Studies on the mechanism of lipase reaction. III. Adsorption of Chromobacterium lipase on hydrophobic glass beads.

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Abstract
The lipase [EC 3.1.1.3] from Chromobacterium was adsorbed on glass beads which were coated with olive oil, liquid paraffin or silicone oil. The adsorption was treated in the Lineweaver-Burk''s plot, and characters of the adsorption were similar to each other regardless of the chemical structure of the hydrophobic materials. Esterase [EC 3.1.1.1] from porcine liver was not adsorbed on hydrophobic glass beads. The interaction between the lipase and hydrophobic surface conformed to the Langmuir''s adsorption isotherm with a Kd = 1.4 .times. 10-7 M. At saturation of the surface with the lipase each protein molecule occupied an average area of 4500 .ANG.2/molecule. Adsorption of lipase on the hydrophobic surface increased activity about 3-fold. The hydrophobic bonds apparently play a major role in the adsorption of the lipase on substrate or hydrophobic surface.

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