A study on the surface hydrophobicity of lipases

Surface properties, including surface net and local hydrophobicities, of bovine serum albumin, γ-globulin, and six lipases of different origins were evaluated using the aqueous two-phase partitioning method. Each showed a specific and characteristic pattern of surface properties. Correlations between the protein surface hydrophobicities and the coverages of the proteins by lipid-coating with a synthetic detergent, dioleyl glucosyl L- glutamate, were discussed. The results indicated that the surface net hydrophobicity of each protein was indicative of the affinity of the protein for the coating detergent applied in lipid-coating. (C) 2000 Elsevier Science S.A.