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Your search keyword '"Denise Bello Magalhães"' showing total 2 results
Start Over Author "Denise Bello Magalhães" Topic chromatography
2 results on '"Denise Bello Magalhães"'

1. Colorimetric assay for lignin peroxidase activity determination using methylene blue as substrate

Author

Elba P. S. Bon, Denise Bello Magalhães, Maria Eleonora Andrade de Carvalho, S. H. Kling, and Julio Silva Araujo Neto

Subjects
chemistry.chemical_classification, Chromatography, biology, fungi, food and beverages, Substrate (chemistry), Applied Microbiology and Biotechnology, Biochemistry, Colorimetry (chemical method), chemistry.chemical_compound, Enzyme, chemistry, MBAS assay, biology.protein, Organic chemistry, Quantitative analysis (chemistry), Methylene blue, Demethylation, Peroxidase
Abstract

A colorimetric method for determination of lignin peroxidase activity has been developed which is based on the demethylation of methylene blue. The use of this dye shows the practical advantage of using a wavelength in the visible region of spectrum. The method can be efficiently used for the enzyme quantification as its sensitivity is close to the veratryl alcohol assay.

Published
1996

2. Immobilization of β glucosidase aggregates in calcium alginate

Author

Maria Helena M. Rocha-Leão and Denise Bello Magalhães

Subjects
chemistry.chemical_classification, Chromatography, Calcium alginate, Immobilized enzyme, biology, Renewable Energy, Sustainability and the Environment, Aspergillus niger, Half-life, Forestry, biology.organism_classification, Catalysis, chemistry.chemical_compound, Enzyme, chemistry, Thermal stability, Bifunctional, Waste Management and Disposal, Agronomy and Crop Science
Abstract

A commercial preparation of β glucosidase obtained from Aspergillus niger was immobilized in calcium alginate, after enzyme crosslinking with a bifunctional agent, which increases its molecular size with the formation of enzymatic aggregates. The immobilized enzyme exhibited changes of activity profiles related to temperature and pH, in comparison to the free enzyme. However, there was no shift in optimum pH and temperature upon immobilization. The catalyst showed an improved thermal stability when compared with the free enzyme, yielding a half-life of 23 days, at 50°C. The free enzyme exhibited a 9-day half life, determined at the same temperature.

Published
1991

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