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| - Tuning Lipase Enantioselectivity in Organic Media UsingSolid-State Buffers
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| - The enantioselectivity exhibited by Candida antarctica lipase B (CALB) in predominantly organicmedia has been studied for different enzyme protonation states. Alcoholysis of (±)-2-phenyl-4-benzyloxazol-5(4H)-one (1) using butan-1-ol as the nucleophile in low-water organic solvents wasused as a model reaction. Using either organo-soluble bases or the newly introduced solid-statebuffers of known pKa, the protonation state of the lipase was altered. By choice of the appropriatesolid-state buffer or organic base, the enantioselectivity could be selectively tuned. Both Et3N andthe solid-state buffer pair CAPSO/CAPSO.Na were found to increase the enantioselectivity of thereaction catalyzed by CALB and that of another lipase (Mucor miehei). Significant differences toboth the enantioselectivity and catalytic rate were observed, especially under hydrated conditionswhere byproduct acid was formed.
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