Polyphosphazenes as Tunable and Recyclable Supports To Immobilize Alcohol Dehydrogenases and Lipases: Synthesis, Catalytic Activity, and Recycling Efficiency
Polyphosphazenes as Tunable and Recyclable Supports To Immobilize Alcohol Dehydrogenases and Lipases: Synthesis, Catalytic Activity, and Recycling Efficiency
复制标题
DOI：
10.1021/bm100091a
复制
发表时间：
2010-05-01
影响因子：
6.2
通讯作者：
Carriedo, Gabino A.
中科院分区：
文献类型：
--
作者：
Cuetos, Anibal;Valenzuela, Maria L.;Carriedo, Gabino A.
通过使{NP[O2C12H7.5（NO2）（0.5）]}与Lalancette试剂反应制备的聚磷腈{NP [O2C12H7.5（NH 2）（0.5]）}（n）用于附着酶如醇脱氢酶（ADH-A）和脂肪酶（CAL-B）。由此产生的新的生物催化剂表现出巨大的潜力，可调支持酶促反应在水和有机介质中。具有固定化ADH-A的材料与商业酶一样有效地在水溶液中进行酮的立体选择性生物还原，并且可用于还原高达60 ° C的各种脂肪族和芳香族酮，并且即使在储存三个月后也不会显著损失活性。与CAL-B获得的生物催化剂是更有效的比游离酶在有机溶剂中的动力学拆分，并表现出适度良好的重复利用能力。
The polyphosphazene {NP[O2C12H7.5(NH2)(0.5])}(n), prepared by reacting {NP[O2C12H7.5(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 degrees 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.