Studies on the Pycnoporus sanguineus CCT-4518 laccase purified by hydrophobic interaction chromatography.
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).
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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