Journal
FOOD CHEMISTRY
Volume 245, Issue -, Pages 1169-1175Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.foodchem.2017.11.044
Keywords
Protease; Casein; Antibacterial activity; Bioactive peptides; Bivalve mollusk
Funding
- Conselho Nacional de Desenvolvimento Cientifico e Tecnologico (CNPq) [446902/2014-4]
- Coordenacao de Aperfeicoamento de Pessoal de Nivel Superior (CAPES) [AUXPE 1454/2013]
- Fundacao de Amparo a Ciencia e Tecnologia do Estado de Pernambuco (FACEPE) [APQ-0108-2.08/14, APQ-0661-2.08/15]
- CNPq
- FACEPE [BFP-0089-2.08/16]
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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 83.1 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 degrees C and stability in a wide pH range (3.0-9.0). K-m was 4.28 +/- 0.34 mM of the synthetic substrate N-benzoyl-DL-arginyl-rho-nitroanilide, whereas V-max was 0.056 +/- 0.001 nmol 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 mu g 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.
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