Kinetic studies on pancreatic lipase activity in micellar systems. I. Inhibition by sodium deoxycholate micelles.

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Abstract
Pancreatic lipase activity toward vinyl laurate (VL) solubilized in sodium deoxycholate (NaDC) micelles was investigated kinetically. The inhibition by substrate-free NaDC micelles, M, was observed, and a Lineweaver-Burk plot and a plot of the reciprocal of initial rate vs. M indicated that the inhibition may be fully competitive or fully mixed inhibition, depending on the value adopted for the aggregation number of NaDC micelles. A fully competitive inhibition mechanism is indicated. Km and the inhibition constant, K4, which is the Kd of lipase-NaDC micelle complex, were estimated. Km indicates the lower limit of the Kd of lipase-NaDC micelle solubilizing VL, K1. The results are discussed in relation to the results of other studies on the inhibition of the enzyme by bile salts in emulsion systems.

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