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Synthesis of terpinyl acetate by lipase-catalyzed esterification in supercritical carbon dioxide

机译:超临界二氧化碳中脂肪酶催化酯化反应合成乙酸叔丁酯

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摘要

Terpinyl acetate was successfully synthesized from (x-terpineol and acetic anhydride in supercritical carbon dioxide (SC-CO2) by enzymatic catalysis. Five different lipases (Candida rugosa type VII, Amano PS, Amano AP-6, Amano G and Lipozyme RM IM) as biocatalysts for the terpinyl acetate synthesis were compared. An esterification extent of 53.0% was obtained in continuous operation using acetic anhydride as acyl donor and C, rugosa lipase as enzyme at 10 MPa and 50 degrees C for 1.5 h. Temperature in the range of 35-50 degrees C demonstrated that the yield of terpinyl acetate increase with temperature increase in the current study. Operating at a alpha-terpineol/acetic anhydride molar ratio 3.0, the conversion of alcohol decreased, probably due to an inhibitory effect on enzyme by high concentration of acetic anhydride or by formation of acetic acid. However, the enzyme activity still remained more than 50% after 10.5 h repeated esterification in a batch under optimized conditions. Crown Copyright (C) 2009 Published by Elsevier Ltd. All rights reserved.
机译:通过酶催化从(x-松油醇和乙酸酐在超临界二氧化碳(SC-CO2)中)成功合成了乙酸萜品酯,五种不同的脂肪酶(皱纹念珠菌VII,Amano PS,Amano AP-6,Amano G和Lipozyme RM IM)比较了乙酸叔丁基酯合成的生物催化剂,在10 MPa和50摄氏度下,乙酸酐作为酰基供体,C,脂酶作为酶,连续操作1.5 h,酯化程度为53.0%。在本研究中,温度为35-50摄氏度时,乙酸叔丁基酯的收率随温度的升高而增加,在α-萜品醇/乙酸酐摩尔比为3.0的条件下,醇的转化率降低,这可能是由于高浓度对酶的抑制作用所致。浓度的乙酸酐或通过形成乙酸,但是,在最佳条件下,一批重复进行酯化反应10.5小时后,酶活性仍保持超过50%。自己的版权(C)2009,由Elsevier Ltd.发行。保留所有权利。

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