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Lamb Pregastric Esterase Catalyzed Hydrolysis of 4-Nitrophenyl-Acetate and -Dodecanoate: pH, Temperature and Bile Salt Effects

Department of Chemistry, The University of Auckland, Private Bag 92019, Auckland, New Zealand

Richard H. Barton

Department of Chemistry, The University of Auckland, Private Bag 92019, Auckland, New Zealand

Douglas T. Lai

Department of Chemistry, The University of Auckland, Private Bag 92019, Auckland, New Zealand

Two fractions, F2 and F3, eluted by ion exchange chromatography of the commercial extract of lamb pregastric enzyme have esterase activity against 4-nitrophenylacetate, PNPA. Preheat treatment of fraction F3 at pH 7.2, 50°C for 15 min effectively removes its lipase activity against tributyrin while leaving the esterase component relatively unaffected. The esterase components in fractions F2 and F3 and the lipase component in fraction F3 have K_m values against PNPA equal to 0.96, 2.1 and 2.7 mM, respectively. When 4-nitrophenyldecanoate, PNPDe, was used as substrate, the maximum activity was reached at its critical micelle concentration, 1.6 µM, for catalysis by all three enzymes. The reactivity is dependent upon pH and pK values of 6.7 and 8.4, 6.7 and 7.5, and 7.3 were determined from the lipase and esterase components in fraction F3, and the fraction F2 esterase, respectively. The dependence upon temperature of the activities of the esterase components against PNPA were determined within the range 25-47.5°C and Arrhenius parameters have been calculated. The presence of sodium taurocholate affected the activity of each enzyme to a small and differing extent.

Journal of Bioactive and Compatible Polymers, Vol. 11, No. 1, 43-60 (1996)
DOI: 10.1177/088391159601100104


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