{"title":"Biosynthesis of ethyl butyrate with immobilized Candida rugosa lipase onto modified Eupergit®C","authors":"Daniele Spinelli, S. Coppi, R. Basosi, R. Pogni","doi":"10.2478/boca-2014-0001","DOIUrl":null,"url":null,"abstract":"Abstract Lipase from Candida rugosa was immobilized onto the modified Eupergit®C. The support was treated with ethylenediamine and subsequently activated with glutaraldehyde. Enzyme immobilization efficiency was 85%. The optimum pH was close to 6.5 for both the free and immobilized lipase. Immobilized lipase retained its maximum activity in a temperature range of 55 – 60°C. Subsequently, ethyl butyrate synthesis was investigated using immobilized enzyme by esterification of butyric acid with ethanol in solvent-free conditions (23% product yield) and using hexane as a solvent (65% product yield). The acid-alcohol molar ratio and different enzyme amounts were tested as efficient reaction parameters. The biocatalyst maintained 60% of its activity when reused in 8 successive batch reactions in organic solvent. Therefore, the immobilized lipase has demonstrated its potential in practical applications such as short-chain ester synthesis for the food industry. Graphical Abstract","PeriodicalId":8747,"journal":{"name":"Biocatalysis","volume":"70 1","pages":"1 - 12"},"PeriodicalIF":0.0000,"publicationDate":"2014-10-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"13","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biocatalysis","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.2478/boca-2014-0001","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 13
Abstract
Abstract Lipase from Candida rugosa was immobilized onto the modified Eupergit®C. The support was treated with ethylenediamine and subsequently activated with glutaraldehyde. Enzyme immobilization efficiency was 85%. The optimum pH was close to 6.5 for both the free and immobilized lipase. Immobilized lipase retained its maximum activity in a temperature range of 55 – 60°C. Subsequently, ethyl butyrate synthesis was investigated using immobilized enzyme by esterification of butyric acid with ethanol in solvent-free conditions (23% product yield) and using hexane as a solvent (65% product yield). The acid-alcohol molar ratio and different enzyme amounts were tested as efficient reaction parameters. The biocatalyst maintained 60% of its activity when reused in 8 successive batch reactions in organic solvent. Therefore, the immobilized lipase has demonstrated its potential in practical applications such as short-chain ester synthesis for the food industry. Graphical Abstract