Effect of Glycosylation on the Biochemical Properties of beta-Xylosidases from Aspergillus versicolor

Alexandre Favarin Somera; Marita Gimenez Pereira; Luis Henrique Souza Guimaraes; Maria de Lourdes Teixeira de Moraes Polizeli; Hector Francisco Terenzi; Rosa Prazeres Melo Furriel; Joao Atilio Jorge

doi:10.1007/s12275-008-0286-9

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Effect of Glycosylation on the Biochemical Properties of beta-Xylosidases from Aspergillus versicolor: Alexandre Favarin Somera ¹, Marita Gimenez Pereira ¹, Luis Henrique Souza Guimaraes ¹, Maria de Lourdes Teixeira de Moraes Polizeli ¹, Hector Francisco Terenzi ¹, Rosa Prazeres Melo Furriel ², Joao Atilio Jorge ¹; Journal of Microbiology 2009;47(3):270-276.
DOI: https://doi.org/10.1007/s12275-008-0286-9
Published online: June 26, 2009

¹Departamentos de Biologia e Quimica, Universidade de Sao Paulo, Avenida Bandeirantes, 3900, CEP 14040-901 Ribeirao Preto, SP, Brasil, ²Faculdade de Filosofia, Ciencias e Letras de Ribeirao Preto, Universidade de Sao Paulo, Avenida Bandeirantes, 3900, CEP 14040-901 Ribeirau Preto, SP, Brasil¹Departamentos de Biologia e Quimica, Universidade de Sao Paulo, Avenida Bandeirantes, 3900, CEP 14040-901 Ribeirao Preto, SP, Brasil, ²Faculdade de Filosofia, Ciencias e Letras de Ribeirao Preto, Universidade de Sao Paulo, Avenida Bandeirantes, 3900, CEP 14040-901 Ribeirau Preto, SP, Brasil

Corresponding author: Joao Atilio Jorge , Tel: 55-16-3602-4679,

Received: 21 November 2008 • Accepted: 4 March 2009

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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 Rf. Temperature optimum of xylan-induced and xylose-induced beta-xylosidases was 45oC and 40oC, respectively, and 35oC 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 55oC 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.

Keywords: beta-xylosidase;xylobiase;glycosylation;deglycosylation;glycoprotein;Aspergillus versicolor

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Effect of Glycosylation on the Biochemical Properties of beta-Xylosidases from Aspergillus versicolor

J. Microbiol. 2009;47(3):270-276. Published online June 26, 2009

DOI: https://doi.org/10.1007/s12275-008-0286-9

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