Identification and characterization of cholesterol esterase and lipase inhibitory peptides from amaranth protein hydrolysates

Abstract

Human diet is undergoing a shift towards plant-based diet as a sustainable source of protein compared to animal-derived protein. In this study, cholesterol esterase (CEase) and pancreatic lipase (PL) inhibitory activities of amaranth protein hydrolysates (APHs) were studied. Bromelain, chymotrypsin, and actinase E were used for generating APHs at 2, 4 & 6 h of hydrolysis. Higher PL inhibiting potential were observed in bromelain-derived APHs (IC50 = 0.38–0.66 mg/mL) in comparison to intact amaranth proteins (IC50 = 3.93 mg/mL). Bromelain-4 h hydrolysates (AB4) demonstrated significant inhibitory potential for both CEase (IC50 = 0.47 mg/mL) and PL (IC50 = 0.48 mg/mL) activity. Peptide identification in AB-4 hydrolysate revealed that among 17 bioactive peptides, three peptides (FPFPPTLGY, FGAPR, and FPFVPAPT) were predicted as potential PL inhibitors and only one peptide (FPFVPAPT) was predicted as CEase inhibitor based on the number of substrate binding sites on active site of the enzymes. This is the first study providing insights into amaranth protein derived bioactive peptide possessing CEase and LIP inhibitory potential.

Keywords

• Amaranth hydrolysates
• Bioactive peptides
• Pancreatic lipase
• Cholesterol esterase
• HPLC