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- W59201430 abstract "We have studied the inactivation of two chymotrypsin-agarose derivatives in different organic media. The more rigid derivative (multipoint covalently attached one) was much more resistant than the less rigid one (one-point covalently attached) to the deleterious effects of organic solvents. When inactivation was performed under “chemically inert conditions” (e.g. high solvent concentrations, neutral pH and moderate temperatures) it was fairly reversible and an important percentage of catalytic activity could be recovered even by simple washing of the inactivated derivatives with fully aqueous media. However, maximal and reproducible recovery of catalytic activity was only achieved when inactivated enzyme molecules were unfolded by incubation of the derivative in high concentrations of urea before the process of refolding in a fully aqueous medium." @default.
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- W59201430 date "1992-01-01" @default.
- W59201430 modified "2023-10-17" @default.
- W59201430 title "Insolubilized Enzyme Derivatives in Organic Solvents: Mechanisms of Inactivation and Strategies for Reactivation" @default.
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- W59201430 doi "https://doi.org/10.1016/b978-0-444-89046-7.50038-2" @default.
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