Immobilization of Y. lipolytica lipase and the continuous synthesis of geranyl propionate

Q2 Chemical Engineering
Jing Tang , Gang Chen , Lu Wang , Ming Miao , Bo Jiang , Biao Feng
{"title":"Immobilization of Y. lipolytica lipase and the continuous synthesis of geranyl propionate","authors":"Jing Tang ,&nbsp;Gang Chen ,&nbsp;Lu Wang ,&nbsp;Ming Miao ,&nbsp;Bo Jiang ,&nbsp;Biao Feng","doi":"10.1016/j.molcatb.2017.01.019","DOIUrl":null,"url":null,"abstract":"<div><p>In this study, <em>Y. lipolytica</em> lipase LIP2 (Lip2) was immobilized on the macroporous adsorptive resin DA201-C in <em>n</em>-heptane and then used to catalyze the continuous synthesis of geranyl propionate in a continuous stirred tank reactor (CSTR). With the lipase loading of 0.01<!--> <!-->g/g resin, 25<!--> <!-->°C and adsorption for 3<!--> <!-->h, the immobilization efficiency can be up to 98.6% and the synthetic activity of the lipase was 690.8<!--> <!-->U/g after immobilization, representing an increase of 28.5% compared with the free lipase (synthetic activity 537.2<!--> <!-->U/g). The immobilized Lip2 was used to generate geranyl propionate in CSTR, the continuous production of geranyl propionate was performed with 3<!--> <!-->g of immobilized Lip2 at 35<!--> <!-->°C. At the flow rate of 6<!--> <!-->mL/h the process can maintain its steady state at least for 12<!--> <!-->h, which was about three times of the average residence time, and the esterification ratio of 72.8% could be attained. Finally, FT-IR and NMR were used to identify the ester.</p></div>","PeriodicalId":16416,"journal":{"name":"Journal of Molecular Catalysis B-enzymatic","volume":"133 ","pages":"Pages S311-S316"},"PeriodicalIF":0.0000,"publicationDate":"2016-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.molcatb.2017.01.019","citationCount":"4","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of Molecular Catalysis B-enzymatic","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S138111771730019X","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q2","JCRName":"Chemical Engineering","Score":null,"Total":0}
引用次数: 4

Abstract

In this study, Y. lipolytica lipase LIP2 (Lip2) was immobilized on the macroporous adsorptive resin DA201-C in n-heptane and then used to catalyze the continuous synthesis of geranyl propionate in a continuous stirred tank reactor (CSTR). With the lipase loading of 0.01 g/g resin, 25 °C and adsorption for 3 h, the immobilization efficiency can be up to 98.6% and the synthetic activity of the lipase was 690.8 U/g after immobilization, representing an increase of 28.5% compared with the free lipase (synthetic activity 537.2 U/g). The immobilized Lip2 was used to generate geranyl propionate in CSTR, the continuous production of geranyl propionate was performed with 3 g of immobilized Lip2 at 35 °C. At the flow rate of 6 mL/h the process can maintain its steady state at least for 12 h, which was about three times of the average residence time, and the esterification ratio of 72.8% could be attained. Finally, FT-IR and NMR were used to identify the ester.

Abstract Image

脂肪酶的固定化及丙酸香叶醇的连续合成
本研究将脂肪菌脂肪酶LIP2 (LIP2)固定在正庚烷大孔吸附树脂DA201-C上,在连续搅拌槽式反应器(CSTR)中催化连续合成丙酸香叶醇。在负载量为0.01 g/g树脂、温度为25℃、吸附时间为3 h的条件下,固定化效率可达98.6%,固定化后脂肪酶的合成活性为690.8 U/g,比游离脂肪酶(合成活性537.2 U/g)提高了28.5%。固定化的Lip2在CSTR中生成丙酸香叶醚,用3g固定化的Lip2在35℃下连续生产丙酸香叶醚。在6 mL/h的流速下,酯化率可达72.8%,至少可保持12 h的稳态,约为平均停留时间的3倍。最后用FT-IR和NMR对其进行了鉴定。
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:481959085
Book学术官方微信