Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/92980
Type: Artigo de periódico
Title: Purification And Partial Characterization Of Manganese Peroxidase From Bacillus Pumilus And Paenibacillus Sp
Author: de Oliveira P.L.
Duarte M.C.T.
Ponezi A.N.
Durrant L.R.
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 °C to 60 °C, 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°C and 11.74 U/L at pH 9.0 and 35°C, 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.
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Rights: aberto
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Address: http://www.scopus.com/inward/record.url?eid=2-s2.0-70350157122&partnerID=40&md5=58ba5bd2b8d3499f96fa6e32688c52cf
Date Issue: 2009
Appears in Collections:Unicamp - Artigos e Outros Documentos

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