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Characterization of a recombinant bifunctional xylosidase/arabinofuranosidase from Phanerochaete chrysosporium.
- Source :
-
Journal of Bioscience & Bioengineering . Aug2013, Vol. 116 Issue 2, p152-159. 8p. - Publication Year :
- 2013
-
Abstract
- A bifunctional xylosidase/arabinofuranosidase gene (PcXyl) was cloned from the cDNA library of Phanerochaete chrysosporium and further expressed in Pichia pastoris. Enzymatic assay indicated that P. pastoris produced rPcXyl at a level of 26,141 U l−1. The xylosidase and arabinofuranosidase activities of rPcXyl were maximized, respectively, at pHs of 5.0 and 5.5 and temperatures of 45°C and 50°C. SDS-PAGE revealed a single band of purified rPcXyl of 83 kDa. Cu2+ and Zn2+ completely inhibited the enzyme activity of rPcXyl. The enzyme activity of rPcXyl was increased 151%, 126% and 123%, respectively, in the presence of glucose, xylose and arabinose at concentrations of 5 mM. rPcXyl hydrolyzed xylobiose to xylose and xylotriose to xylose and xylobiose, indicating rPcXyl acts as an exo-type enzyme. Additionally, rPcXyl enhanced xylose release from xylan substrates in synergy with rPcXynC. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 13891723
- Volume :
- 116
- Issue :
- 2
- Database :
- Academic Search Index
- Journal :
- Journal of Bioscience & Bioengineering
- Publication Type :
- Academic Journal
- Accession number :
- 89119567
- Full Text :
- https://doi.org/10.1016/j.jbiosc.2013.02.004