[Immobilization of proteins on macroporous glasses involving maleinimide as the anchoring group]

Macroporous glasses with pore sizes from 400-1000 A appropriate for protein binding were produced and characterized by a thermal demixing procedure and alkaline after treatment. To achieve a covalent binding capacity relative to proteins, the gamma-aminopropyl derivative was allowed to react with 4-maleinimido benzoylic chloride to give preparations containing, in addition to maleinimide residues, acid chloride structures for the protein binding. A preparation of 400 A pore size was tested for its protein binding capacity relative to bovine serum albumin and trypsin. Furthermore, the capacity of binding glucoamylase from Endomycopsis bispora in active form was studied.