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. 2002 Nov-Dec;38(6):604-8.

[Reaction kinetics of hydrolysis of animal fat by pancreatic lipase]

[Article in Russian]
A B German  1 , A D Nekliudov, A N Ivankin, A V Berdutina
Affiliations
  • PMID: 12449787

[Reaction kinetics of hydrolysis of animal fat by pancreatic lipase]

[Article in Russian]
A B German et al. Prikl Biokhim Mikrobiol. 2002 Nov-Dec.

Abstract

Hydrolysis of lipids from beef fat by pancreatic lipase was studied. Maximal release of free fatty acids was shown to take place for the first 3 h of experiment. After this, transetherification developed. Following most important time course parameters were determined: maximal hydrolysis rate V = 1.25 +/- 0.1 mg fat/(ml min), Michaelis constant KMH = 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 time course method used could be applied to develop biotransformation of poorly assimilated fats to more valuable products.

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