Application of dual-enzyme nanoflower in the epoxidation of alkenes

Zhang, Liu; Ma, Yuguang; Wang, Chunyu; Wang, Zhi; Chen, Xiao; Li, Meixi; Zhao, Rui; Wang, Lei

doi:10.1016/j.procbio.2018.08.029

Cited by 28 publications

(18 citation statements)

References 35 publications

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“…Enzyme catalytic promiscuity is the functional properties of enzymes which can catalyze new types of transformations in addition to their natural reactions . In this field, lipases are the most used enzymes for their excellent promiscuous catalytic capabilities in many organic transformations . Several lipases can catalyze aza‐Michael additions as efficient and environmentally friendly catalysts.…”

Section: Introductionmentioning

confidence: 99%

“…12 In this field, lipases are the most used enzymes for their excellent promiscuous catalytic capabilities in many organic transformations. [13][14][15][16][17][18][19] Several lipases can catalyze aza-Michael additions as efficient and environmentally friendly catalysts. For example, the wild-type and Ser105Ala mutant of CAL-B can catalyze the Michael-type addition of thiol and amine nucleophiles to a range of , -unsaturated carbonyl compounds.…”

Section: Introductionmentioning

confidence: 99%

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Lipase‐catalyzed aza‐Michael addition of amines to acrylates in supercritical carbon dioxide

Zhang

Wang

et al. 2019

J of Chemical Tech & Biotech

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BACKGROUND Aza‐Michael addition, a powerful method for the synthesis of β‐amino carbonyl derivatives, has been extensively studied in organic chemistry. In this study, the efficient and chemoselective aza‐Michael addition of amines to acrylates catalyzed by lipase in supercritical carbon dioxide (scCO2) was reported for the first time. RESULTS Under the optimal conditions [amine (1 mmol), acrylate (1 mmol), novozym 435 (20 mg), 40 °C, scCO2 (25 mL, 10 MPa)], the corresponding Michael adducts of amines to acrylates were exclusively obtained in high yields (60–93%) for a short reaction time (1 h). No aminolysis was observed when scCO2 was used as reaction medium. Moreover, novozym 435 showed high reusability in scCO2 for aza‐Michael addition. CONCLUSION The excellent chemoselectivity and reusability of novozym 435 in scCO2 indicate the method's great potential for practical application. © 2019 Society of Chemical Industry

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Lipase‐catalyzed aza‐Michael addition of amines to acrylates in supercritical carbon dioxide

Zhang

Wang

et al. 2019

J of Chemical Tech & Biotech

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“…After ten cycles, the co-immobilized enzymes' activity in the epoxidation reaction remained at 82 %, proving the efficiency of reusing the catalyst. [53] Another application of hybrid structures was evaluated by He et al [54] on the selective oxidation of sulfides. The authors have produced nanoflowers from cytochrome P450, an extremely versatile biocatalyst for different reactions, and copper phosphate.…”

Section: Enzymatic Synthesis Of Chemicalsmentioning

confidence: 99%

Nanoflowers: A New Approach of Enzyme Immobilization

Costa

Cipolatti

Fúrigo

et al. 2022

The Chemical Record

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Enzymes are biocatalysts known for versatility, selectivity, and brand operating conditions compared to chemical catalysts. However, there are limitations to their large-scale application, such as the high costs of enzymes and their low stability under extreme reaction conditions. Immobilization techniques can efficiently solve these problems; nevertheless, most current methods lead to a significant loss of enzymatic activity and require several steps of activation and functionalization of the supports. In this context, a new form of immobilization has been studied: forming organic-inorganic hybrids between metal phosphates as inorganic parts and enzymes as organic parts. Compared to traditional immobilization methods, the advantages of these nanomaterials are high surface area, simplicity of synthesis, high stability, and catalytic activity. The current study presents an overview of organic-inorganic hybrid nanoflowers and their applications in enzymatic catalysis.

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“…[1,2] Glucose is also a major carbon source for industrial fermentation yielding important chemicals such as amino acids, organic acids, vitamins, and biofuels. [3,4] The conversion of glucose into chemicals often involves a large number of enzymatic cascades that employ glucose oxidase (GOx) to generate hydrogen peroxide (H 2 O 2 ) for subsequent reactions such as oxidation, [5] epoxidation, [6] and halogenation. [7] The in vitro fabrication of glucose empowered by enzymatic cascades has also been actively pursued for chemical synthesis in non-natural environments unfavorable for microbial growth.…”

Section: Introductionmentioning

confidence: 99%

Glucose Induces Heme Leakage and Suppresses H₂O₂ Uptake of Chloroperoxidase in the Asymmetric Hydroxylation of Ethylbenzene

Wang

Jian

et al. 2022

ChemCatChem

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As a basic feedstock for both natural life and chemical production, glucose is converted into various chemicals upon the help of peroxidase cascades composed of glucose oxidase (GOx) and peroxidases. However, little is known about the glucose effect on the structure and activity of peroxidases in a non-natural environment. We report herein that glucose deactivates chloroperoxidase (CPO) used in the asymmetric hydroxylation of ethylbenzene into (R)-1-phenylethanol. Through both experiment and molecular simulation, we discover that glucose deactivates CPO through hydrophobic interaction with heme and hydrogen bonding with Glu 183 . These interactions lead to heme leakage and the reduction of H 2 O 2 uptake thereby undermining the CPO activity. The mechanism appears generically applicable to other hemeproteins such as horseradish peroxidase, hemoglobin, and myoglobin. These findings may open new avenues for the design of peroxidase cascades for applications ranging from better diagnosis of diabetes to green synthesis of chemicals by direct functionalization of CÀ H bonds.

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Application of dual-enzyme nanoflower in the epoxidation of alkenes

Cited by 28 publications

References 35 publications

Lipase‐catalyzed aza‐Michael addition of amines to acrylates in supercritical carbon dioxide

Lipase‐catalyzed aza‐Michael addition of amines to acrylates in supercritical carbon dioxide

Nanoflowers: A New Approach of Enzyme Immobilization

Glucose Induces Heme Leakage and Suppresses H₂O₂ Uptake of Chloroperoxidase in the Asymmetric Hydroxylation of Ethylbenzene

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Application of dual-enzyme nanoflower in the epoxidation of alkenes

Cited by 28 publications

References 35 publications

Lipase‐catalyzed aza‐Michael addition of amines to acrylates in supercritical carbon dioxide

Lipase‐catalyzed aza‐Michael addition of amines to acrylates in supercritical carbon dioxide

Nanoflowers: A New Approach of Enzyme Immobilization

Glucose Induces Heme Leakage and Suppresses H2O2 Uptake of Chloroperoxidase in the Asymmetric Hydroxylation of Ethylbenzene

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Product

Resources

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Glucose Induces Heme Leakage and Suppresses H₂O₂ Uptake of Chloroperoxidase in the Asymmetric Hydroxylation of Ethylbenzene