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首页> 外文期刊>Catalysis science & technology >Carbon nanotube/PTFE as a hybrid platform for lipase B from Candida antarctica in transformation of alpha-angelica lactone into alkyl levulinates
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Carbon nanotube/PTFE as a hybrid platform for lipase B from Candida antarctica in transformation of alpha-angelica lactone into alkyl levulinates

机译：碳纳米管/聚四氟乙烯作为混合动力平台从南极假丝酵母脂肪酶B的变换alpha-angelica内酯

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摘要

In this work an enzymatic method for the synthesis of alkyl levulinates from alpha-angelica lactone has been reported for the first time. Lipase B from Candida antarctica was immobilized via interfacial activation on the surface of a hybrid support, consisting of commercially available multi-walled carbon nanotubes (MWCNTs) and polytetrafluoroethylene (PTFE). Among the biocatalysts with various contents of PTFE in the support, the CALB/MWCNT-PTFE (0.10 wt%) biocatalyst with 22.5 wt% CALB loading was determined as the most active one in the model synthesis of the n-butyl levulinate in toluene. n-Butyl levulinate was obtained quantitively after 120 min of the reaction under the selected reaction conditions (2-fold molar excess of n-butanol, 0.150 g of biocatalyst per 1 mmol of alpha-angelica lactone, 20 degrees C). The yield of n-butyl levulinate was found to be higher than that in the presence of accurate amounts of sulfuric acid or Novozyme-435. Additionally, the unique stability of the developed biocatalyst was demonstrated over 6 reaction cycles at 20 degrees C. The biocatalyst remained stable over 3 reaction cycles at 60 degrees C as well. The essence of the proposed approach lies in the possibility to overcome the equilibrium limitations occurring in the conventional Fisher esterification. The activity of the elaborated hybrid biocatalyst in the reactions non-specific for lipases is a clear proof of the versatility of the novel system.
机译：在这工作一个酶的合成方法的烷基levulinates alpha-angelica内酯首次报道。从南极假丝酵母固定化通过界面激活表面上的混合支持,包括商用多壁碳纳米管(热合)和聚四氟乙烯(PTFE)。聚四氟乙烯的生物催化剂与各种内容支持,CALB / MWCNT-PTFE (0.10 wt %)生物催化剂为22.5 wt % CALB加载模型中最活跃的一个决定在甲苯的合成正丁基levulinate。正丁基levulinate得到特征120分钟后选择下的反应反应条件(2倍摩尔过剩正丁醇,0.150克每1更易与生物催化剂alpha-angelica内酯,20摄氏度),收益率正丁基的levulinate高于被发现在准确的数量硫酸或novozyme - 435。独特的发达生物催化剂的稳定性在20度证明6反应周期c的生物催化剂保持稳定/ 3反应周期60摄氏度。该方法的本质在于可能克服平衡缺陷发生在传统的费舍尔酯化。混合生物催化剂的非特异性反应脂酶是一个多才多艺的明显的证据小说的系统。

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