Effect of glycosylation on the biochemical properties of beta-xylosidases from Aspergillus versicolor
| Autor: | Rosa dos Prazeres Melo Furriel, Maria de Lourdes Teixeira de Moraes Polizeli, Héctor Francisco Terenzi, Luis Henrique Souza Guimarães, João Atílio Jorge, Alexandre Favarin Somera, Marita Gimenez Pereira |
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| Rok vydání: | 2008 |
| Předmět: |
Glycosylation
Proteolysis macromolecular substances Xylose Applied Microbiology and Biotechnology Microbiology Fungal Proteins chemistry.chemical_compound Enzyme Stability medicine Glycoproteins chemistry.chemical_classification medicine.diagnostic_test Temperature food and beverages General Medicine Xylosidases Hydrogen-Ion Concentration Xylan carbohydrates (lipids) Enzyme Aspergillus chemistry Biochemistry Aspergillus versicolor Glycoprotein Protein Processing Post-Translational |
| Zdroj: | Journal of microbiology (Seoul, Korea). 47(3) |
| ISSN: | 1976-3794 |
| Popis: | 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 45 degrees C and 40 degrees C, respectively, and 35 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 55 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. |
| Databáze: | OpenAIRE |
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