Operational stability of high initial activity protease catalysts in organic solvents

J.F.A. Fernandes, P.J. Halling

Research output: Contribution to journalArticle

25 Citations (Scopus)

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).
LanguageEnglish
Pages1455-1457
Number of pages2
JournalBiotechnology Progress
Volume18
Issue number6
DOIs
Publication statusPublished - Nov 2002

Fingerprint

Peptide Hydrolases
Subtilisin
1-Propanol
Enzymes
alpha-chymotrypsin

Keywords

  • Immobilized thermolysin
  • peptide-synthesis
  • aspartame precursor
  • methyl-ester
  • enzyme
  • water
  • acetonitrile
  • crystals

Cite this

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title = "Operational stability of high initial activity protease catalysts in organic solvents",
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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Operational stability of high initial activity protease catalysts in organic solvents. / Fernandes, J.F.A.; Halling, P.J.

In: Biotechnology Progress, Vol. 18, No. 6, 11.2002, p. 1455-1457.

Research output: Contribution to journalArticle

TY - JOUR

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AU - Fernandes, J.F.A.

AU - Halling, P.J.

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AB - 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).

KW - Immobilized thermolysin

KW - peptide-synthesis

KW - aspartame precursor

KW - methyl-ester

KW - enzyme

KW - water

KW - acetonitrile

KW - crystals

UR - http://pubs.acs.org/cgi-bin/article.cgi/bipret/2002/18/i06/pdf/bp020098g.pdf

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DO - 10.1021/bp020098g

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