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Studies on the Pycnoporus sanguineus CCT-4518 laccase purified by hydrophobic interaction chromatography.
Garcia, Telma Alves; Santiago, Mariângela Fontes; Ulhoa, Cirano José.
Afiliação
  • Garcia TA; Faculdade de Farmácia, Universidade Federal de Goiás, 74001-970, Goiânia, GO, Brazil.
Appl Microbiol Biotechnol ; 75(2): 311-8, 2007 May.
Article em En | MEDLINE | ID: mdl-17216440
A laccase from Pycnoporus sanguineus was purified by two steps using phenyl-Sepharose columm. A typical procedure provided 54.1-fold purification, with a yield of 8.37%, using syringaldazine as substrate. The molecular weight of the purified laccase was 69 and 68 kDa as estimated by 12% (w/v) SDS-PAGE gel and by gel filtration, respectively. The K (m) values for the substrates ABTS, syringaldazine, and guaiacol were 58, 8.3, and 370 muM, respectively. The enzyme's pH optimum for syringaldazine was 4.2 and optimal activity was 50 degrees C. The enzyme showed to be thermostable because when kept at 50 degrees C for 24 and 48 h it retained 93 and 76% activity. This laccase was inhibited by L: -cysteine, beta-mercaptoethanol, NaN(3), NaF, and HgCl(2).
Assuntos
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Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Polyporaceae / Cromatografia / Lacase / Interações Hidrofóbicas e Hidrofílicas Idioma: En Revista: Appl Microbiol Biotechnol Ano de publicação: 2007 Tipo de documento: Article País de afiliação: Brasil País de publicação: Alemanha
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Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Polyporaceae / Cromatografia / Lacase / Interações Hidrofóbicas e Hidrofílicas Idioma: En Revista: Appl Microbiol Biotechnol Ano de publicação: 2007 Tipo de documento: Article País de afiliação: Brasil País de publicação: Alemanha