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).
authors.affiliation: Department of Pure and Applied Chemistry, University of Strathclyde, Glasgow G1 1XW, Scotland, UK.
authors.forename: João F
authors.initials: JF
authors.lastname: Amorim Fernandes
authors.forename: Peter J
authors.initials: PJ
authors.lastname: Halling
mesh_terms: D019149:Bioreactors; D002384:Catalysis; D003460:Crystallization; D010450:Endopeptidases / Q000737:chemistry*; D004795:Enzyme Stability; D007700:Kinetics; D012997:Solvents; D020860:Subtilisin / Q000737:chemistry
chemical_list: D012997:Solvents; D010450:Endopeptidases; D020860:Subtilisin