Kinetics of acylglycerol sequential hydrolysis by human milk bile salt activated lipase and effect of taurocholate as fatty acid acceptor

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Abstract
The simplest reaction scheme for the conversion of trioleoylglycerol to glycerol catalyzed by human milk bile salt activate lipase can be described by consecutive first-order reactions: triacylglycerol .**GRAPHIC**. diacylglycerol .**GRAPHIC**. monoacylglycerol .**GRAPHIC**. glycerol. In these equations, k1, k2, and k3 represent the pseudo-first-order the rate constants for the indicated reactions. The results from this study show that although the relative ratio of k2/k1 or k3/k1 may change somewhat, depending on the reaction conditions, the enzyme has a reactivity with the order of dioleoylglycerol > trioleoylglycerol > monooleoylglycerol. The incomplete equilibration of the intermediary diacylglycerol and monoacylglycerol with the bulk of the substrate during sequential lipolysis of triacylglycerol provides a means for their efficient lipolysis and minimizes the effect of partial acylglycerol as competitive substrates for intact triacylglycerol lipolysis. Taurocholate functions both as an activator of the enzyme and also as fatty acid acceptor to relieve product inhibition. In the presence of sufficient taurocholate, bovine serum albumin is no longer required as a fatty acid acceptor for the in vitro lipolysis.

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