Enhanced production and organic solvent stability of a protease fromBrevibacillus laterosporus strain PAP04
Braz. j. med. biol. res
; 49(4): e5178, 2016. graf
Article
em En
| LILACS
| ID: biblio-951664
Biblioteca responsável:
BR1.1
ABSTRACT
A bacterial strain (PAP04) isolated from cattle farm soil was shown to produce an extracellular, solvent-stable protease. Sequence analysis using 16S rRNA showed that this strain was highly homologous (99%) to Brevibacillus laterosporus. Growth conditions that optimize protease production in this strain were determined as maltose (carbon source), skim milk (nitrogen source), pH 7.0, 40°C temperature, and 48 h incubation. Overall, conditions were optimized to yield a 5.91-fold higher production of protease compared to standard conditions. Furthermore, the stability of the enzyme in organic solvents was assessed by incubation for 2 weeks in solutions containing 50% concentration of various organic solvents. The enzyme retained activity in all tested solvents except ethanol; however, the protease activity was stimulated in benzene (74%) followed by acetone (63%) and chloroform (54.8%). In addition, the plate assay and zymography results also confirmed the stability of the PAP04 protease in various organic solvents. The organic solvent stability of this protease at high (50%) concentrations of solvents makes it an alternative catalyst for peptide synthesis in non-aqueous media.
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LILACS
Assunto principal:
Compostos Orgânicos
/
Peptídeo Hidrolases
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Proteínas de Bactérias
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Brevibacillus
Limite:
Animals
Idioma:
En
Revista:
Braz. j. med. biol. res
Assunto da revista:
BIOLOGIA
/
MEDICINA
Ano de publicação:
2016
Tipo de documento:
Article