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Updated: Jan 8, 2026
Evaluation of Protein–Protein Interactions using an On-Membrane Digestion Technique
Published on: July 19, 2019
Identification, characterization and resistance to digestion assessment of hemp-derived dipeptidyl-peptidase IV
Miryam Amigo-Benavent1,2,3, Fernando Rivero-Pino4,5, Alvaro Villanueva-Lazo6
1Proteins and Peptides Research Group, Department of Biological Sciences, Faculty of Science and Engineering, University of Limerick, V94 T9PX Limerick, Ireland.
Abstract:
Hemp seeds (Cannabis sativa L.) are an adequate source of protein. Food-derived peptides exert bioactivity depending on the sequences. In this work, enzymatic hydrolysis with Alcalase (subtilisin) and Flavourzyme was carried out to obtain hemp protein hydrolysates with increased dipeptidyl-peptidase IV (DPP-IV) inhibitory activity. In addition, the hydrolysates were subjected to digestion following the INFOGEST protocol. The serial hydrolysis with both proteases showed the highest inhibition compared to the hydrolysis only with Alcalase. The peptides sequences contained in the samples and the digested samples were identified and characterized employing different bioinformatics tools. The sequences TNGPQLIH (released after addition of Flavourzyme), and GKLDLVKPQ (from Alcalase-treated samples) were proposed as the most active peptides. The peptides were chemically synthesized, and TNGPQLIH showed an IC50 value of 1.70 mg mL-1. The DPP-IV inhibitory activity was generally conserved or improved after digestion. These peptides could be employed as constituents in foods helping to prevent the development of diabetes.
