Purification and characterization of an alpha-galactosidase from Aspergillus fumigatus

Purification and characterization of an alpha-galactosidase from Aspergillus fumigatus

Aspergillus fumigatus secreted invertase (beta-fructofuranosidase) and alpha-galactosidase enzymatic activities able to hydrolyzing raffinose oligosaccharides (RO). alpha-Galactosidase was induced by galactose, melibiose and raffinose, but galactose was the most efficient inducer. It was purified by gel filtration and two ion exchange chromatographies and showed Mw of 54.7 kDa. The purified enzyme showed maximal activity against p-nitrophenyl-alpha-D-galactopyranoside (pNPGal) at pH 4.5-5.5 and 55 °C, and retained about 80% of the original activity after incubation for 90 minutes at 50ºC. The KM for pNPGal was 0.3 mM. Melibiose was hydrolyzed by the enzyme but raffinose was very poor substrate.

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Main Authors: Rezende,Sebastião Tavares de, Guimarães,Valéria Monteze, Rodrigues,Marília de Castro, Felix,Carlos Roberto
Format: Digital revista
Language:English
Published: Instituto de Tecnologia do Paraná - Tecpar 2005
Online Access:http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132005000200005
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spelling oai:scielo:S1516-891320050002000052005-04-26Purification and characterization of an alpha-galactosidase from Aspergillus fumigatusRezende,Sebastião Tavares deGuimarães,Valéria MontezeRodrigues,Marília de CastroFelix,Carlos Roberto Aspergillus fumigatus alpha-galactosidase raffinose oligosaccharides Aspergillus fumigatus secreted invertase (beta-fructofuranosidase) and alpha-galactosidase enzymatic activities able to hydrolyzing raffinose oligosaccharides (RO). alpha-Galactosidase was induced by galactose, melibiose and raffinose, but galactose was the most efficient inducer. It was purified by gel filtration and two ion exchange chromatographies and showed Mw of 54.7 kDa. The purified enzyme showed maximal activity against p-nitrophenyl-alpha-D-galactopyranoside (pNPGal) at pH 4.5-5.5 and 55 °C, and retained about 80% of the original activity after incubation for 90 minutes at 50ºC. The KM for pNPGal was 0.3 mM. Melibiose was hydrolyzed by the enzyme but raffinose was very poor substrate.info:eu-repo/semantics/openAccessInstituto de Tecnologia do Paraná - TecparBrazilian Archives of Biology and Technology v.48 n.2 20052005-03-01info:eu-repo/semantics/articletext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132005000200005en10.1590/S1516-89132005000200005
institution SCIELO
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country Brasil
countrycode BR
component Revista
access En linea
databasecode rev-scielo-br
tag revista
region America del Sur
libraryname SciELO
language English
format Digital
author Rezende,Sebastião Tavares de
Guimarães,Valéria Monteze
Rodrigues,Marília de Castro
Felix,Carlos Roberto
spellingShingle Rezende,Sebastião Tavares de
Guimarães,Valéria Monteze
Rodrigues,Marília de Castro
Felix,Carlos Roberto
Purification and characterization of an alpha-galactosidase from Aspergillus fumigatus
author_facet Rezende,Sebastião Tavares de
Guimarães,Valéria Monteze
Rodrigues,Marília de Castro
Felix,Carlos Roberto
author_sort Rezende,Sebastião Tavares de
title Purification and characterization of an alpha-galactosidase from Aspergillus fumigatus
title_short Purification and characterization of an alpha-galactosidase from Aspergillus fumigatus
title_full Purification and characterization of an alpha-galactosidase from Aspergillus fumigatus
title_fullStr Purification and characterization of an alpha-galactosidase from Aspergillus fumigatus
title_full_unstemmed Purification and characterization of an alpha-galactosidase from Aspergillus fumigatus
title_sort purification and characterization of an alpha-galactosidase from aspergillus fumigatus
description Aspergillus fumigatus secreted invertase (beta-fructofuranosidase) and alpha-galactosidase enzymatic activities able to hydrolyzing raffinose oligosaccharides (RO). alpha-Galactosidase was induced by galactose, melibiose and raffinose, but galactose was the most efficient inducer. It was purified by gel filtration and two ion exchange chromatographies and showed Mw of 54.7 kDa. The purified enzyme showed maximal activity against p-nitrophenyl-alpha-D-galactopyranoside (pNPGal) at pH 4.5-5.5 and 55 °C, and retained about 80% of the original activity after incubation for 90 minutes at 50ºC. The KM for pNPGal was 0.3 mM. Melibiose was hydrolyzed by the enzyme but raffinose was very poor substrate.
publisher Instituto de Tecnologia do Paraná - Tecpar
publishDate 2005
url http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132005000200005
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