Abstract
Bioactive peptides released from the enzymatic hydrolysis of food proteins are currently a trending topic in the scientific community. Their potential as antidiabetic agents, by regulating the glycemic index, and thus to be employed in food formulation, is one of the most important functions of these peptides. In this review, we aimed to summarize the whole process that must be considered when talking about including these molecules as a bioactive ingredient. In this regard, at first, the production, purification and identification of bioactive peptides is summed up. The detailed metabolic pathways described included carbohydrate hydrolases (glucosidase and amylase) and dipeptidyl-peptidase IV inhibition, due to their importance in the food-derived peptides research field. Then, their characterization, concerning bioavailability in vitro and in situ, stability and functionality in food matrices, and ultimately, the in vivo evidence (from invertebrate animals to humans), was described. The future applicability that these molecules have due to their biological potential as functional ingredients makes them an important field of research, which could help the world population avoid suffering from several diseases, such as diabetes.
Highlights
IntroductionProteins are one of the main components of human diets. These biomacromolecules are formed by the association of amino acids, through the peptidic bond between the amino group of one amino acid and the carboxyl group from the following amino acid in the chain [1]
The technological property modification of protein hydrolysates, compared to the intact protein, is an advantage related to their use in functional feeding, because it mainly involves the facilitation of the formulation of the food
What is remarkable is the importance of amino acids containing a hydroxyl or basic side chain at the N-terminal, and of proline within the chain and alanine or methionine at the C-terminal
Summary
Proteins are one of the main components of human diets. These biomacromolecules are formed by the association of amino acids, through the peptidic bond between the amino group of one amino acid and the carboxyl group from the following amino acid in the chain [1]. The technological property modification of protein hydrolysates, compared to the intact protein, is an advantage related to their use in functional feeding, because it mainly involves the facilitation of the formulation of the food This improvement is due to the exposition of the residues of different amino acids. Focusing on the bioactivities those peptides can exert, their antioxidant, antihypertensive and antidiabetic (glycemic index regulation) activities are the most remarkable because of the diseases they would prevent, which are some of the most prevalent worldwide nowadays (cardiovascular disease, diabetes, hypertension) Recent studies, both in vitro and in vivo, show the functionality of these protein hydrolysates. We will focus on glycemic index-regulating peptides, that is, antidiabetic peptides
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