Biocatalytic epoxidation of α-pinene to oxy-derivatives over cross-linked lipase aggregates

Q2 Chemical Engineering

Journal of Molecular Catalysis B-enzymatic Pub Date : 2016-12-01 DOI:10.1016/j.molcatb.2016.09.009

Madalina Tudorache , Andreea Gheorghe , Ana S. Viana , Vasile I. Parvulescu

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引用次数: 18

Abstract

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.

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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

研究了基于脂肪酶的交联聚集体的非特异性反应，即α-蒎烯环氧化成其氧合衍生物。生物催化剂的活性在绿色环境下进行了评估，即乙酸乙酯作为醋酸盐供应商和有机溶剂，H2O2/UHP/TBHP作为氧化剂。脂肪酶来源的筛选表明，黑曲霉脂肪酶是该反应最有效的生物催化剂。以活性为主要参数，评价了不同固定方案((i)交联酶聚集体(CLEA)， (ii)交联酶聚集体磁性颗粒(CLEMPA)和(iii)共价固定化酶(CIE)磁性颗粒(MP))。因此，CLEA和CLEMPA对CIE具有较好的α-蒎烯环氧化产率。所研究的生物催化系统允许将α-蒎烯转化为具有工业和商业应用的氧化衍生物(例如α-蒎烯氧化物，莰烯，蒎二醇和莰烯醛)。FTIR研究揭示了固定化方案对酶二级结构的影响。此外，通过扫描电子显微镜(SEM)、透射电子显微镜(TEM)和原子力显微镜(AFM)分析进行了纹理表征。

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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.