A comparison of micellar casein and β‐casein as sources of basic peptides through tryptic hydrolysis and their enrichment using two‐stage ultrafiltration

For the application of functional peptides in innovative products, these peptides have to be individually available. This may be accomplished by a well‐considered combination of a pure protein precursor, a selective cleaving enzyme, and an advanced separation technology. In this proof‐of‐principle approach, micellar casein and β‐casein were subjected to tryptic hydrolysis and the generated casein peptides were identified and characterised. The basic target peptides, β‐casein f(177‐183) and β‐casein f(170‐176), were then enriched. A permeate containing 35% of the target peptides was produced after two‐stage ultrafiltration of micellar casein tryptic hydrolysate. In comparison, enrichment up to 58% was achieved starting from β‐casein tryptic hydrolysate.