Abstract
Selective hydrolysis of borage oil byCandida rugosa lipase immobilized on microporous polypropylene was carried out in an iso-octane-water two-phase system in order to obtain glycerides rich in γ-linolenic acid (GLA). Lipase was immobilized on hydrophobic microporous polypropylene supports by physical adsorption, γ-linolenic acid content in the unhydrolyzed acylglycerols could be raised to 51.7 mol% from an initial content of 23.6 mol% in borage oil with a yield of 59%. A simplified kinetic model was proposed for this selective hydrolysis. The Michaelis constantK M and the maximal-rate constantV max are 0.107M and 393.9 U/mg-protein, respectively. Product inhibition with a dissociation constant of the enzyme-product complexK I = 25 mM was confirmed. Some properties of the immobilized lipase were also examined.
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Abbreviations
- ES*:
-
complex of enzyme and substrate molecules
- K I total mass of enzyme in the reactor (mg):
-
kcat
- rate constant in the Michaelis-Menten equation (mmol/min mg protein):
-
K I dissociation constant for the complex EP* (M)
- K M :
-
apparent Michaelis constant (M)
- P:
-
oleic acid concentration (M)
- Po :
-
initial concentration of oleic acid (mM)
- S:
-
substrate concentration (M)
- So :
-
initial value of S (M)
- t:
-
reaction time (min)
- Vi :
-
initial velocity of reaction (µmol/min)
- Vmax :
-
apparent maximal velocity (µmol/min)
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Huang, FC., Ju, YH. & Huang, Cw. Enrichment in γ-linolenic acid of acylglycerols by the selective hydrolysis of borage oil. Appl Biochem Biotechnol 67, 227–236 (1997). https://doi.org/10.1007/BF02788800
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DOI: https://doi.org/10.1007/BF02788800