Garlapati Vijay Kumar, Banerjee Rintu
Microbial Biotechnology and Downstream Processing Laboratory, Agricultural and Food Engineering Department, Indian Institute of Technology, Kharagpur, West Bengal 721302, India.
Enzyme Res. 2013;2013:367410. doi: 10.1155/2013/367410. Epub 2013 May 30.
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.
在无溶剂条件下,研究了固定化米根霉NRRL 3562脂肪酶介导的丁酸甲酯和乙酸辛酯的合成。考察了不同酯交换变量,即醇的摩尔浓度、反应时间、温度、搅拌、水的添加量和酶用量对摩尔转化率(%)的影响。在32℃和36℃下,分别使用80 U和60 U固定化脂肪酶,搅拌速度为200 rpm,添加0.2%的水,在丁酸乙烯酯中使用0.6 M甲醇、在乙酸乙烯酯中使用2 M辛醇的酯交换变量条件下,反应14小时和12小时时,丁酸甲酯和乙酸辛酯的最大摩尔转化率分别为70.42%和92.35%。固定化酶分别对丁酸甲酯和乙酸辛酯进行了五次和六次循环,仍保持了良好的相对活性(超过95%)。因此,本研究通过将无溶剂条件下合成的产品引入香料市场,对天然香料行业产生了重大影响。