exoproteasas

Exoproteasas, also known as exopeptidases, are proteolytic enzymes that catalyze the hydrolysis of peptide bonds at the ends of protein or peptide substrates. They release single amino acids or dipeptides from either the N-terminus or the C-terminus of a chain, in contrast to endoproteases that cleave peptide bonds within the interior of the molecule. Exoproteases are typically categorized as aminopeptidases, which remove amino acids from the N-terminus, and carboxypeptidases, which remove residues from the C-terminus. Some enzymes also function as dipeptidyl peptidases, trimming dipeptides from the N-terminus.

Biological roles and distribution vary, but exoproteases generally participate in protein turnover, processing and maturation of signaling peptides and hormones, antigen processing, and nutrient acquisition. They are produced by a wide range of organisms, including bacteria, fungi, plants, and animals, and may be intracellular, membrane-associated, or secreted into the extracellular environment. Many exopeptidases are metal-dependent or serine proteases, with activity influenced by pH and the presence of cofactors or inhibitors.

Applications and relevance span several fields. In food and biotech industries, exoproteases help modify protein hydrolysates, debittering peptides, and tenderizing proteins, as well as enabling controlled production of small peptides and amino acids. In research and diagnostics, they are used to generate defined peptide fragments for sequencing, proteomics, and peptide synthesis workflows. Regulation of exoprotease activity occurs through gene expression, localization within cellular compartments, and inhibition by specific molecules.

Overall, exoproteasas constitute a diverse and essential class of proteases with important physiological roles and broad industrial utility.