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Lipase-catalyzed esterification of conjugated linoleic acid with L-carnitine in solvent-free system and acetonitrile

机译:无溶剂体系和乙腈中脂肪酶催化的共轭亚油酸与左旋肉碱的酯化反应

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摘要

Lipase-catalyzed esterification of conjugated linoleic acid (CLA) with L-carnitine in solvent-free system and acetonitrile was studied. Three lipases (Novzym 435, Amamo AY30 and Amano AYS) have been assayed as suitable biocatalysts in the reaction. It was found that Amano AY30 was the most effective biocatalyst in both solvent-free system and acetonitrile. The conversion rate varied from 8.05 to 60.9% in terms of reaction conditions such as the amount of lipase, the presence of water, the amount of molecular sieves and reaction time. The conversions of substrate in solvent-free system were higher than that in acetonitrile. When the substrates were 1 mmol CLA and 1 mmol L-carnitine, the maximum conversion (60.9%) was obtained in solvent-free system with 150 mg lipase AY30, 50% water content and 150 mg molecular sieves at the reaction time of 24 h. A novel CLA ester product was successfully isolated and characterized by ESI-MS and ~1H NMR.
机译:研究了在无溶剂体系和乙腈中脂肪酶催化的共轭亚油酸(CLA)与左旋肉碱的酯化反应。已经测定了三种脂肪酶(Novzym 435,Amomo AY30和Amano AYS)作为反应中合适的生物催化剂。发现Amano AY30是无溶剂体系和乙腈中最有效的生物催化剂。就反应条件而言,例如脂肪酶的量,水的存在,分子筛的量和反应时间,转化率在8.05%至60.9%之间变化。无溶剂体系中底物的转化率高于乙腈。当底物为1 mmol CLA和1 mmol L-肉碱时,在24小时的反应时间下,在150 mg脂肪酶AY30、50%水分和150 mg分子筛的无溶剂体系中,可获得最大转化率(60.9%)。 。已成功分离出新型CLA酯产物,并通过ESI-MS和〜1H NMR对其进行了表征。

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