Biosynthesis of oleyl oleate in solvent-free system by Candida rugosa Lipase (CRL) immobilized in macroporous resin with cross-linking of aldehyde-dextran

Q2 Chemical Engineering
Yicheng Bi, Min Yu, Haiyan Zhou, Hua Zhou, Ping Wei
{"title":"Biosynthesis of oleyl oleate in solvent-free system by Candida rugosa Lipase (CRL) immobilized in macroporous resin with cross-linking of aldehyde-dextran","authors":"Yicheng Bi,&nbsp;Min Yu,&nbsp;Haiyan Zhou,&nbsp;Hua Zhou,&nbsp;Ping Wei","doi":"10.1016/j.molcatb.2016.05.002","DOIUrl":null,"url":null,"abstract":"<div><p>In our study, oleyl oleate was synthesized through enzymatic esterification of oleic acid with oleyl alcohol using <em>Candida rugosa</em><span> lipase (CRL) immobilized on macroporous resin in a solvent-free system. CRL was immobilized flexibly on the support via aldehyde-dextran, and the effectiveness of aldehyde-dextrans, as cross-linking agents with different molecular weights, was compared and discussed. The impact of various factors, such as different molecular weights of dextran, molar ratio between oleic acid and oleyl alcohol, and the temperature and stability of enzymes, on esterification was investigated as well. Our study indicated that lipase immobilized by 20000</span> <!-->Da dextran yielded the best result. The optimal condition to produce oleyl oleate using immobilized CRL was found in our study and turned out to be molar ratio of 1, reaction temperature of 40<!--> <!-->°C, and a 12-h reaction time to reach reaction equilibrium. Under the optimal reaction conditions, a high percentage yield of ester was achieved (92.6%). The immobilized CRL also reached a conversion rate of 86.7% with excellent stability even after 8 cycles.</p></div>","PeriodicalId":16416,"journal":{"name":"Journal of Molecular Catalysis B-enzymatic","volume":"133 ","pages":"Pages 1-5"},"PeriodicalIF":0.0000,"publicationDate":"2016-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.molcatb.2016.05.002","citationCount":"25","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of Molecular Catalysis B-enzymatic","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S138111771630073X","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"2016/5/10 0:00:00","PubModel":"Epub","JCR":"Q2","JCRName":"Chemical Engineering","Score":null,"Total":0}
引用次数: 25

Abstract

In our study, oleyl oleate was synthesized through enzymatic esterification of oleic acid with oleyl alcohol using Candida rugosa lipase (CRL) immobilized on macroporous resin in a solvent-free system. CRL was immobilized flexibly on the support via aldehyde-dextran, and the effectiveness of aldehyde-dextrans, as cross-linking agents with different molecular weights, was compared and discussed. The impact of various factors, such as different molecular weights of dextran, molar ratio between oleic acid and oleyl alcohol, and the temperature and stability of enzymes, on esterification was investigated as well. Our study indicated that lipase immobilized by 20000 Da dextran yielded the best result. The optimal condition to produce oleyl oleate using immobilized CRL was found in our study and turned out to be molar ratio of 1, reaction temperature of 40 °C, and a 12-h reaction time to reach reaction equilibrium. Under the optimal reaction conditions, a high percentage yield of ester was achieved (92.6%). The immobilized CRL also reached a conversion rate of 86.7% with excellent stability even after 8 cycles.

Abstract Image

醛-葡聚糖交联固定化假丝酵母脂肪酶(CRL)在无溶剂体系中合成油酸油酯
在无溶剂体系中,以假丝酵母(Candida rugosa)脂肪酶(CRL)固定在大孔树脂上,通过油酸与油醇的酶促酯化反应合成油酸油酯。通过醛-葡聚糖将CRL灵活地固定在载体上,并比较和讨论了醛-葡聚糖作为不同分子量交联剂的效果。考察了葡聚糖的分子量、油酸与油醇的摩尔比、温度和酶的稳定性等因素对酯化反应的影响。结果表明,用20000葡聚糖固定脂肪酶效果最好。本研究确定了固定化CRL制备油酸油酯的最佳工艺条件为摩尔比为1,反应温度为40℃,反应时间为12 h达到反应平衡。在最佳反应条件下,酯的收率可达92.6%。固定化后的CRL在8次循环后仍具有良好的稳定性,转化率达到86.7%。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
求助全文
约1分钟内获得全文 求助全文
来源期刊
Journal of Molecular Catalysis B-enzymatic
Journal of Molecular Catalysis B-enzymatic 生物-生化与分子生物学
CiteScore
2.58
自引率
0.00%
发文量
0
审稿时长
3.4 months
期刊介绍: Journal of Molecular Catalysis B: Enzymatic is an international forum for researchers and product developers in the applications of whole-cell and cell-free enzymes as catalysts in organic synthesis. Emphasis is on mechanistic and synthetic aspects of the biocatalytic transformation. Papers should report novel and significant advances in one or more of the following topics; Applied and fundamental studies of enzymes used for biocatalysis; Industrial applications of enzymatic processes, e.g. in fine chemical synthesis; Chemo-, regio- and enantioselective transformations; Screening for biocatalysts; Integration of biocatalytic and chemical steps in organic syntheses; Novel biocatalysts, e.g. enzymes from extremophiles and catalytic antibodies; Enzyme immobilization and stabilization, particularly in non-conventional media; Bioprocess engineering aspects, e.g. membrane bioreactors; Improvement of catalytic performance of enzymes, e.g. by protein engineering or chemical modification; Structural studies, including computer simulation, relating to substrate specificity and reaction selectivity; Biomimetic studies related to enzymatic transformations.
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
确定
请完成安全验证×
copy
已复制链接
快去分享给好友吧!
我知道了
右上角分享
点击右上角分享
0
联系我们:info@booksci.cn Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。 Copyright © 2023 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号:604180095
Book学术官方微信
小红书