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Purification and characterization of β-glucosidases and β-xylosidase of Aspergillus niger NCIM 1207
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 den...
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Published in: | Biofuels (London) 2013-03, Vol.4 (2), p.203-217 |
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description | 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. |
doi_str_mv | 10.4155/bfs.12.92 |
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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.</description><identifier>ISSN: 1759-7269</identifier><identifier>EISSN: 1759-7277</identifier><identifier>DOI: 10.4155/bfs.12.92</identifier><language>eng</language><publisher>London, UK: Future Science Ltd</publisher><ispartof>Biofuels (London), 2013-03, Vol.4 (2), p.203-217</ispartof><rights>Future Science Ltd 2013</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c274t-6af774e38546e7d4d1d8d4b52f29211e25d7eb35f3ee0620b9ca73f210b27de93</citedby><cites>FETCH-LOGICAL-c274t-6af774e38546e7d4d1d8d4b52f29211e25d7eb35f3ee0620b9ca73f210b27de93</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids></links><search><creatorcontrib>Khisti, Ujwala</creatorcontrib><creatorcontrib>Gokhale, Digambar</creatorcontrib><title>Purification and characterization of β-glucosidases and β-xylosidase of Aspergillus niger NCIM 1207</title><title>Biofuels (London)</title><description>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. 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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.</abstract><cop>London, UK</cop><pub>Future Science Ltd</pub><doi>10.4155/bfs.12.92</doi><tpages>15</tpages></addata></record> |
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title | Purification and characterization of β-glucosidases and β-xylosidase of Aspergillus niger NCIM 1207 |
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