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Characterization of an extracellular α-xylosidase involved in xyloglucan degradation in Aspergillus oryzae.
- Source :
-
Applied Microbiology & Biotechnology . Jan2022, Vol. 106 Issue 2, p675-687. 13p. - Publication Year :
- 2022
-
Abstract
- α-Xylosidases release the α-d-xylopyranosyl side chain from di- and oligosaccharides derived from xyloglucans and are involved in xyloglucan degradation. In this study, an extracellular α-xylosidase, named AxyB, is identified and characterized in Aspergillus oryzae. AxyB belongs to the glycoside hydrolase family 31 and releases d-xylose from isoprimeverose (α-d-xylopyranosyl-(1 → 6)-d-glucopyranose) and xyloglucan oligosaccharides. In the hydrolysis of xyloglucan oligosaccharides (XLLG, Glc4Xyl3Gal2 nonasaccharide; XLXG/XXLG, Glc4Xyl3Gal1 octasaccharide; and XXXG, Glc4Xyl3 heptasaccharide), AxyB releases one molecule of the xylopyranosyl side chain attached to the non-reducing end of the β-1,4-glucan main chain of these xyloglucan oligosaccharides to yield GLLG (Glc4Xyl2Gal2), GLXG/GXLG (Glc4Xyl2Gal1), and GXXG (Glc4Xyl2). A. oryzae has both extracellular and intracellular α-xylosidase, suggesting that xyloglucan oligosaccharides are degraded by a combination of isoprimeverose-producing oligoxyloglucan hydrolase and intracellular α-xylosidase and a combination of extracellular α-xylosidase and β-glucosidase(s) in A. oryzae. Key points: • An extracellular α-xylosidase, AxyB, is identified in Aspergillus oryzae. • AxyB releases the xylopyranosyl side chain from xyloglucan oligosaccharides. • Different sets of glycosidases degrade xyloglucan oligosaccharides in A. oryzae. [ABSTRACT FROM AUTHOR]
- Subjects :
- *KOJI
*GLUCANS
*BETA-glucans
*OLIGOSACCHARIDES
*XYLOGLUCANS
*GLYCOSIDASES
Subjects
Details
- Language :
- English
- ISSN :
- 01757598
- Volume :
- 106
- Issue :
- 2
- Database :
- Academic Search Index
- Journal :
- Applied Microbiology & Biotechnology
- Publication Type :
- Academic Journal
- Accession number :
- 154714392
- Full Text :
- https://doi.org/10.1007/s00253-021-11744-7