In silico determination of physicochemical properties of Lactoferrin peptides isolated from Equine milk

Whey protein contains low-molecular-weight bioactive peptides with various medicinal properties, such as anti-inflammatory, antioxidant, and antimicrobial effects. The presence of these low-molecular-weight peptide molecules plays a significant role in promoting health through food. For peptides to function as effective food ingredients, they must be digested and absorbed. Current research includes information on 56 peptides from the most active fractions of lactoferrin (LF) isolated from equine milk hydrolysate. The potential bioactivity, including allergenicity, toxicity, and physicochemical properties, as well as the applicability of these peptides, was determined using the Peptide Ranker online database (http://distilldeep.ucd.ie/PeptideRanker/). The studied peptides were classified as cationic (13), anionic (23), and neutral (20). The findings revealed that only the cationic and neutral peptides demonstrated significant biological activity (>0.75). Furthermore, peptide bioactivity was positively correlated with phenylalanine content. These research findings can significantly contribute to the MS-based proteomics of equine milk LF and shed light on the composition of its bioactive peptides. Further research is required to comprehensively investigate the biochemical nature and pathways of bioactive peptides responsible for the antimicrobial and antioxidant properties of LF from equine milk.

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