Studies on the mechanism of the lipase reaction. II. Comparative studies on the adsorption of lipases and various proteins at the air-water interface.
Adsorption of lipases (EC 3.1.1.3) and various proteins at the air-water interface has been investigated in relation to the mechanism of lipase reaction. Aqueous solutions of lipases and denaturated proteins show surface activity as strong as that of synthetic detergents. However, ths surface activity of esterases and various other proteins is little or none. By foam fractionation it was shown that lipases were adsorbed at the air-water interface and the adsorption followed the equation of Langmuir's adsorption isotherm. The properties of lipase at the interface are discussed in relation to the mechanism of lipase reaction and the differences from the esterase reaction.
D000327:Adsorption; D000388:Air; D000818:Animals; D001230:Aspergillus / Q000201:enzymology; D002175:Candida / Q000201:enzymology; D002645:Chickens; D002861:Chromobacterium / Q000201:enzymology; D004950:Esterases; D008049:Lipase / Q000378:metabolism*; D008099:Liver / Q000201:enzymology; D009113:Muramidase; D011485:Protein Binding; D011506:Proteins; D011549:Pseudomonas / Q000201:enzymology; D013499:Surface Properties; D013500:Surface Tension; D014867:Water
D011506:Proteins; D014867:Water; D004950:Esterases; D008049:Lipase; D009113:Muramidase