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Effect of Temperature and pH on the Esterase Activity of Bile-Salt-Stimulated Human Milk Lipase

Department of Chemistry University of Auckland Private Bag Auckland, New Zealand

Paul A.G. Butler

Department of Chemistry University of Auckland Private Bag Auckland, New Zealand

Bridget M. Sutton

Department of Chemistry University of Auckland Private Bag Auckland, New Zealand

The initial rate constants of hydrolysis of 4-nitrophenyl acetate, catalyzed by bile-salt-stimulated human milk lipase, have been measured over the tempera ture range 20 ° C to 37 ° C, in 0.1 M buffer solutions in the pH range 6-10, and in the presence of 2 mM sodium taurocholate. From these data, the values of the energy of activation have been calculated and found to be independent of pH. Analysis of the data has also led to determination of the values of the disso ciation constants, pK₁ (8.20) and pK₂ (8.70) (at 25°C), and heats of formation, H° (40.2 and 59.4 kJ mol ^-1, respectively), of the essential ionizable residues of the enzyme.

Journal of Bioactive and Compatible Polymers, Vol. 3, No. 3, 219-231 (1988)
DOI: 10.1177/088391158800300303


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