Naver_1995_Scand.J.Immunol_41_443

The antigenicity of 36 Humicola lanuginosa lipase (HL) variants, generated by site directed mutagenesis, was compared with that of the unchanged enzyme. Polyclonal antibodies raised against variant lipases were investigated and compared with the antibodies raised against the wild type lipase in an ELISA competition assay. The results showed that exchange of charged amino acids with polar residues in surface epitopes of HL, results in a tighter binding of the antibody to the epitope. Four amino acids (Trp at position 89, Asp at positions 96 and 254 and Phe at position 211) were found to be essential for antibody binding in each their epitope of the wild type enzyme.