- Trypsin is a pancreatic enzyme that specifically cleaves peptide bonds on the carboxyl side of basic amino acids, primarily arginine and lysine.
- This specificity is due to the structure of trypsin's active site, which contains a negatively charged aspartate residue that attracts and stabilizes the positively charged side chains of these basic amino acids.

To contrast:
- Chymotrypsin cleaves peptide bonds adjacent to aromatic amino acids such as phenylalanine, tyrosine, and tryptophan.
- Carboxypeptidase A is an exopeptidase that removes amino acids from the carboxyl terminus of proteins but prefers bulky hydrophobic residues rather than basic residues.
- Elastase cleaves peptide bonds adjacent to small, neutral amino acids like alanine.

Therefore, among the options, trypsin is the enzyme secreted by the pancreas that specifically targets peptide bonds next to basic amino acids.

Reference: Guyton and Hall Textbook of Medical Physiology, 14th Edition, Chapter 65: Pancreatic Secretion, Page 849