The effect of surface-active agents on pancreatic lipase

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Abstract
The majority of anionic detergents tested inhibited enzymic hydrolysis of triolein in high concentrations and all had no effect in dilute solutions. Liquoid (Roche) increased the velocity of triolein hydrolysis. Sodium dodecyl sulfate inhibited triacetin hydrolysis but strongly stimulated tributyrin hydrolysis. Cationic detergents, when used under certain conditions, markedly increased the velocity of triolein hydrolysis by lipase. The increased rate of hydrolysis produced by these detergents and that produced by bile salts were not additive. Hexadecyl-pyridinium bromide inhibited triacetin hydrolysis but increased the rate of tributyrin hydrolysis. Non-ionic detergents, with the exception of Lubrol MO, which caused a small increase in rate, had no effect on the rate of triolein hydrolysis used in dilute solutions and inhibited lipase in concentrated solutions. Cholesterol added to triolein increased the velocity of hydrolysis of triolein by lipase. Experimental evidence, though not conclusive, supports the hypothesis that the main role of bile salts is to emulsify the fatty substrates rather than to act as lipase activators.