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Trypsin specifically cleaves peptide bonds at the carboxyl side of the amino acids lysine and arginine, making it highly effective in breaking down proteins into smaller peptides. This specificity is due to the structure of its active site, which accommodates these positively charged amino acids. The enzyme operates optimally at a slightly alkaline pH, which is consistent with the pH environment of the small intestine.
In addition to its digestive function, trypsin has significant applications in biotechnology and research. It is commonly used in cell culture to dissociate adherent cells from surfaces, a process known as trypsinization. Furthermore, trypsin is employed in proteomics for protein digestion prior to mass spectrometry analysis, enabling the identification and characterization of proteins.