ABSTRACT
Marine mussels secrete the byssus in order to attach to solid surfaces and to servive under the turbulent effects of waves. The adhesive responsable for this atachment is the polyphenolic protein secreted by the phenol gland in the foot of the animal To purify this adhesive protein form the chilean mussel Mylilus chilensis, a modification of previous procedures has been developed. Accordingly, the protein is differentially precipitated with acetone in the presence of 0.25 N HCl. The purified protein is rich in the amino acids lysine, 3,4-dihydroxyphenylalanine, serine, threonine, proline and hydrozyproline. The protein exhibited strong adhesion to glass and other solid supports. Moreover, its has been found that the adhesive protein can mediate the immobilization of ß-galactosidase to glass. About 75% of the enzyme activity was immobilized under the experimental conditions described. This is the first study reporting the use of the polyphenolic protein to immobilize enzymes