Antioxidant, angiotensin-converting enzyme, and α-amylase inhibitory activities of protein hydrolysates of Leucaena leucocephala seeds
Iván Balderas-León | Diana Baigts-Allende | Anaberta Cardador-Martínez
The Leucaena leucocephala seeds (LLS) cotyledon proteins, globulins, and glutelins were independently hydrolyzed by Alcalase, Trypsin, and α-Chymotrypsin up to 180 min. The degree of hydrolysis (DH), antioxidant, ACE-inhibitory, and α-Amylase inhibition were assessed. The higher DH values were 76.75% and 82.71% for globulin α-Chymotrypsin, and glutelin Alcalase hydrolysates, respectively. The glutelin hydrolyzed with Trypsin showed the higher DPPH• antioxidant activity while the higher ABTS antioxidant activity was for globulin Alcalase hydrolysate after 180 min digestion. The highest ACE-inhibitory activity was 95.44% for globulin-Alcalase hydrolysate at 180 min; while, for the α-Amylase inhibition assay, glutelin-Alcalase showed the highest values at 100 min of reaction. LLS cotyledon protein concentrates and hydrolysates with relatively low mimosine content were obtained after protein extraction. Such findings indicate the possibility of getting bioactive peptides from LLS cotyledon proteins using enzyme digestions and might be utilized for functional foods with physiological enhancer effects.
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