Keratinolytic activity of Streptomyces sp isolated of poultry processing plant


Autoria(s): Oliveira, G. M.; Cortezi, M.; Contiero, Jonas; MendezVilas, A
Contribuinte(s)

Universidade Estadual Paulista (UNESP)

Data(s)

30/09/2013

20/05/2014

30/09/2013

20/05/2014

01/01/2009

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.

Formato

282-285

Identificador

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

http://hdl.handle.net/11449/20103

WOS:000268100200059

Idioma(s)

eng

Publicador

World Scientific Publ Co Pte Ltd

Relação

Current Research Topics In Applied Microbiology and Microbial Biotechnology

Direitos

closedAccess

Palavras-Chave #Keratinase #Streptomyces sp #pH #temperature #amino acids
Tipo

info:eu-repo/semantics/conferencePaper