The inhibition of lysozyme by bile acids.

The effect of bile acids on the bacteriolytic activity of lysozyme towards Micrococcus lysodeikticus was studied in vitro. All bile acids tested inhibited lysozyme activity. Conjugated bile acids were better inhibitors than their unconjugated homologs and sulfation resulted in still stronger inhibition. A study of UV-difference spectra of bile acid-lysozyme mixtures suggests that bile acids distort the tertiary structure of the enzyme. The inhibition-concentration curves of micelle-forming bile acids were bell-shaped, and peak inhibition was apparently related to the critical micellar concentration. The inhibition-concentration curves of sulfated bile acids, which do not form micelles, are characterized by a plateau of maximal inhibition. A mechanism of lysozyme activation by bile acid micelles is proposed. Our results illustrate the complex interactions between antibacterial compounds in the gut. As bile acids are known to inhibit lipase activity as well, these studies suggest that bile acids may have an important influence on intestinal enzyme activity in general.