Keratinolytic activity of Streptomyces sp isolated of poultry processing plant

Nenhuma Miniatura disponível

Data

2009-01-01

Autores

Oliveira, G. M. [UNESP]
Cortezi, M. [UNESP]
Contiero, Jonas [UNESP]

Título da Revista

ISSN da Revista

Título de Volume

Editor

World Scientific Publ Co Pte Ltd

Resumo

The keratin is not degraded by common enzyme, keratinases have the ability to degrade native keratin and others insoluble enzymes. In the present work was Studied keratinase produced by Streptomyces sp LMI-1 isolated from industrial plant of poultry processing. The enzyme degraded 87% of feathers after 120 h, it was stimulated by Ba(2+) and inhibited by Ca(2+), Mn(2+), EDTA and Hg(+). The optimum pH and temperature for the enzyme was 8.5 and 60 degrees C, respectively. The enzyme was stable after 2 hours at 50 degrees C. The culture broth analysis by thin layer chromatography showed presence of amino acids serine, methionine, proline, tyrosine and leucine after 72 hours of incubation. The microorganism showed potential for use in industrial process because of higher enzyme production and feathers degradation.

Descrição

Palavras-chave

Keratinase, Streptomyces sp, pH, temperature, amino acids

Como citar

Current Research Topics In Applied Microbiology and Microbial Biotechnology. Singapore: World Scientific Publ Co Pte Ltd, p. 282-285, 2009.