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 Et3 N on synthesis of fragments of bioactive peptides including OGP-(10-14) and enkephalin
by immobilized enzymes were different from free enzyme.
Key words
immobilized enzyme - MCM-22 - OGP-(10-14) - enzymatic peptide synthesis - organic
solvents
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