Madalina Tudorache , Andreea Gheorghe , Ana S. Viana , Vasile I. Parvulescu
{"title":"交联脂肪酶聚合体上α-蒎烯环氧化生成氧衍生物的生物催化反应","authors":"Madalina Tudorache , Andreea Gheorghe , Ana S. Viana , Vasile I. Parvulescu","doi":"10.1016/j.molcatb.2016.09.009","DOIUrl":null,"url":null,"abstract":"<div><p>Lipase-based cross-linked aggregates were investigated for a non-specific reaction, <em>i.e.</em> the epoxidation of α-pinene to its oxygenated derivatives. The activity of the biocatalysts has been evaluated in a green context, <em>i.e</em>. ethyl acetate as both acetate-supplier and organic solvent with H<sub>2</sub>O<sub>2</sub>/UHP/TBHP as oxidant. Screening of the lipase sources indicated <em>Aspergillus niger</em> lipase as the most efficient biocatalyst for this reaction. Different immobilization protocols ((i) cross-linked enzyme aggregates (CLEA), (ii) cross-linked enzyme aggregates onto magnetic particles (CLEMPA) and (iii) covalent immobilized enzyme (CIE) onto magnetic particles (MP)) were evaluated considering the activity as main parameter. Thus, CLEA and CLEMPA afforded better epoxidation yields of α-pinene towards CIE. The investigated biocatalytic systems allowed to transform α-pinene into oxigenated derivatives with industrial and commercial applications (<em>e.g.</em> α-pinene oxide, camphene, pinanediol and camphonelic aldehyde). FTIR investigations on the biocatalysts revealed the effects of the immobilization protocol on the enzyme secondary-structure. Additionally, textural characterizations were performed by Scanning Electron Microscopy (SEM), Transmission Electron Microscopy (TEM) and Atomic Force Microscopy (AFM) analysis.</p></div>","PeriodicalId":16416,"journal":{"name":"Journal of Molecular Catalysis B-enzymatic","volume":"134 ","pages":"Pages 9-15"},"PeriodicalIF":0.0000,"publicationDate":"2016-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.molcatb.2016.09.009","citationCount":"18","resultStr":"{\"title\":\"Biocatalytic epoxidation of α-pinene to oxy-derivatives over cross-linked lipase aggregates\",\"authors\":\"Madalina Tudorache , Andreea Gheorghe , Ana S. Viana , Vasile I. Parvulescu\",\"doi\":\"10.1016/j.molcatb.2016.09.009\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>Lipase-based cross-linked aggregates were investigated for a non-specific reaction, <em>i.e.</em> the epoxidation of α-pinene to its oxygenated derivatives. The activity of the biocatalysts has been evaluated in a green context, <em>i.e</em>. ethyl acetate as both acetate-supplier and organic solvent with H<sub>2</sub>O<sub>2</sub>/UHP/TBHP as oxidant. Screening of the lipase sources indicated <em>Aspergillus niger</em> lipase as the most efficient biocatalyst for this reaction. Different immobilization protocols ((i) cross-linked enzyme aggregates (CLEA), (ii) cross-linked enzyme aggregates onto magnetic particles (CLEMPA) and (iii) covalent immobilized enzyme (CIE) onto magnetic particles (MP)) were evaluated considering the activity as main parameter. Thus, CLEA and CLEMPA afforded better epoxidation yields of α-pinene towards CIE. The investigated biocatalytic systems allowed to transform α-pinene into oxigenated derivatives with industrial and commercial applications (<em>e.g.</em> α-pinene oxide, camphene, pinanediol and camphonelic aldehyde). FTIR investigations on the biocatalysts revealed the effects of the immobilization protocol on the enzyme secondary-structure. Additionally, textural characterizations were performed by Scanning Electron Microscopy (SEM), Transmission Electron Microscopy (TEM) and Atomic Force Microscopy (AFM) analysis.</p></div>\",\"PeriodicalId\":16416,\"journal\":{\"name\":\"Journal of Molecular Catalysis B-enzymatic\",\"volume\":\"134 \",\"pages\":\"Pages 9-15\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2016-12-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1016/j.molcatb.2016.09.009\",\"citationCount\":\"18\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Journal of Molecular Catalysis B-enzymatic\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/S1381117716301734\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q2\",\"JCRName\":\"Chemical Engineering\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of Molecular Catalysis B-enzymatic","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S1381117716301734","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q2","JCRName":"Chemical Engineering","Score":null,"Total":0}
Biocatalytic epoxidation of α-pinene to oxy-derivatives over cross-linked lipase aggregates
Lipase-based cross-linked aggregates were investigated for a non-specific reaction, i.e. the epoxidation of α-pinene to its oxygenated derivatives. The activity of the biocatalysts has been evaluated in a green context, i.e. ethyl acetate as both acetate-supplier and organic solvent with H2O2/UHP/TBHP as oxidant. Screening of the lipase sources indicated Aspergillus niger lipase as the most efficient biocatalyst for this reaction. Different immobilization protocols ((i) cross-linked enzyme aggregates (CLEA), (ii) cross-linked enzyme aggregates onto magnetic particles (CLEMPA) and (iii) covalent immobilized enzyme (CIE) onto magnetic particles (MP)) were evaluated considering the activity as main parameter. Thus, CLEA and CLEMPA afforded better epoxidation yields of α-pinene towards CIE. The investigated biocatalytic systems allowed to transform α-pinene into oxigenated derivatives with industrial and commercial applications (e.g. α-pinene oxide, camphene, pinanediol and camphonelic aldehyde). FTIR investigations on the biocatalysts revealed the effects of the immobilization protocol on the enzyme secondary-structure. Additionally, textural characterizations were performed by Scanning Electron Microscopy (SEM), Transmission Electron Microscopy (TEM) and Atomic Force Microscopy (AFM) analysis.
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.
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