Author(s): ARRUDA, M. S.; SILVA, F. O.; EGITO, A. S. do; SILVA, T. M. S.; LIMA FILHO, J. L.; PORTO, A. L. F.; MOREIRA, K. A.

Summary: Abstract: The casein and its hydrolysates have many desirable functional properties, so there is great interest in its use in food and pharmaceutical industries. The hydrolysis of casein by a new protease obtained from latex Jacaratia corumbensis was performed to obtain antimicrobial peptides. Four proteins were visualized by electrophoresis of the enzyme extract of J. corumbensis, a band of molecular weight of approximately 30 kDa with the presence of other bands of low density. The fractions as-CN, b-CN and k-CN, were subjected to hydrolysis for a period of 1 min 24 h, where aliquots were collected and analyzed by SDS-PAGE to the characterization of peptides. The hydrolysates were evaluated for antimicrobial activity by determining the Minimum Inhibitory Concentration (MIC). The hydrolysates obtained at time of 2 h showed antimicrobial activity against microorganisms Enterococcus faecalis, Bacillus subtilis, Escherichia coli, Pseudomonas aeruginosa, Klebsiella pneumoniae and Staphylococcus aureus, indicating that the peptides obtained by hydrolysis of bovine casein by latex extract J. corumbensis showed activity antimicrobial. This fraction was subjected to reverse phase chromatography for puri?cation of peptides and subsequent mass spectrometric evaluation. The peptides were sequenced and evaluated for their antimicrobial potential.

Publication year: 2012

Types of publication: Journal article

Unit: Embrapa Goats & Sheep

Keywords: Antimicrobial peptides, Antimicrobial properties, Bovino, Casein, Caseinates, Caseína, Hidrólise, Hydrolyzed proteins, Jacaratia corumbensis, Latex, Leite, Milk, Protease