Preparation of core–shell polymer supports to immobilize lipase B from Candida antarctica

南极洲假丝酵母 脂肪酶 化学 水解 固定化酶 聚合物 醋酸乙烯酯 动力学分辨率 聚乙烯醇 肺表面活性物质 色谱法 有机化学 高分子化学 共聚物 催化作用 生物化学 对映选择合成
作者
Aline G. Cunha,Marina D. Besteti,Evelin Andrade Manoel,Angelo A.T. da Silva,Rodrigo Volcan Almeida,Alessandro B. C. Simas,Roberto Fernández‐Lafuente,José Carlos Pinto,Denise Maria Guimarães Freire
出处
期刊:Journal of Molecular Catalysis B-enzymatic [Elsevier BV]
卷期号:100: 59-67 被引量:75
标识
DOI:10.1016/j.molcatb.2013.11.020
摘要

Core–shell supports have been prepared and utilized to immobilize lipase B from Candida antarctica. The hydrophobic nature of the supports permitted to immobilize the enzyme via interfacial activation at low ionic strength. Different supports were prepared having different hydrophobicity and crosslinking degree, and compared to the commercially available. Accurel MP 1000 (hydrophobic macroporous polymer of propylene) is a commercial support described as advantageous in different circumstances and it was used as comparative control in the process of immobilization. The immobilized lipase preparations were evaluated in the hydrolysis of p-nitro-phenyl laurate and the esterification of oleic acid with ethanol. On the kinetic resolution of (±)-1,2-O-isopropylidene-3,6-di-O-benzyl-myo-inositol, vinyl acetate was used as activated acyl donor. Results were very diverse, as the lipase properties may be easily tuned via immobilization, and some of the supports permitted to obtain activities even a two fold factor higher than the same amount of lipase immobilized in Accurel MP 1000. Moreover, in many instances, the loading of the support with enzyme produced reduced total activity in some reactions while not in other. This was explained by changes in the physical properties of the support surface that may alter the entry of substrates. Supports PS-co-DVB/PS-co-DVB 25% and PMMA-co-DVB/PMMA-co-DVB 25% presented very good features to immobilize CALB.

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