Synthesis of a Precursor of Bioactive Pentapeptide OGP-(10-14) and the Fragment of Enkephalin Catalyzed by MCM-22 Immobilized or Free Proteases in Organic Solvents

Abstract

Full enzymatic synthesis of a precursor of osteogenic growth peptide fragment (10-14), Z-Tyr-Gly-Phe-Gly-Gly--OEt, was accomplished using immobilized proteases on molecular sieve MCM-22 by adsorption as catalyst via 3+2 synthetic route for the first time. The reuse time of immobilized enzyme was dependent on concrete reaction system. Compared with free enzyme, the reaction rate catalyzed by immobilized enzyme was remarkably enhanced and its synthetic yield was also increased in most cases. The effects of water content and the added amount of Et 3 N on synthesis of fragments of bioactive peptides including OGP-( I 0-14) and enkephalin by immobilized enzymes were different from free enzyme.