Abstract
An active-site titration method for immobilized trypsin with p-nitrophenyl p′-guanidinobenzoate (NPGB) employing a recirculation reactor system is described. Trypsin, covalently linked to 35 and 150 μm diameter porous glass particles was titrated by this procedure, analyzed for protein content, and then compared with soluble trypsin. Analysis of the titration results indicates that the amount of p-nitrophenol produced by the burst is equal to the amount of active immobilized trypsin. This active site titration determines the absolute amount of active immobilized enzyme and is preferable to either total protein analysis or kinetic assays for characterization of immobilized enzymes.
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