dc.creator | SOMERA, Alexandre Favarin | |
dc.creator | PEREIRA, Marita Gimenez | |
dc.creator | GUIMARAES, Luis Henrique Souza | |
dc.creator | POLIZELI, Maria de Lourdes Teixeira de Moraes | |
dc.creator | TERENZI, Hector Francisco | |
dc.creator | FURRIEL, Rosa Prazeres Melo | |
dc.creator | JORGE, Joao Atilio | |
dc.date.accessioned | 2012-10-19T14:13:06Z | |
dc.date.accessioned | 2018-07-04T15:00:23Z | |
dc.date.available | 2012-10-19T14:13:06Z | |
dc.date.available | 2018-07-04T15:00:23Z | |
dc.date.created | 2012-10-19T14:13:06Z | |
dc.date.issued | 2009 | |
dc.identifier | JOURNAL OF MICROBIOLOGY, v.47, n.3, p.270-276, 2009 | |
dc.identifier | 1225-8873 | |
dc.identifier | http://producao.usp.br/handle/BDPI/20676 | |
dc.identifier | 10.1007/s12275-008-0286-9 | |
dc.identifier | http://dx.doi.org/10.1007/s12275-008-0286-9 | |
dc.identifier.uri | http://repositorioslatinoamericanos.uchile.cl/handle/2250/1617455 | |
dc.description.abstract | Aspergillus versicolor grown on xylan or xylose produces two beta-xylosidases with differences in biochemical properties and degree of glycosylation. We investigated the alterations in the biochemical properties of these beta-xylosidases after deglycosylation with Endo-H or PNGase F. After deglycosylation, both enzymes migrated faster in PAGE or SDS-PAGE exhibiting the same R(f). Temperature optimum of xylan-induced and xylose-induced beta-xylosidases was 45A degrees C and 40A degrees C, respectively, and 35A degrees C after deglycosylation. The xylan-induced enzyme was more active at acidic pH. After deglycosylation, both enzymes had the same pH optimum of 6.0. Thermal resistance at 55A degrees C showed half-life of 15 min and 9 min for xylose- and xylan-induced enzymes, respectively. After deglycosylation, both enzymes exhibited half-lives of 7.5 min. Native enzymes exhibited different responses to ions, while deglycosylated enzymes exhibited identical responses. Limited proteolysis yielded similar polypeptide profiles for the deglycosylated enzymes, suggesting a common polypeptide core with differential glycosylation apparently responsible for their biochemical and biophysical differences. | |
dc.language | eng | |
dc.publisher | MICROBIOLOGICAL SOCIETY KOREA | |
dc.relation | Journal of Microbiology | |
dc.rights | Copyright MICROBIOLOGICAL SOCIETY KOREA | |
dc.rights | restrictedAccess | |
dc.subject | beta-xylosidase | |
dc.subject | xylobiase | |
dc.subject | glycosylation | |
dc.subject | deglycosylation | |
dc.subject | glycoprotein | |
dc.subject | Aspergillus versicolor | |
dc.title | Effect of glycosylation on the biochemical properties of beta-xylosidases from Aspergillus versicolor | |
dc.type | Artículos de revistas | |