Abstract
The present work was undertaken to examine rat pancreatic lipase activity in relation to its ability to be adsorbed on emulsified tributyrin. This study was conducted at a supramicellar concentration of sodium taurodeoxycholate, between pH 6.0 and 8.0, and at different colipase concentrations. A pH adsorption curve was differentiated from the pH activity curve of lipase. The authors concluded that the socalled acid shift of the optimal pH for lipase action described earlier is due to the low adsorption rate of lipase on its substrate at alkaline pH rather than to a change of the pH dependence of the V(max) and K(m) of the enzyme.
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