Peptidsynthesen mit immobilisierten Enzymen II. Immobilisiertes Trypsin,Thermolysin und Papain

Model studies were performed on the utility of covalently immobilized trypsin, thermolysin and papain for peptide bond formation. Trypsin and thermolysin catalyzed the formation of peptide bonds with nearly the same efficiency as the soluble proteases and they could be re-used successfully for further coupling experiments. The possibility of using immobilized trypsin and papain for kinetically controlled peptide bond formation was investigated. With the serine type enzyme trypsin excellent product yields were obtained starting with ester carboxyl components and an economical ratio of substrates. Experiments with the thiol protease papain were unsatisfactory because the once formed product is hydrolyzed as fast as the starting ester substrate used.