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Abstract
Background: The extracellular β-glucosidases (cellulose and xylan induced) and xylan-induced β-xylosidase from Aspergillus niger NCIM 1207 were purified to homogeneity. The protocols were based on fractional ethanol precipitation, pH and thermal stability, and separation of impurities by thermal denaturation. Results: The molecular weights of all the three enzymes were 122 and 336 kDa as estimated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and gel perme\ation chromatography. Mass spectrometric analysis revealed that cellulose and xylan-induced β-glucosidases showed 24 and 12% sequence coverage, respectively, with β-glucosidase A of A. niger CBS 513.88/FGSC A1513. Xylan-induced β-xylosidase exhibited 35% homology with probable exo-1,4-β-xylosidase of A. niger CBS 513.88/FGSC A1513 and 11% homology with β-glucosidase A of A. niger CBS 513.88/FGSC A1513. Conclusion: The enzymes are high-molecular weight proteins and are trimeric in nature. This is the first report on high-molecular weight trimeric β-xylosidase from fungal species.
Financial & competing interests disclosure
The authors have no relevant affiliations or financial involvement with any organization or entity with a financial interest in or financial conflict with the subject matter or materials discussed in the manuscript. This includes employment, consultancies, honoraria, stock ownership or options, expert testimony, grants or patents received or pending, or royalties.
No writing assistance was utilized in the production of this manuscript.