Application of an immobilized penicillin acylase to the deprotection of N-phenylacetyl insulin
Wang, Q.C.; Fei, J.; Cui, D.F.; Zhu, S.G.; Xu, L.G.
Biopolymers 25 Suppl: S109-S114
1986
ISSN/ISBN: 0006-3525 PMID: 3535913 Document Number: 3799
An immobilized enzymatic approach for amino group protection of proteins or large peptides is presented. As a model, porcine insulin was N-phenylacetylated and deprotected by an immobilized penicillin acylase. The enzymatic hydrolysis was achieved in the presence of a basic resin used to remove the small molecule by-product, phenylacetate. No apparent damage to the peptide backbone has been found in the enzymatic deprotection process because the conditions for both the protection and deprotection were very mild and the enzyme was quite specific to phenylacetyl amides. Therefore, this approach seems particularly useful to the semisyntheses of protein or large peptide analogs, and it is superior to those deprotection approaches using proteases or peptidases.
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