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首页> 外文期刊>Journal of the American Oil Chemists' Society >Esterification of Lauric Acid Using Lipase Immobilized in the Micropores of a Hollow-Fiber Membrane
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Esterification of Lauric Acid Using Lipase Immobilized in the Micropores of a Hollow-Fiber Membrane

机译:使用固定在中空纤维膜微孔中的脂肪酶酯化月桂酸

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摘要

A porous anion-exchange hollow-fiber membrane was prepared by radiation-induced graft polymerization and chemical modification to immobilize lipase for enzymatic reaction in an organic solvent.The amount of anion-exchange group introduced to the porous hollow-fiber membrane was 2.5 mol/kg_(fiber).A lipase solution was allowed to permeate through the porous anion-exchange hollow-fiber membrane,and lipase molecules that adsorbed onto the grafted polymer brush were cross-linked with glutaraldehyde.The lipase was immobilized at a density of 0.14 kg_(lipase)/kg_(fiber),which was equivalent to a degree of multilayer binding of 20.Esterification was carried out by passing a solution of lauric acid and benzyl alcohol in anhydrous isooctane through the lipase-immobilized membrane,and lipase activity was determined.A reaction percentage of 50% was achieved at space velocity 68 h~(-1).The maximum immobilized lipase and native lipase activities were 8.9 and 0.38 mol/(h centre dot kg_(lipase) ),respectively.Thus,the activity of the immobilized lipase was 23.4 times higher than that of the native lipase.
机译:通过辐射诱导的接枝聚合反应和化学修饰制备脂肪族阴离子交换中空纤维膜,将脂肪酶固定在有机溶剂中进行酶促反应,引入到阴离子交换中空纤维膜的量为2.5 mol /脂肪酶溶液透过多孔的阴离子交换中空纤维膜渗透,吸附在接枝聚合物刷上的脂肪酶分子与戊二醛交联,脂肪酶以0.14 kg_的密度固定化。 (脂肪酶)/ kg_(纤维),相当于多层结合度为20。通过使月桂酸和苯甲醇在无水异辛烷中的溶液通过固定有脂肪酶的膜进行酯化,并测定脂肪酶活性。在空速68 h〜(-1)时达到50%的反应百分数。最大固定化脂肪酶和天然脂肪酶的活性为8.9和0.38 mol /(h中心点kg_(脂肪酶)),res因此,固定化脂肪酶的活性是天然脂肪酶的23.4倍。

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