Optimization of the Enzymatic Hydrolysis of Lupin (Lupinus) Proteins for Producing ACE-Inhibitory Peptides.
Recently, the enzymatic hydrolysis of Lupinus albus and Lupinus angustifolius proteins with pepsin was showed to produce peptides able to inhibit the angiotensin-converting enzyme (ACE). The objective of the present work was to test different hydrolytic enzymes and to investigate three lupin species (L. albus, L. angustifolius, Lupinus luteus) with the final goal of selecting the best enzyme/species combination for an efficient production of ACE-inhibitory peptide mixtures. Pepsin gave peptides with the best IC50 values (mean value on three species 186 ± 10 μg/mL), followed by pepsin + trypsin (198 ± 16 μg/mL), chymotrypsin (213 ± 83 μg/mL), trypsin (405 ± 54 μg/mL), corolase PP (497 ± 32 μg/mL), umamizyme (865 ± 230 μg/mL), and flavourzyme (922 ± 91 μg/mL). The three species showed similar activity scales, but after pepsin + trypsin and chymotrypsin treatments, L. luteus peptide mixtures resulted to be significantly the most active. This investigation indicates that lupin proteins may be a valuable source of ACE-inhibitory peptides, which may explain the activity observed in experimental and clinical studies and foresee the application of lupin proteins into functional foods or dietary supplements.
Department of Pharmaceutical Sciences, University of Milan , via Mangiagalli 25, 20133 Milano, Italy.
Giovanna
G
Boschin
Graziana Maria
GM
Scigliuolo
Donatella
D
Resta
Anna
A
Arnoldi
D000806:Angiotensin-Converting Enzyme Inhibitors / Q000737:chemistry* / Q000302:isolation & purification; D001671:Biochemistry / Q000379:methods*; D006868:Hydrolysis; D031297:Lupinus / Q000737:chemistry*; D010447:Peptide Hydrolases / Q000737:chemistry*; D010455:Peptides / Q000737:chemistry* / Q000302:isolation & purification; D010940:Plant Proteins / Q000737:chemistry*
D000806:Angiotensin-Converting Enzyme Inhibitors; D010455:Peptides; D010940:Plant Proteins; D010447:Peptide Hydrolases