Substrate Specifity Of Porcine Pancreatic Lipase Studied In Terms Of The Steady-State Kinetics Binding And Rate Constants

Abstract

The steady-state kinetics binding constants have been rarely determined for emulsified lipase substrates since the apparent Michaelis constant has the dimension of the emulsion surface area in this case [1,2] which typically could not be determined precisely. On the other hand, only a combination of binding and rate parameters could be determined in experiments with substrate monolayers [3,4], and the range of suitable substratesis strictly limited in these experiments due to requirements on the stability of monolayers, productsolubility, etc. [4]. In this paper we review data on the substrate specificity of porcine pancreatic lipase on emulsified triacylglycerolsubstrates studied in terms of the steady-state binding and rate constants in the assay system lipase/colipase/micellar NaTDC'/-triacylglycerol emulsion’.