Purification and characterization of a protease from the visceral mass of Mytella charruana and its evaluation to obtain antimicrobial peptides.
Food Chem
; 245: 1169-1175, 2018 Apr 15.
Article
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| MEDLINE
| ID: mdl-29287337
ABSTRACT
This work describes purification of a protease from the visceral mass of the mussel Mytella charruana as well as evaluation of its ability to hydrolyze milk casein to generate antimicrobial peptides. The enzyme showed pI of 4.1 and a single polypeptide band of 83.1â¯kDa after SDS-PAGE. Sequence similarities with tropomyosin and myosin from mollusks were detected. The protease showed a trypsin-like activity with optimal temperature of 40⯰C and stability in a wide pH range (3.0-9.0). Km was 4.28⯱â¯0.34â¯mM of the synthetic substrate N-benzoyl-dl-arginyl-ρ-nitroanilide, whereas Vmax was 0.056⯱â¯0.001â¯nmolâ¯min-1. The enzyme hydrolyzed casein, and the hydrolysate inhibited the growth of Escherichia coli, Micrococcus luteus, Bacillus subtilis, and Klebsiella pneumoniae at a minimal inhibitory concentration of 5.0⯵gâ¯mL-1. In conclusion, the visceral mass of M. charruana contains a trypsin-like protease that can generate peptides from casein that have a bacteriostatic effect.
Palabras clave
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Péptidos
/
Serina Endopeptidasas
/
Bivalvos
/
Antibacterianos
/
Antifúngicos
Límite:
Animals
Idioma:
En
Revista:
Food Chem
Año:
2018
Tipo del documento:
Article
País de afiliación:
Brasil