The Kinetics of Hydrolysis of Animal Fat by Pancreatic Lipase


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Abstract

Hydrolysis of lipids from beef fat by pancreatic lipase was studied. The maximum release of free fatty acids was shown to occur at 40°C for the first 3 h of the experiment. After this, transetherification was predominant. The main kinetic parameters were the following: maximum hydrolysis rate, V = 1.25 ± 0.1 mg fat/ml min; Michaelis constant, KHM = 100 ± 12 mg fat/ml; constant of substrate inhibition, KS = 10.0 ± 0.8 mg fat/ml; equilibrium constant, KP = 277 ± 170 mg fat/ml; and activation energy of beef fat hydrolysis by pancreatic lipase, Ea = 19.1 ± 1.1 kJ/mole. The kinetic method used could be applied to development of the method for biotransformation of poorly assimilated fats into more valuable products.

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