Abstract
Three bioactive peptides, angiotensin-converting enzyme-inhibitory peptides (ACEIPs), casein phosphopeptides (CPPs) and antimicrobial peptides (AMPs), were simultaneously prepared from casein by pancreatic hydrolysis via an enzymatic membrane reactor (EMR) and combinational chromatography. The reaction was performed at 37°C and pH 8.0 for 3h followed by ultrafiltration. ACEIPs were purified by size exclusion chromatography (SEC) from permeate fractions with molecular weight (MW) below 1kDa. Concurrently, strong cation exchange high-performance liquid chromatography (SCE-HPLC) was used to isolate CPPs and AMPs from retentate fractions ranging from 1kDa and 5kDa. Following reverse-phase high performance liquid chromatography–electrospray ionization tandem mass spectrometry (RP-HPLC–ESI-MS/MS) analysis, potential ACEIPs and a total of 34 CPPs were identified (18 corresponded to αs1-casein, 2 to αs2-casein, 10 to β-casein and 4 to κ-casein). Additionally, the ACEIPs in fraction B from SEC had the highest ACE-inhibiting-activity (73.5% in 1.0mg/ml), while total concentrations of AMPs were directly proportional to overall antibacterial activity. Uniquely, fraction 5 from SCE exhibited the highest activity against Staphylococcus aureus (97.49% in 1.0mg/ml).
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