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首页> 外文期刊>Biomacromolecules >Polyphosphazenes as Tunable and Recyclable Supports To Immobilize Alcohol Dehydrogenases and Lipases: Synthesis, Catalytic Activity, and Recycling Efficiency
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Polyphosphazenes as Tunable and Recyclable Supports To Immobilize Alcohol Dehydrogenases and Lipases: Synthesis, Catalytic Activity, and Recycling Efficiency

机译:聚磷腈作为可调节和可回收的载体来固定酒精脱氢酶和脂肪酶:合成,催化活性和回收效率。

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摘要

The polyphosphazene {NP[O2C_(12)H_(7.5)(NH2)_(0.5)]}_n, prepared by reacting {NP[O2C_(12)H_(7.5)(NO2)_(0.5)]} with the Lalancette's reagent, was used for attaching enzymes such as alcohol dehydrogenase (ADH-A) and lipase (CAL-B). The resulting new biocatalysts exhibited great potential as tunable supports for enzymatic reactions in both aqueous and organic media. The material with immobilized ADH-A was as efficient as the commercial enzyme to perform stereoselective bioreductions of ketones in aqueous solutions and could be used for the reduction of various aliphatic and aromatic ketones up to 60 °C and recycled several times without significant loss of activity even after three months of storage. The biocatalyst obtained with CAL-B was more efficient than the free enzyme for kinetic resolutions in organic solvents and exhibited a moderately good capability of reutilization.
机译:使{NP [O2C_(12)H_(7.5)(NO2)_((0.5)]}与Lalancette's反应制得的聚磷腈{NP [O2C_(12)H_(7.5)(NH2)_(0.5)]} _ n试剂,用于连接酶,例如乙醇脱氢酶(ADH-A)和脂肪酶(CAL-B)。所得的新型生物催化剂作为在水和有机介质中进行酶促反应的可调载体均具有巨大潜力。固定化ADH-A的材料与商业酶一样有效,可以在水溶液中进行酮的立体选择性生物还原,可用于还原高达60°C的各种脂肪族和芳香族酮,并循环使用数次而不会显着降低活性即使储存三个月也是如此。对于有机溶剂中的动力学拆分,用CAL-B获得的生物催化剂比游离酶更有效,并且具有中等良好的再利用能力。

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