Enantioselective acetylation of (R,S)-atenolol: The use of Candida rugosa lipases immobilized onto magnetic chitosan nanoparticles in enzyme-catalyzed biotransformation

Q2 Chemical Engineering Journal of Molecular Catalysis B-enzymatic Pub Date : 2016-12-01 DOI:10.1016/j.molcatb.2016.09.017

Adam Sikora , Dorota Chełminiak-Dudkiewicz , Tomasz Siódmiak , Agata Tarczykowska , Wiktor Dariusz Sroka , Marta Ziegler-Borowska , Michał Piotr Marszałł

{"title":"Enantioselective acetylation of (R,S)-atenolol: The use of Candida rugosa lipases immobilized onto magnetic chitosan nanoparticles in enzyme-catalyzed biotransformation","authors":"Adam Sikora , Dorota Chełminiak-Dudkiewicz , Tomasz Siódmiak , Agata Tarczykowska , Wiktor Dariusz Sroka , Marta Ziegler-Borowska , Michał Piotr Marszałł","doi":"10.1016/j.molcatb.2016.09.017","DOIUrl":null,"url":null,"abstract":"<div>This paper describes the enzyme immobilization protocol as well as the enzymatic method for the direct resolution of (R,S)-atenolol. The used magnetic enzyme carriers possess on their surface new-synthetized chitosan derivatives with free amine groups distanced by ethyl or butyl chain. Additionally the catalytic activity of two types of commercially available lipases from Candida rugosa immobilized onto two different magnetic nanoparticles were compared. The highest values of enantioselectivity (E=66.9), enantiomeric excess of product (eep    <!-->41.84%) were obtained by using lipase from Candida rugosa OF immobilized onto Fe3O4-CS-EtNH2. The study confirmed that even after 5 reaction cycles the immobilized lipase maintain its high catalytic activity.</div>","PeriodicalId":16416,"journal":{"name":"Journal of Molecular Catalysis B-enzymatic","volume":"134 ","pages":"Pages 43-50"},"PeriodicalIF":0.0000,"publicationDate":"2016-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.molcatb.2016.09.017","citationCount":"27","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of Molecular Catalysis B-enzymatic","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S1381117716301916","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: 27

Abstract

This paper describes the enzyme immobilization protocol as well as the enzymatic method for the direct resolution of (R,S)-atenolol. The used magnetic enzyme carriers possess on their surface new-synthetized chitosan derivatives with free amine groups distanced by ethyl or butyl chain. Additionally the catalytic activity of two types of commercially available lipases from Candida rugosa immobilized onto two different magnetic nanoparticles were compared. The highest values of enantioselectivity (E = 66.9), enantiomeric excess of product (ee_p = 94.1%) and conversion (c = 41.84%) were obtained by using lipase from Candida rugosa OF immobilized onto Fe₃O₄-CS-EtNH₂. The study confirmed that even after 5 reaction cycles the immobilized lipase maintain its high catalytic activity.

Abstract Image

查看原文

微信好友朋友圈 QQ好友复制链接

本刊更多论文

(R,S)-阿替洛尔的对映选择性乙酰化:磁性壳聚糖纳米颗粒固定化念珠菌脂肪酶在酶催化生物转化中的应用

本文介绍了酶固定方法和酶法直接分离(R,S)-阿替洛尔的方法。所使用的磁性酶载体表面具有以乙基或丁基链为间隔的游离胺基的新合成壳聚糖衍生物。此外，还比较了两种不同磁性纳米颗粒固定化假丝酵母脂肪酶的催化活性。以Fe3O4-CS-EtNH2固定念珠菌脂肪酶对映体选择性(E = 66.9)、产物对映体过量(eep = 94.1%)和转化率(c = 41.84%)最高。研究证实，即使经过5个反应循环，固定化脂肪酶仍保持较高的催化活性。

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分钟内获得全文去求助

来源期刊

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

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.