2 published verifications about Pancreatic Lipase Pancreatic Lipase ×
“When the environment pH decreases from 9 to 8, some amino acid residues in pancreatic lipase bind slightly more hydrogen ions, causing a small charge change that alters the active site's shape or binding affinity and slightly reduces the enzyme's efficiency at binding fat.”
The evidence does not support the claim that lowering pH from 9 to 8 makes pancreatic lipase bind fat less efficiently. General biochemistry does show that pH can change residue protonation and enzyme shape, but pancreatic lipase is commonly reported to work best around pH 8 or within about 7.5–8.5. That means the specific directional conclusion is unsupported and may be the reverse of what the evidence suggests.
“When the environmental pH becomes more acidic, certain amino acid residues in pancreatic lipase bind additional hydrogen ions, causing small charge changes that alter the enzyme's active site shape or binding properties and slightly reduce its efficiency at binding fats.”
The described mechanism is well supported: lower pH can protonate pancreatic lipase residues, alter charge interactions, and change active-site or interface-binding behavior in ways that reduce fat processing. The main caveat is scope. A small reduction is plausible for moderate acidification, but stronger acidity can impair the enzyme far more than “slightly.”