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- W2000641540 abstract "Purified hydroxynitrile lyase (HNL) from Manihot esculenta was crystallized by the sitting-drop vapour-diffusion method. The bipyramidal crystals formed (10–20 μm) were cross-linked with different amounts of glutaraldehyde and used as biocatalyst for the synthesis of optically active cyanohydrins. The cross-linked crystals were more stable than Celite-immobilized enzymes when incubated in organic solvents, especially in polar solvents. After six consecutive batch reactions in dibutylether, the remaining activity of the cross-linked crystals was more than 70 times higher than for the immobilized enzymes. Nevertheless, the specific activity of the cross-linked crystals (per milligram protein) was reduced compared to the activity of immobilized enzymes. The product enantiopurity was independent of the type of enzyme preparation used." @default.
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- W2000641540 date "2001-01-01" @default.
- W2000641540 modified "2023-10-13" @default.
- W2000641540 title "Cross-linked crystals of hydroxynitrile lyase as catalyst for the synthesis of optically active cyanohydrins" @default.
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- W2000641540 doi "https://doi.org/10.1016/s1381-1177(00)00057-6" @default.
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