Optimization of culture conditions and properties of immobilized sulfide oxidase from Arthrobacter species.
J Biotechnol
; 124(3): 523-31, 2006 Jul 25.
Article
em En
| MEDLINE
| ID: mdl-16530872
ABSTRACT
Arthrobacter species strain FR-3, isolated from sediments of a swamp, produced a novel serine-type sulfide oxidase. The production of sulfide oxidase was maximal at pH 7.5 and 30 degrees C. Among various carbon and nitrogen sources tested, glucose and yeast extract were found to be the most effective substrates for the secretion of sulfide oxidase. The sulfide oxidase was purified to homogeneity and the molecular weight of the purified enzyme was 43 kDa when estimated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The purified sulfide oxidase can be effectively immobilized in DEAE (diethylaminoethyl)-cellulose matrix with a yield of 66%. The purified free and immobilized enzyme had optimum activity at pH 7.5 and 6.0, respectively. Immobilization increases the stability of the enzyme with respect to temperature. The half-life of the immobilized enzyme was 30 min at 45 degrees C, longer than that of the free enzyme (10 min). The purified free sulfide oxidase activity was completely inhibited by 1 mM Co2+ and Zn2+ and sulfhydryl group reagents (para-chloromercuribenzoic acid and iodoacetic acid). Catalytic activity was not affected by 1 mM Ca2+, Mg2+, Na+ and metal-chelating agent (EDTA).
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Arthrobacter
/
Técnicas de Cultura de Células
/
Reatores Biológicos
/
Oxirredutases atuantes sobre Doadores de Grupo Enxofre
Idioma:
En
Revista:
J Biotechnol
Ano de publicação:
2006
Tipo de documento:
Article