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Cloning and optimized expression of a GH-11 xylanase from Fusarium oxysporum in Pichia pastoris
National Technical University of Athens.
National Technical University of Athens.
2011 (English)In: New Biotechnology, ISSN 1871-6784, E-ISSN 1876-4347, Vol. 28, no 4, p. 369-374Article in journal (Refereed) Published
Abstract [en]

The endo-1,4-beta-xylanase gene xyn11a from Fusarium oxysporum, member of the fungal glycosyl hydrolase (GH) family 11, was cloned and expressed in Pichia pastoris. The mature xylanase gene, which generates after the excision of one intron and the secreting signal peptide, was placed under the control of an alcohol oxidase promoter (AOX1) in the plasmid pPICZ alpha C. The final construction was integrated into the genome of the methylotrophic yeast P. pastoris X33 and the ability to produce xylanase activity was evaluated in flask cultures. Recombinant P. pastoris efficiently secreted xylanase into the medium and produced high level of enzymatic activity (110 U/ml) after 216 hours of growth, under methanol induction. To achieve higher enzyme production, the influence of initial pH, methanol concentration, agitation and flask design was evaluated. Under optimum culture conditions, production of the recombinant xylanase increased by 50%, reaching a final yield of 170 U/ml, underpinning aeration as the most important factor in improving enzyme production.

Place, publisher, year, edition, pages
2011. Vol. 28, no 4, p. 369-374
Identifiers
URN: urn:nbn:se:ltu:diva-5529DOI: 10.1016/j.nbt.2011.03.002Local ID: 3a8ba605-ebf9-4be2-8a22-ce20af9bd9bbOAI: oai:DiVA.org:ltu-5529DiVA, id: diva2:978403
Note
Upprättat; 2011; 20130212 (ysko)Available from: 2016-09-29 Created: 2016-09-29 Last updated: 2017-11-24Bibliographically approved

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