- Biochemical Properties of an Extracellular Trehalase from Malbranchea pulchella var. Sulfurea
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Marita Gimenez Pereira , Luis Henrique Souza Guimarães , Rosa Prazeres Melo Furriel , Maria de Lourdes , Teixeira de Moraes Polizeli , Hector Francisco Terenzi , João Atílio Jorge
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J. Microbiol. 2011;49(5):809-815. Published online November 9, 2011
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DOI: https://doi.org/10.1007/s12275-011-0532-4
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The thermophilic fungus Malbranchea pulchella var. sulfurea produced good amounts of extracellular trehalase activity when grown for long periods on starch, maltose or glucose as the main carbon source. Studies with young cultures suggested that the main role of the extracellular acid trehalase is utilizing trehalose as a carbon source. The specific activity of the purified enzyme in the presence of manganese (680 U/mg protein) was comparable to that of other thermophilic fungi enzymes, but many times higher than the values reported for trehalases from other microbial sources. The apparent molecular mass of the native enzyme was estimated to be 104 kDa by gel filtration and 52 kDa by SDS-PAGE, suggesting that the enzyme was composed by two subunits. The carbohydrate content of the purified enzyme was estimated to be 19% and the pI was 3.5. The optimum pH and temperature were 5.0-5.5 and 55°C, respectively. The purified enzyme was stimulated by manganese and inhibited by calcium ions, and insensitive to ATP and ADP, and 1 mM silver ions. The apparent KM values for trehalose hydrolysis by the purified enzyme in the absence and presence of manganese chloride were 2.70±0.29 and 2.58±0.13 mM, respectively. Manganese ions affected only the apparent Vmax, increasing the catalytic efficiency value by 9.2-fold. The results reported herein indicate that Malbranchea pulchella produces a trehalase with mixed biochemical properties, different from the conventional acid and neutral enzymes and also from trehalases from other thermophilic fungi.
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Citations
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- Effect of Glycosylation on the Biochemical Properties of beta-Xylosidases from Aspergillus versicolor
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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
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J. Microbiol. 2009;47(3):270-276. Published online June 26, 2009
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DOI: https://doi.org/10.1007/s12275-008-0286-9
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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.
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