Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/27548
Type: Artigo de periódico
Title: Purification and Partial characterization of manganese peroxidase from Bacillus pumilus AND Paenibacillus sp.
Author: Oliveira, Patrícia Lopes de
Duarte, Marta Cristina Teixeira
Ponezi, Alexandre Nunes
Durrant, Lúcia Regina
Abstract: The production of manganese peroxidase (MnP) from Bacillus pumilus and Paenibacillus sp. was studied under absence and presence of the inducers indulin AT, guayacol, veratryl alcohol, lignosulfonic acid and lignosulfonic acid desulfonated. Indulin AT increased the activity of B. pumilus MnP up to 31.66 U/L after 8 h, but no improve was observed for Paenibacillus sp., which reached maximum activity (12.22 U/L) after 20 h. Both MnPs produced by these microorganisms were purified in phenyl sepharose resin and the proteins from crude extracts were eluted in two fractions. However, only the first fraction of each extract exhibited MnP activities. Tests in different pH and temperature values, from pH 5.0 to pH 10.0 and 30 ºC to 60 ºC, respectively, were carried out with the purified MnP. The maximum activity reached for B. pumilus and Paenibacillus sp. MnPs were 4.3 U/L at pH 8.0 and 25 ºC and 11.74 U/L at pH 9.0 and 35 ºC, respectively. The molar masses determined by SDS-PAGE gel eletrophoresis were 25 kDa and 40 kDa, respectively, for the purified enzyme from B. pumilus and Paenibacillus sp.
Subject: Bacillus pumilus
Paenibacillus sp.
Manganese peroxidase
Purification
Characterization
Editor: Sociedade Brasileira de Microbiologia
Rights: aberto
Identifier DOI: 10.1590/S1517-83822009000400012
Address: http://dx.doi.org/10.1590/S1517-83822009000400012
http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822009000400012
Date Issue: 1-Dec-2009
Appears in Collections:Unicamp - Artigos e Outros Documentos

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