Influence of surface properties of mixed monolayers on lipolytic hydrolysis

被引:27
|
作者
Peters, GH
Dahmen-Levison, U
de Meijere, K
Brezesinski, G
Toxvaerd, S
Möhwald, H
Svendsen, A
Kinnunen, PKJ
机构
[1] Tech Univ Denmark, Dept Chem, Membrane & Stat Phys Grp MEMPHYS, DK-2800 Lyngby, Denmark
[2] Max Planck Inst Colloids & Interfaces, D-14476 Golm, Germany
[3] Univ Copenhagen, HC Orsted Inst, Chem Dept 3, DK-2100 Copenhagen O, Denmark
[4] Novo Nordisk AS, DK-2880 Bagsvaerd, Denmark
[5] Univ Helsinki, Inst Biomed, Dept Med Chem, Helsinki, Finland
[6] Univ Helsinki, Inst Biomed, Dept Physiol, Helsinki, Finland
关键词
D O I
10.1021/la9906673
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
Fluorescence microscopy, surface potential, and activity measurements were used to investigate the influence of fatty acids and fatty alcohols on the lipolytic activity of several lipases. We have determined the lateral lipid distribution and interfacial properties of Langmuir mixed monolayers composed of 1,2-didecanoylglycerol/eicosanoic acid or 1,2-didecanoylglycerol/1-octadecanol molecules and have measured lipase activities toward these films. Enzymatic activities are remarkably influenced by the addition of fatty acid. Activity decreases continuously up to a mole fraction of approximate to 0.1 fatty acid, where phase separation and a change in surface potential are observed. Higher concentrations of fatty acid have only marginal effects on the lipase activities. The relative activity between the different lipases varies substantially and there is an indication that the level of inhibition correlates with the isoelectric point (pI) of the enzymes. A simpler mechanism is observed by the addition of fatty alcohol. Within the concentration range studied, 1-octadecanol is immiscible in the diacylglyceride matrix, forming liquid-condensed domains. The inhibitory effect is related to the reduction of available diacylglyceride area to the enzyme; Direct imaging of the lipolytic hydrolysis of these monolayers show that relatively small domains are formed, suggesting that the enzyme preferentially acts on pure diacylglyceride patches.
引用
收藏
页码:2779 / 2788
页数:10
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