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Operational stability of high initial activity protease catalysts in organic solvents.

Authors
  • Amorim Fernandes, João F1
  • Halling, Peter J
  • 1 Department of Pure and Applied Chemistry, University of Strathclyde, Glasgow G1 1XW, Scotland, UK.
Type
Published Article
Journal
Biotechnology Progress
Publisher
Wiley (John Wiley & Sons)
Publication Date
Jan 01, 2002
Volume
18
Issue
6
Pages
1455–1457
Identifiers
PMID: 12467486
Source
Medline
License
Unknown

Abstract

The first studies on the operational stability of cross-linked enzyme crystals (CLECs) in organic media are described. Although these catalysts display high initial specific activity, they inactivate rapidly, losing more than 50% of the initial activity within the first 4 h under continuous flow. Furthermore, the inactivation is not reversible when returned to an aqueous medium. The same rapid inactivation occurs with adsorbed protease preparations that show similar high initial specific activity (propanol-rinsed enzyme preparations (PREPs) of subtilisin and alpha-chymotrypsin).

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