Secretive expression of bacterial β-xylosidase gene including hexahistidin-tag in Pichia pastoris
| Author | Shirin Yousefian | en |
| Author | Omid Ranaei siadat | en |
| Author | Ehsan Dehnavi | en |
| Author | Mohammadtaghy BarChianBorojeni | en |
| Author | Farnaz Nikzad jamnani | en |
| Issued Date | 2013-09-30 | en |
| Abstract | Introduction: β-D-Xylosidases (EC 3.2.1.37), one of the most important hemicellulases with high potential industrial application such as bioethanol production, are exo-type glycosidases that catalyze the successive removal of β-xylosyl residues from the non-reducing termini of xylobiose and higher linear β-1,4-xylooligosaccharides and in conjunction with β-xylanases are essential in completely depolymerizing xylan. The aim of this study was secretive expression of bacterial β-xylosidase gene including hexahistidin-tag in Pichia pastoris in order to achieve high level expression and enzyme purification subsequently. Materials and Methods: In this study, after optimizing the sequence of protein encoding bacterial β-xylosidase based on the expression codon usage of Pichia pastoris and addition of 6xHis-tag sequence through suitable designed primers to gene, transformation of recombinant plasmids was performed through electroporation method into the expression yeast. Results: The results showed that the recombinant β-xylosidase production was 40 U/L with 0/6 U/mg specific activity in flask culture. Conclusion: Cloning and successful expression of bacterial β-xylosidase gene was carried out in order to obtain an active and stable enzyme with high level expression from yeast expression system | en |
| DOI | https://doi.org/ | en |
| URI | https://brieflands.com/journals/koomesh/articles/152592 | en |
| Keyword | Yeasts, Xylosidases, Histidine, Gene expressio | en |
| Keyword | مخمرها، گزایلوزیدازها، هیستیدین، بیان ژنی | en |
| Publisher | Brieflands | en |
| Title | Secretive expression of bacterial β-xylosidase gene including hexahistidin-tag in Pichia pastoris | en |
| Type | Research Article | en |
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