Cross-Linked Enzyme Aggregates: A Simple and Effective Method for the Immobilization of Penicillin Acylase
Top Cited Papers
- 20 April 2000
- journal article
- letter
- Published by American Chemical Society (ACS) in Organic Letters
- Vol. 2 (10), 1361-1364
- https://doi.org/10.1021/ol005593x
Abstract
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.Keywords
This publication has 7 references indexed in Scilit:
- Penicillin Acylase in the Industrial Production of β-Lactam AntibioticsOrganic Process Research & Development, 1998
- Penicillin V acylase: Its potential in the production of 6-aminopenicillanic acidEnzyme and Microbial Technology, 1997
- Effect of pH in the synthesis of ampicillin by penicillin acylaseEnzyme and Microbial Technology, 1996
- Dynamic reaction design of enzymic biotransformations in organic media: equilibrium‐controlled synthesis of antibiotics by penicillin G acylaseBiotechnology and Applied Biochemistry, 1996
- Modification of Enzyme Properties by the use of Inhibitors During Their Stabilisation by Multipoint Covalent AttachmentBiocatalysis and Biotransformation, 1995
- Cross-linked enzyme crystals as robust biocatalystsJournal of the American Chemical Society, 1992
- Enzyme reaction engineering: Synthesis of antibiotics catalysed by stabilized penicillin G acylase in the presence of organic cosolventsEnzyme and Microbial Technology, 1991