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Bioactive peptide production is a biological and industrial process involving the generation of short, physiologically active amino acid sequences (typically 2–20 residues) from larger precursor proteins [1, 13]. In the body, this process is essential for the biogenesis of hormones, neuropeptides, and cytokines through the coordinated action of enzymes like proprotein convertases, carboxypeptidases, and Peptidyl-glycine alpha-amidating monooxygenase (PAM) [3, 12]. In the pharmaceutical and nutraceutical industries, it refers to the use of enzymatic hydrolysis or microbial fermentation to release 'encrypted' peptides from dietary proteins (such as milk, soy, or marine sources) that exhibit antihypertensive, antioxidant, or antimicrobial properties [4, 5]. While not a single molecular target, the machinery and enzymes responsible for bioactive peptide production are significant areas of therapeutic focus for metabolic and cardiovascular diseases [1, 15].
Modulation of proteolytic cleavage of precursor proteins by proprotein convertases or exogenous proteases to release physiologically active peptide fragments.
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