Characterisation of a recombinant β-xylosidase (xylA) from Aspergillus oryzae expressed in Pichia pastoris

β-xylosidases catalyse the hydrolysis of short chain xylooligosaccharides from their non-reducing ends into xylose. In this study we report the heterologous expression of Aspergillus oryzae β-xylosidase (XylA) in Pichia pastoris under the control of the glyceraldehyde-3-phosphate dehydrogenase promo...

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Main Authors: Kirikyali, Narin, Wood, Jonathan, Connerton, Ian F.
Format: Article
Published: SpringerOpen 2014
Online Access:https://eprints.nottingham.ac.uk/28794/
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author Kirikyali, Narin
Wood, Jonathan
Connerton, Ian F.
author_facet Kirikyali, Narin
Wood, Jonathan
Connerton, Ian F.
author_sort Kirikyali, Narin
building Nottingham Research Data Repository
collection Online Access
description β-xylosidases catalyse the hydrolysis of short chain xylooligosaccharides from their non-reducing ends into xylose. In this study we report the heterologous expression of Aspergillus oryzae β-xylosidase (XylA) in Pichia pastoris under the control of the glyceraldehyde-3-phosphate dehydrogenase promoter. The recombinant enzyme was optimally active at 55°C and pH 4.5 with Km and Vmax values of 1.0 mM and 250 μmol min−1 mg−1 respectively against 4-nitrophenyl β-xylopyranoside. Xylose was a competitive inhibitor with a Ki of 2.72 mM, whereas fructose was an uncompetitive inhibitor reducing substrate binding affinity (Km) and conversion efficiency (Vmax). The enzyme was characterised to be an exo-cutting enzyme releasing xylose from the non-reducing ends of β-1,4 linked xylooligosaccharides (X2, X3 and X4). Catalytic conversion of X2, X3 and X4 decreased (Vmax and kcat) with increasing chain length.
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spelling nottingham-287942020-05-04T16:51:55Z https://eprints.nottingham.ac.uk/28794/ Characterisation of a recombinant β-xylosidase (xylA) from Aspergillus oryzae expressed in Pichia pastoris Kirikyali, Narin Wood, Jonathan Connerton, Ian F. β-xylosidases catalyse the hydrolysis of short chain xylooligosaccharides from their non-reducing ends into xylose. In this study we report the heterologous expression of Aspergillus oryzae β-xylosidase (XylA) in Pichia pastoris under the control of the glyceraldehyde-3-phosphate dehydrogenase promoter. The recombinant enzyme was optimally active at 55°C and pH 4.5 with Km and Vmax values of 1.0 mM and 250 μmol min−1 mg−1 respectively against 4-nitrophenyl β-xylopyranoside. Xylose was a competitive inhibitor with a Ki of 2.72 mM, whereas fructose was an uncompetitive inhibitor reducing substrate binding affinity (Km) and conversion efficiency (Vmax). The enzyme was characterised to be an exo-cutting enzyme releasing xylose from the non-reducing ends of β-1,4 linked xylooligosaccharides (X2, X3 and X4). Catalytic conversion of X2, X3 and X4 decreased (Vmax and kcat) with increasing chain length. SpringerOpen 2014-08-31 Article PeerReviewed Kirikyali, Narin, Wood, Jonathan and Connerton, Ian F. (2014) Characterisation of a recombinant β-xylosidase (xylA) from Aspergillus oryzae expressed in Pichia pastoris. AMB Express, 4 (68). pp. 1-7. ISSN 2191-0855 http://www.amb-express.com/content/4/1/68 doi:10.1186/s13568-014-0068-1 doi:10.1186/s13568-014-0068-1
spellingShingle Kirikyali, Narin
Wood, Jonathan
Connerton, Ian F.
Characterisation of a recombinant β-xylosidase (xylA) from Aspergillus oryzae expressed in Pichia pastoris
title Characterisation of a recombinant β-xylosidase (xylA) from Aspergillus oryzae expressed in Pichia pastoris
title_full Characterisation of a recombinant β-xylosidase (xylA) from Aspergillus oryzae expressed in Pichia pastoris
title_fullStr Characterisation of a recombinant β-xylosidase (xylA) from Aspergillus oryzae expressed in Pichia pastoris
title_full_unstemmed Characterisation of a recombinant β-xylosidase (xylA) from Aspergillus oryzae expressed in Pichia pastoris
title_short Characterisation of a recombinant β-xylosidase (xylA) from Aspergillus oryzae expressed in Pichia pastoris
title_sort characterisation of a recombinant β-xylosidase (xyla) from aspergillus oryzae expressed in pichia pastoris
url https://eprints.nottingham.ac.uk/28794/
https://eprints.nottingham.ac.uk/28794/
https://eprints.nottingham.ac.uk/28794/