Cross-linked enzyme aggregates: a simple and effective method for the immobilization of penicillin acylase

Org Lett. 2000 May 18;2(10):1361-4. doi: 10.1021/ol005593x.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Ampicillin / chemical synthesis
  • Cross-Linking Reagents
  • Enzymes, Immobilized / metabolism*
  • Hydrolysis
  • Kinetics
  • Penicillin Amidase / metabolism*
  • Solvents

Substances

  • Cross-Linking Reagents
  • Enzymes, Immobilized
  • Solvents
  • Ampicillin
  • Penicillin Amidase