Theaflavins inhibit pancreatic lipase (PL) at physiological concentrations.
Theaflavin-3,3′-digallate (TFdiG) is the most potent inhibitor.
TFdiG inhibits PL in a non-competitive manner with regard to substrate.
An in silico model predicts that TFdiG binds adjacent to the PL active site.
The model predicts that TFdiG perturbs His264, the key catalytic amino acid.