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Cross-Linked Enzyme Aggregates:  A Simple and Effective Method for the Immobilization of Penicillin Acylase

Organic Letters · 2000 · Vol. 2(10) · pp. 1361–1364

Abstract

[reaction--see text] Penicillin G acylase (penicillin amidohydrolase, E.C. 3.5.1.11) was immobilized in a simple and effective way by physical aggregation of the enzyme, using a precipitant, followed by chemical cross-linking to form insoluble cross-linked enzyme aggregates (CLEAs). These had the same activity in the synthesis of ampicillin as cross-linked crystals of the same enzyme, but the accompanying hydrolysis of the side-chain donor was much less. Penicillin G acylase CLEAs also catalyzed the synthesis of ampicillin in a broad range of organic solvents.

Enzyme Catalysis and ImmobilizationChemical Synthesis and AnalysisGlycosylation and Glycoproteins ResearchChemistryPenicillinHydrolysisEnzymeAmpicillinAmidohydrolasePenicillin amidaseCatalysisImmobilized enzymeOrganic chemistry

MeSH terms

AmpicillinCross-Linking ReagentsEnzymes, ImmobilizedHydrolysisKineticsPenicillin AmidaseSolvents
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