Purification and Partial characterization of manganese peroxidase from Bacillus pumilus AND Paenibacillus sp.

Brazilian Journal of Microbiology

Patrícia Lopes De Oliveira²  Marta Cristina Teixeira Duarte²  Alexandre Nunes Ponezi²  Lúcia Regina Durrant¹ 

[1] ,Universidade Estadual de Campinas Centro Pluridisciplinar de Pesquisas Químicas, Biológicas e Agrícolas Divisão de MicrobiologiaCampinas SP ,Brasil

关键词: Bacillus pumilus;    Paenibacillus sp.;    Manganese peroxidase;    Purification;    Characterization;   

DOI  :  10.1590/S1517-83822009000400012

来源: SciELO

【 摘 要 】

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.

【 授权许可】

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