Fernandes, J.F.A. and Halling, P.J. (2002) Operational stability of high initial activity protease catalysts in organic solvents. Biotechnology Progress, 18 (6). pp. 1455-1457. ISSN 8756-7938Full text not available in this repository. (Request a copy from the Strathclyde author)
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).
|Keywords:||Immobilized thermolysin, peptide-synthesis, aspartame precursor, methyl-ester, enzyme, water, acetonitrile, crystals, Chemistry, Biotechnology|
|Subjects:||Science > Chemistry|
|Department:||Faculty of Science > Pure and Applied Chemistry|
|Depositing user:||Users 16 not found.|
|Date Deposited:||14 Mar 2006|
|Last modified:||22 Mar 2017 09:10|