Stimulation of Chromobacterium lipase activity and prevention of its adsorption to palmitoyl cellulose by hydrophobic binding of fatty acids.
Fatty acids prevented adsorption of purified Chromobacterium lipase [triacylglycerol acylhydrolase, EC 3.1.1.3] onto palmitoyl cellulose (Pal-C) and also increased the activity of the purified lipase. These effects increased with increase in the concentration and chainlength (up to 16 carbon atoms) of the fatty acids, and long-chain unsaturated fatty acids, such as oleic acid, linoleic acid and erucic acid, were most effective. When the lipase was adsorbed (immobilized) on Pal-C, its activity was elevated to 20 times that of the free lipase in detergent-free reaction mixture (olive oil-buffer system). Thus lipase was adsorbed to Pal-C through a hydrophobic site distinct from its catalytic site and the binding of fatty acids to the hydrophobic site seems to result in stimulation of the lipase activity.
D000327:Adsorption; D001665:Binding Sites; D002482:Cellulose / Q000031:analogs & derivatives*; D002846:Chromatography, Affinity; D002861:Chromobacterium / Q000201:enzymology*; D004800:Enzymes, Immobilized; D005227:Fatty Acids / Q000494:pharmacology*; D008049:Lipase / Q000378:metabolism; D010168:Palmitates; D013329:Structure-Activity Relationship
D004800:Enzymes, Immobilized; D005227:Fatty Acids; D010168:Palmitates; D002482:Cellulose; D008049:Lipase