 degrees C. the enzyme activity was maintained fully after 24 h and over 50% after 168 h at pH 4.0-10.0, while optimum pH was 7.0. K-m and V-max for beech wood xylan were measured as 3.18 mg mL(-1), 123 U mg protein(-1). in addition, Ca2+, Na+, Al3+, Zn2+, Cd2+, Mg2+, Ni2+, Cu2+ had decreasing effect on enzyme activity, while enzyme activity had been protected against anions, especially HSO3- and HPO42- stimulated enzyme activity. Xylanase applications (with 15 U/mL enzyme activity) in orange and pomegranate juices were increased; and the sugar and turbidity amounts were reduced 17.36% +/- 1.18 and 30.52 +/- 1.23, respectively. These results indicated that the xylanase of G. galactosidasius BS61 has biotechnological potential in juice clarification due to its stability against metal ions, chemicals and high pH-values. (C) 2018 Elsevier B.V. All rights reserved. | en_US |
dc.description.sponsorship | Research Development Centre of Ataturk UniversityAtaturk University [2015-339, FAD-2018-6352] | en_US |
dc.description.sponsorship | This work was supported by the Research Development Centre of Ataturk University (Grant numbers are 2015-339 and FAD-2018-6352). | en_US |
dc.language.iso | eng | en_US |
dc.publisher | Elsevier Science Bv | en_US |
dc.rights | info:eu-repo/semantics/closedAccess | en_US |
dc.subject | Thermophilic | en_US |
dc.subject | 16S rRNA sequencing | en_US |
dc.subject | BOX-PCR | en_US |
dc.subject | Cloning | en_US |
dc.subject | Geobacillus galactosidasius BS61 | en_US |
dc.subject | Xylanase | en_US |
dc.title | New xylanolytic enzyme from Geobacillus galactosidasius BS61 from a geothermal resource in Turkey | en_US |
dc.type | article | en_US |
dc.contributor.department | RTEÜ, Fen - Edebiyat Fakültesi, Kimya Bölümü | en_US |
dc.contributor.institutionauthor | Faiz, Özlem | |
dc.identifier.doi | 10.1016/j.ijbiomac.2018.07.166 | |
dc.identifier.volume | 119 | en_US |
dc.identifier.startpage | 1017 | en_US |
dc.identifier.endpage | 1026 | en_US |
dc.relation.journal | International Journal of Biological Macromolecules | en_US |
dc.relation.publicationcategory | Makale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanı | en_US |