Isocyanide-based multi-component reactions for carrier-free and carrier-bound covalent immobilization of enzymes

Yousefi, Maryam; Shahedi, Mansour; Ahrari, Faezeh; Mostafavi, Mostafa; Habibi, Zohreh; Yousefi, Maryam

doi:10.1038/s41596-023-00812-z

Cited by 12 publications

(3 citation statements)

References 44 publications

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“…Multi-component reactions (MCRs) 1 are widely recognized as important tools in synthetic and medicinal chemistry, providing efficient and atom-economical routes to drugs 2 and structurally diverse compounds with a broad range of biological activities. 3 Active intermediates involved in MCRs make them a valuable methodological arsenal in the synthesis of complex molecules, enabling rapid access to a diverse chemical space. 4 Metal carbynes/carbynoids constitute an active and unique class of organometallic species, and as such exhibit distinctive electronic properties, are capable of forming up to three sigma bonds on a single carbon, and hold great potential for the development of new synthetic methodologies and the synthesis of complex molecules (Scheme 1A).…”

Section: Introductionmentioning

confidence: 99%

Rhodium-catalyzed formal four-component reaction with hypervalent iodine diazoesters, alcohols, and isatins for the synthesis of multi-functionalized oxindoles

Tang,

Yang,

Niu

et al. 2024

Org. Chem. Front.

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Section: Introductionmentioning

confidence: 99%

Rhodium-catalyzed formal four-component reaction with hypervalent iodine diazoesters, alcohols, and isatins for the synthesis of multi-functionalized oxindoles

Tang,

Yang,

Niu

et al. 2024

Org. Chem. Front.

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“…15 Among all methods, carrier-bound immobilization achieved by covalent linkage of enzymes to a solid support is highly desirable since it can minimize enzyme contamination in the final product and facilitate straightforward product separation. 16 Furthermore, the immobilization of enzymes can also offer additional benefits that include easy handling, repeated use in reaction cycles, and improved recovery from the reaction mixture. Direct visualization of the enzyme distribution within solidsupported materials is crucial for the development and optimization of enzyme immobilization processes and evaluating its reaction performance.…”

Section: Introductionmentioning

confidence: 99%

“…Biocatalyst immobilization methods can be classified into three categories: entrapment by confining an enzyme within a network or matrix, adsorption or covalent binding to a solid carrier, and intermolecular bond formation between enzymes by cross-linking . Among all methods, carrier-bound immobilization achieved by covalent linkage of enzymes to a solid support is highly desirable since it can minimize enzyme contamination in the final product and facilitate straightforward product separation . Furthermore, the immobilization of enzymes can also offer additional benefits that include easy handling, repeated use in reaction cycles, and improved recovery from the reaction mixture.…”

Section: Introductionmentioning

confidence: 99%

Modernized Machine Learning Approach to Illuminate Enzyme Immobilization for Biocatalysis

Wei,

Smith

2023

ACS Cent. Sci.

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Biocatalysis is an established technology with significant application in the pharmaceutical industry. Immobilization of enzymes offers significant benefits for commercial and practical purposes to enhance the stability and recyclability of biocatalysts. Determination of the spatial and chemical distributions of immobilized enzymes on solid support materials is essential for an optimal catalytic performance. However, current analytical methodologies often fall short of rapidly identifying and characterizing immobilized enzyme systems. Herein, we present a new analytical methodology that combines non-negative matrix factorization (NMF)an unsupervised machine learning toolwith Raman hyperspectral imaging to simultaneously resolve the spatial and spectral characteristics of all individual species involved in enzyme immobilization. Our novel approach facilitates the determination of the optimal NMF model using new data-driven, quantitative selection criteria that fully resolve all chemical species present, offering a robust methodology for analyzing immobilized enzymes. Specifically, we demonstrate the ability of NMF with Raman hyperspectral imaging to resolve the spatial and spectral profiles of an engineered pantothenate kinase immobilized on two different commercial microporous resins. Our results demonstrate that this approach can accurately identify and spatially resolve all species within this enzyme immobilization process. To the best of our knowledge, this is the first report of NMF within hyperspectral imaging for enzyme immobilization analysis, and as such, our methodology can now provide a new powerful tool to streamline biocatalytic process development within the pharmaceutical industry.

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Improving the stability of an unstable lipase by applying different immobilization strategies for the selective hydrolysis of fish oil

Ahrari,

Pourmohammadi Lish,

Yousefi

et al. 2024

J Americ Oil Chem Soc

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Rhizopus oryzae lipase (ROL) is known to present high selectivity in chemical reactions. However, the poor stability of ROL effectively limits its industrial applications. In this study, several immobilization protocols, such as hydrophobic adsorption, covalent immobilization, multi‐point covalent attachment, ionic adsorption/cross‐linking, and ionic interaction, were applied to improve the stability of ROL. Heterogeneous modification of aspartic and glutamic acid residues on the surface of ROL was carried out by 1‐ethyl‐3‐(3‐dimethylaminopropyl) carbodiimide (EDC) to introduce new amine groups with lower pKb. The highest immobilization yield of 89% was achieved for octyl‐agarose, producing specific activity of 45 U/mg, which is 15 folds higher than the specific activity of the soluble enzyme. Improved stability of ROL was observed, in particular for those derivatives obtained by multi‐point covalent attachment of ROL on glyoxyl‐agarose (Gx‐ROL) and aminated ROL on glyoxyl‐agarose (Gx‐NH2‐ROL) by retaining 28%–36% of their initial activities after 24 h incubation at 60°C. Immobilization also altered the co‐solvent stability profile of the immobilized derivatives producing biocatalysts with varied co‐solvent stabilities. Furthermore, utilization of the immobilized preparations in fish oil hydrolysis revealed the selective release of cis‐5,8,11,14,17‐eicosapentaenoic acid (EPA) and cis‐4,7,10,13,16,19‐docosahexaenoic acid (DHA) in favor of EPA. The highest EPA/DHA selectivity of 33 was observed for the hydrophobically immobilized ROL on octyl‐sepharose.

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Isocyanide-based multi-component reactions for carrier-free and carrier-bound covalent immobilization of enzymes

Cited by 12 publications

References 44 publications

Rhodium-catalyzed formal four-component reaction with hypervalent iodine diazoesters, alcohols, and isatins for the synthesis of multi-functionalized oxindoles

Rhodium-catalyzed formal four-component reaction with hypervalent iodine diazoesters, alcohols, and isatins for the synthesis of multi-functionalized oxindoles

Modernized Machine Learning Approach to Illuminate Enzyme Immobilization for Biocatalysis

Improving the stability of an unstable lipase by applying different immobilization strategies for the selective hydrolysis of fish oil

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