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• W76878189 abstract "Abstract Enzymes in crystalline form are functionally stabilized by the intermolecular lattice contacts within the crystal and by chemical cross-links formed with bifunctional reagents such as glutaraldehyde. Such cross-linked enzyme crystals (or CLECs™) remain active in environments that are otherwise incompatible with enzyme function, including prolonged exposure to high temperatures, extremes of pH, near-anhydrous organic solvents and aqueous-organic solvent mixtures. In addition, CLECs™ are remarkably resistant to autolysis and to exogenous protease degradation. Surprisingly, CLECs™ retain their activity when reconstituted after lyophilization and, in that form, can be stored indefinitely at room temperature. Lyophilized CLECs™ can be easily reconstituted in a variety of solvent systems - including organics - as monodisperse, non-aggregated suspensions. We have only recently reported all of these properties in CLECs™ of the enzyme thermolysin [1,2], which is used in the manufacture of the artificial sweetener aspartame [3–5]. As discussed below, deep seated and widely held misconceptions about crystalline enzymes may have discouraged the earlier development of this technology." @default.
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• W76878189 date "1993-01-01" @default.
• W76878189 modified "2023-10-10" @default.
• W76878189 title "Crosslinked enzyme crystals (CLECs™) as immobilized enzyme particles" @default.
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• W76878189 doi "https://doi.org/10.1016/b978-0-444-89372-7.50013-0" @default.
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