Recent Progress in Enzymatic Release of Peptides in Foods of Animal Origin and Assessment of Bioactivity

Abstract

There is a wide variety of peptides released from food proteins which are able to exert a relevant benefit for human health like angiotensin-converting enzyme (ACE) inhibition, antioxidant, anti-inflammatory, hypoglucemic or antithrombotic activity, among others. This manuscript is reviewing the recent advances on enzymatic mechanisms for the hydrolysis of food proteins, including the types of enzymes and mechanisms of action involved, the strategies followed for the isolation and identification of bioactive peptides through advanced proteomic tools, the assessment of bioactivity and its beneficial effects. Specific applications in fermented and/or ripened foods where a significant number of bioactive peptides have been reported with relevant in vivo physiological effects on laboratory rats and humans, as well as the hydrolysis of food proteins for the production of bioactive peptides are also reviewed.

Ultrasound-assisted covalent reaction of myofibrillar protein: The improvement of functional properties and its potential mechanism

“…Myofibrillar proteins (MPs) have been widely studied in recent years due to their unique essential amino acid contents and superior biological digestibility [1] , [2] , [3] . Additionally, MPs have been considered as individualized building blocks in constructing gel or delivery systems that meet the requirements of health benefits and food quality for modern consumers [4] , [5] .…”

Inhibition of 3-hydroxy-3-methyl-glutaryl-coenzyme A reductase enzyme by dipeptides identified in dry-cured ham

“…Dry-cured hams are protein-rich foods, and due to the proteolytic process associated with the dry-curing stage, they may constitute a highly potential source of bioactive peptides (Kęska & Stadnik 2016. As a result of endogenous proteolytic enzyme activities, the length of the polypeptides is progressively reduced, leading to the generation of short peptides (Toldrá et al 2020) which are responsible of the final characteristics of the product, but also of its functional properties (Gallego et al, 2015, Gallego et al 2019b, Mora et al 2019. Regarding the biological activity, in vitro angiotensin I-converting enzyme (ACEI), dipeptidyl peptidase-IV (DPP-IV), αamylase and α-glucosidase inhibitory activities, antiinflammatory, antioxidant, and antilisterial activities have been reported (Castellano et al 2016;Gallego et al 2014;Gallego et al 2016;Gallego et al 2019a;Mora et al 2020).…”

“…The main limiting fact for peptides to exert beneficial effects is their susceptibility to a partial or total loss of activity as a result of food matrix interactions and further hydrolysis by digestive enzymes and intestinal microbiota. Finally, peptides must reach their target sites in an active form in significant quantity (Gallego et al 2016;Toldrá et al 2020). In this sense, dipeptides are of great therapeutic interest because they can be absorbed more efficiently in the intestinal tract (Bouglé & Bouhallab 2017;Guha & Majumder 2019) and arrive intact through the blood stream to the target sites of the organs where they could exert their functionalities.…”

Characterization of Umami Dry-Cured Ham-Derived Dipeptide Interaction with Metabotropic Glutamate Receptor (mGluR) by Molecular Docking Simulation

“…Dipeptides in dry-cured ham are mainly generated by dipeptidyl dipeptidases (DPPs) and by the progressive shortening of longer peptides by other endogenous enzymes. It has been shown that DPPs release dipeptides from the N-terminal of peptide fragments [45], and despite their substrate specificities, all of them are able to release other dipeptides at lower rates [46]. Short peptides are in the limit of some standard proteomic approaches due to their small sizes and signal inhibition, due to matrix interactions in the mass spectrometers [45,47,48].…”