title: Cross-linked enzyme aggregates: a simple and effective method for the immobilization of penicillin acylase.
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.
authors.affiliation: Laboratory of Organic Chemistry and Catalysis, Julianalaan 136, 2628 BL Delft, The Netherlands.
authors.forename: L
authors.initials: L
authors.lastname: Cao
authors.forename: F
authors.initials: F
authors.lastname: van Rantwijk
authors.forename: R A
authors.initials: RA
authors.lastname: Sheldon
mesh_terms: D000667:Ampicillin / Q000138:chemical synthesis; D003432:Cross-Linking Reagents; D004800:Enzymes, Immobilized / Q000378:metabolism*; D006868:Hydrolysis; D007700:Kinetics; D010399:Penicillin Amidase / Q000378:metabolism*; D012997:Solvents
chemical_list: D003432:Cross-Linking Reagents; D004800:Enzymes, Immobilized; D012997:Solvents; D000667:Ampicillin; D010399:Penicillin Amidase