Solvent-Free Synthesis of Flavour Esters through Immobilized Lipase Mediated Transesterification.

Q2 Biochemistry, Genetics and Molecular Biology
Enzyme Research Pub Date : 2013-01-01 Epub Date: 2013-05-30 DOI:10.1155/2013/367410
Vijay Kumar Garlapati, Rintu Banerjee
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引用次数: 59

Abstract

The synthesis of methyl butyrate and octyl acetate through immobilized Rhizopus oryzae NRRL 3562 lipase mediated transesterification was studied under solvent-free conditions. The effect of different transesterification variables, namely, molarity of alcohol, reaction time, temperature, agitation, addition of water, and enzyme amount on molar conversion (%) was investigated. A maximum molar conversion of 70.42% and 92.35% was obtained in a reaction time of 14 and 12 h with the transesterification variables of 0.6 M methanol in vinyl butyrate and 2 M octanol in vinyl acetate using 80 U and 60 U immobilized lipase with the agitation speed of 200 rpm and 0.2% water addition at 32°C and 36°C for methyl butyrate and octyl acetate, respectively. The immobilized enzyme has retained good relative activity (more than 95%) up to five and six recycles for methyl butyrate and octyl acetate, respectively. Hence, the present investigation makes a great impingement in natural flavour industry by introducing products synthesized under solvent-free conditions to the flavour market.

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固定化脂肪酶介导的无溶剂风味酯合成研究。
在无溶剂条件下,研究了固定化米根霉NRRL 3562脂肪酶介导的酯交换反应合成丁酸甲酯和乙酸辛酯。考察了醇的摩尔浓度、反应时间、温度、搅拌、水的加入和酶的用量对摩尔转化率(%)的影响。固定脂肪酶用量为80u和60u,搅拌速度为200 rpm,加入0.2%水,32℃和36℃,丁酸甲酯和乙酸辛酯的酯交换速率分别为0.6 M甲醇和2 M辛醇,反应时间为14 h和12 h,最大摩尔转化率为70.42%和92.35%。该固定化酶对丁酸甲酯和乙酸辛酯分别可循环5次和6次,相对活性均保持在95%以上。因此,本研究将在无溶剂条件下合成的产品引入香精市场,对天然香精行业产生重大影响。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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来源期刊
Enzyme Research
Enzyme Research Biochemistry, Genetics and Molecular Biology-Biochemistry
CiteScore
4.60
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