Lipase kinetics at the triacylglycerol-water interface using surface tension measurements.
Two methods, the so-called "oil drop" and "Teflon plunger" methods, were designed to monitor lipase hydrolysis of natural long-chain triacylglycerols through the variation with time of the oil-water interfacial tension. The first part of this work is devoted to the development of these two techniques using pure, well-characterized porcine pancreatic lipase. They gave linear responses with enzyme concentrations ranging from 1 x 10(-3) to 30 units x ml-1. We then applied them to a study of the optimal pH conditions for human gastric lipase which were found to range around 5, as previously observed. In the presence of variable concentrations of sodium taurodeoxycholate, these two methods also showed that human gastric lipase is active in the 8-13 dyn cm-1 range of interfacial tension. It is concluded that these two methods, based upon variations with time of the oil-water interfacial tension, constitute reliable, sensitive and convenient means of investigating lipase kinetics.[1]References
- Lipase kinetics at the triacylglycerol-water interface using surface tension measurements. Nury, S., Piéroni, G., Rivière, C., Gargouri, Y., Bois, A., Verger, R. Chem. Phys. Lipids (1987) [Pubmed]
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