Enhanced production and organic solvent stability of a protease fromBrevibacillus laterosporus strain PAP04
Braz. j. med. biol. res
;
49(4): e5178, 2016. graf
Artículo
en Inglés
| LILACS
| ID: biblio-951664
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.
Texto completo:
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Índice:
LILACS (Américas)
Asunto principal:
Compuestos Orgánicos
/
Péptido Hidrolasas
/
Proteínas Bacterianas
/
Brevibacillus
Límite:
Animales
Idioma:
Inglés
Revista:
Braz. j. med. biol. res
Asunto de la revista:
Biologia
/
Medicina
Año:
2016
Tipo del documento:
Artículo
País de afiliación:
Corea del Sur
Institución/País de afiliación:
Inha University/KR
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