Data/hora: 12/06/2024 15:33:48

Provedor de dados: | 58
País: | Brazil
Título: | Purification and Partial characterization of manganese peroxidase from Bacillus pumilus AND Paenibacillus sp.
Autores: | Oliveira,Patrícia Lopes de; Duarte,Marta Cristina Teixeira; Ponezi,Alexandre Nunes; Durrant,Lúcia Regina.
Data: | 2009-12-01
Ano: | 2009
Palavras-chave: | Bacillus pumilus; Paenibacillus sp.; Manganese peroxidase; Purification; Characterization.
Resumo: | 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.
Tipo: | Info:eu-repo/semantics/article
Idioma: | Inglês
Identificador: | http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822009000400012
Editor: | Sociedade Brasileira de Microbiologia
Relação: | 10.1590/S1517-83822009000400012
Formato: | text/html
Fonte: | Brazilian Journal of Microbiology  v.40 n.4 2009
Fonte: | info:eu-repo/semantics/openAccess