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The trypsin inhibitor is the substance that prevents the trypsin enzyme from breaking the protein and therefore reduces the enzyme efficiency.It is found in certain food and can also be produced by the human, bovine pancreas.

TheX-ray study made by Robert Huber while studying the complex between bovine pancreatic trypsin inhibitor (BPTI) and trypsin gave the most convincing structural evidence for the existence of the tetrahedral intermediate.The trypsin active site area and the 58-residue BPTI bind together to create a complex with a closely packed interface and a web of hydrogen-bonded cross-links. Any trypsin that is prematurely activated in the pancreas is prevented from digesting that organ by this contact. The significance of BPTI for physiological processes is shown by the complex's 10¹³M^-1 association constant, which is among the greatest of any known protein-protein interaction.

Hence,bovine trypsin inhibitors revealthe existence of a tetrahedral intermediateabout trypsin's catalytic mechanism.