dc.contributor.author | Pinar, Orkun | |
dc.contributor.author | Tamerler, Candan | |
dc.contributor.author | Yazgan Karataş, Ayten | |
dc.date.accessioned | 2018-12-14T19:27:40Z | |
dc.date.available | 2018-12-14T19:27:40Z | |
dc.date.issued | 2017 | |
dc.identifier.citation | Pinar, O., BEHAR, C. T., & KARATAŞ, A. (2017). Heterologous expression and characterization of a high redox potential laccase from Coriolopsis polyzona MUCL 38443. Turkish Journal of Biology, 41(2), 278-291. | en_US |
dc.identifier.uri | http://hdl.handle.net/1808/27520 | |
dc.description.abstract | In this study, a novel laccase gene, named as Cplcc1, and its corresponding cDNA were isolated and characterized from the
Coriolopsis polyzona MUCL 38443 strain. The Cplcc1 gene consists of a 1563-bp open reading frame encoding a protein of 520 amino acids with a 20-residue putative signal peptide. The size of the Cplcc1 gene is 2106 bp and it contains ten introns and five potential N-glycosylation sites. Additionally, the isolated full-length Cplcc1 cDNA was successfully expressed in Pichia pastoris. The heterologous expression conditions were also optimized and the highest activity value increased to 800 U L–1 with 1.5% methanol, 0.8 mM CuSO4, and 0.6% L-alanine supplementation. The recombinant laccase was partially purified and the molecular weight was found as approximately 54 kDa. The maximum oxidation activity was observed for 2,2-azinobis-(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) at pH 3.0. The optimal temperature was found as 70 °C. On the other hand, at 30 °C, the enzyme was stable for more than a week and its half-life was longer than 8 h. The Km, Vmax, kcat, and kcat Km
–1 values of the recombinant laccase were identified as 0.137 mM, 288.6 µmol min–1 L–1, 5.73 × 105 min–1, and 4.18 × 106 min–1 mM–1,respectively. Sodium azide, L-cysteine, and SDS were found as usual inhibitors. | en_US |
dc.publisher | TÜBİTAK | en_US |
dc.rights | This article is distributed under the terms of the Creative Commons Attribution License (CC-BY 4.0), which permits any use, distribution and reproduction in any medium, provided the original author(s) and source are credited. | en_US |
dc.rights.uri | https://creativecommons.org/licenses/by/4.0/ | en_US |
dc.subject | Coriolopsis polyzona | en_US |
dc.subject | Enzyme activity | en_US |
dc.subject | Heterologous expression | en_US |
dc.subject | Laccase | en_US |
dc.subject | Pichia pastoris | en_US |
dc.subject | Purification | en_US |
dc.title | Heterologous expression and characterization of a high redox potential laccase from Coriolopsis polyzona MUCL 38443 | en_US |
dc.type | Article | en_US |
dc.identifier.doi | 10.3906/biy-1605-51 | en_US |
kusw.oaversion | Scholarly/refereed, publisher version | en_US |
kusw.oapolicy | This item meets KU Open Access policy criteria. | en_US |
dc.rights.accessrights | openAccess | en_US |