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Exploration of Potentially Bioactive Peptides Generated from the Enzymatic Hydrolysis of Hempseed Proteins

Aiello, Gilda, Lammi, Carmen, Boschin, Giovanna, Zanoni, Chiara, Arnoldi, Anna
Journal of agricultural and food chemistry 2017 v.65 no.47 pp. 10174-10184
active sites, antioxidant activity, dipeptidyl-peptidase IV, enzymatic hydrolysis, enzyme activity, functional foods, glucose, hemp, hydrolysates, pancreatin, pepsin, peptides, peptidyl-dipeptidase A, protein concentrates, protein sources, trypsin
The seed of industrial hemp is an underexploited protein source. In view of a possible use in functional foods, a hempseed protein concentrate was hydrolyzed with pepsin, trypsin, pancreatin, or a mixture of these enzymes. A detailed peptidomic analysis using data-dependent acquisition showed that the numbers of peptides identified ranged from 90 belonging to 33 parent proteins in the peptic hydrolysate to 9 belonging to 6 proteins in the pancreatin digest. The peptic and tryptic hydrolysates resulted to be the most efficient inhibitors of 3-hydroxymethyl-coenzyme A reductase activity when tested on the catalytic domain of the enzyme. Using the open access tools PeptideRanker and BIOPEP, a list of potentially bioactive peptides was generated: the alleged activities included the antioxidant property, the glucose uptake stimulating activity, the inhibition of dipeptidyl peptidase-IV and angiotensin-converting enzyme I.