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

J Agric Food Chem. 2017 Nov 29;65(47):10174-10184. doi: 10.1021/acs.jafc.7b03590. Epub 2017 Nov 14.

Abstract

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.

Keywords: Cannabis sativa; HMGCoAR; LC−MS/MS; bioactive peptides; hempseed hydrolysates; peptidomics.

MeSH terms

  • Angiotensin-Converting Enzyme Inhibitors / chemistry
  • Antioxidants / chemistry
  • Cannabis / chemistry*
  • Dipeptidyl-Peptidase IV Inhibitors / chemistry
  • Hydrolysis
  • Pancreatin / chemistry
  • Pepsin A / chemistry
  • Peptides / chemistry*
  • Plant Proteins / chemistry*
  • Seeds / chemistry*

Substances

  • Angiotensin-Converting Enzyme Inhibitors
  • Antioxidants
  • Dipeptidyl-Peptidase IV Inhibitors
  • Peptides
  • Plant Proteins
  • Pancreatin
  • Pepsin A