Much attention is paid to the study of biologically active peptides from milk caseins, which are usually obtained by partial hydrolysis by the proteolytic system of lactic acid bacteria. These peptides have a wide range of beneficial properties, including mineral binding, antidiabetic, satiating, immunomodulating, opioid, antimicrobial and antioxidant properties. In this work, we investigated the antimicrobial and antioxidant activity of peptides obtained during the hydrolysis of milk caseins by Enterococcus faecalis AN1 proteases. SDS PAAG electrophoretic analysis of peptide fractions after 8 hours of milk casein proteolysis showed that proteases of this strain cleave all casein fractions (αs1-, αs2 and β-casein). RP-HPLC profile elution revealed a large amount of small, medium and long cationic and anionic peptides. Some fractions of these peptides have antimicrobial activity against Listeria monocytogenes EGDe 107776, Bacillus cereus, Escherichia coli CCM 4517 and Aspergillus niger CCM 8189. Peptide fractions obtained during the hydrolysis of caseins possessed strong antioxidant activity and surpassed native casein by 4.5 times. These data stimulate further research in the field of biomedicine and food technology with the aim of developing new and effective preparations and products for maintaining the health and safety of consumers.
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