Modification of Mesoporous Silicates for Immobilization of Enzymes

Gaffney, Darragh; Cooney, Jakki C.; Magner, Edmond

doi:10.1007/s11244-012-9899-7

Cited by 24 publications

(18 citation statements)

References 61 publications

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“…6 Among the various methods reported for protein immobilization, 5 a recent approach is based on the specific interaction between histidine-tagged proteins engineered by molecular biology 7 and porous materials holding divalent complexes. 8 Examples are available for enzyme immobilization on mesoporous silicates [9][10][11] or electrode surfaces, 8 including controlled orientation, 12 while keeping their catalytic activity. 8,11 The histidine tag-metal complex being reversible, 13 a significant portion of the proteins can be lost upon prolonged use in solution.…”

Section: Introductionmentioning

confidence: 99%

Immobilization of Cysteine-Tagged Proteins on Electrode Surfaces by Thiol–Ene Click Chemistry

Lin

Vilà

Klein

et al. 2016

ACS Appl. Mater. Interfaces

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Thiol-ene click chemistry can be exploited for the immobilization of cysteine-tagged dehydrogenases in an active form onto carbon electrodes (glassy carbon and carbon felt). The electrode surfaces have been first modified with vinylphenyl groups by electrochemical reduction of the corresponding diazonium salts generated in situ from 4-vinylaniline. The grafting process has been optimized in order to not hinder the electrochemical regeneration of NAD(+)/NADH cofactor and soluble mediators such as ferrocenedimethanol and [Cp*Rh(bpy)Cl](+). Having demonstrated the feasibility of thiol-ene click chemistry for attaching ferrocene moieties onto those carbon surfaces, the same approach was then applied to the immobilization of d-sorbitol dehydrogenases with cysteine tag. These proteins can be effectively immobilized (as pointed out by XPS), and the cysteine tag (either 1 or 2 cysteine moieties at the N terminus of the polypeptide chain) was proven to maintain the enzymatic activity of the dehydrogenase upon grafting. The bioelectrode was applied to electroenzymatic enantioselective reduction of d-fructose to d-sorbitol, as a case study.

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Section: Introductionmentioning

confidence: 99%

Immobilization of Cysteine-Tagged Proteins on Electrode Surfaces by Thiol–Ene Click Chemistry

Lin

Vilà

Klein

et al. 2016

ACS Appl. Mater. Interfaces

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“…Consequently, affinity binding showed a higher adsorption capacity (98.1 mg g 21 particles) and activity recovery (92.5%) than the physical adsorption procedure. Cu-and Ni-modified silicas were also used to specifically bind His-tagged lipase [85,86] and a protease inhibitor [87]. Another immobilization technique is to form a spacer arm between the enzyme and activated matrix [88].…”

Section: Silica Nanocarriersmentioning

confidence: 99%

Nanobiocatalyst advancements and bioprocessing applications

Misson

Zhang

Jin

2015

J. R. Soc. Interface.

211

108

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The nanobiocatalyst (NBC) is an emerging innovation that synergistically integrates advanced nanotechnology with biotechnology and promises exciting advantages for improving enzyme activity, stability, capability and engineering performances in bioprocessing applications. NBCs are fabricated by immobilizing enzymes with functional nanomaterials as enzyme carriers or containers. In this paper, we review the recent developments of novel nanocarriers/nanocontainers with advanced hierarchical porous structures for retaining enzymes, such as nanofibres (NFs), mesoporous nanocarriers and nanocages. Strategies for immobilizing enzymes onto nanocarriers made from polymers, silicas, carbons and metals by physical adsorption, covalent binding, cross-linking or specific ligand spacers are discussed. The resulting NBCs are critically evaluated in terms of their bioprocessing performances. Excellent performances are demonstrated through enhanced NBC catalytic activity and stability due to conformational changes upon immobilization and localized nanoenvironments, and NBC reutilization by assembling magnetic nanoparticles into NBCs to defray the high operational costs associated with enzyme production and nanocarrier synthesis. We also highlight several challenges associated with the NBC-driven bioprocess applications, including the maturation of large-scale nanocarrier synthesis, design and development of bioreactors to accommodate NBCs, and long-term operations of NBCs. We suggest these challenges are to be addressed through joint collaboration of chemists, engineers and material scientists. Finally, we have demonstrated the great potential of NBCs in manufacturing bioprocesses in the near future through successful laboratory trials of NBCs in carbohydrate hydrolysis, biofuel production and biotransformation.

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“…In addition to pure silicate materials, a wide range of functionalised MPS can be prepared 25,26 .Modification of silicates 35 can be performed by the functionalization with a range of organic ligands 25,26 or by the incorporation of metals 28,29 . Functionalised MPS can be prepared via three methods; (i) post-synthetically, (ii) directly, and (iii) by incorporation of bridged silesquioxanes.…”

Section: Functionalised Mesoporous Materialsmentioning

confidence: 99%

Immobilisation of enzymes on mesoporous silicate materials

2013

Self Cite

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Mesoproous silicates (MPS) are attractive materials for the immobilisation of enzymes. They possess 5 ordered pore structures, narrow pore size distributions, large surface areas, high stability and can be chemically modified with various functional groups. The properties of MPS materials are reviewed in terms of their ability to act as supports for enzymes for use in biocatalysis with a particular focus on the ability to tailor the surface functionalization of the MPS to suit a specific enzyme. While many reports of the immobilisation of enzymes on MPS have been described, their use as biocatalytic supports is limited. 10Large scale reactors based on MPS will require continuous flow systems where the properties of the support can be tailored while allowing fluid flow at reasonable low pressure.

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Modification of Mesoporous Silicates for Immobilization of Enzymes

Cited by 24 publications

References 61 publications

Immobilization of Cysteine-Tagged Proteins on Electrode Surfaces by Thiol–Ene Click Chemistry

Immobilization of Cysteine-Tagged Proteins on Electrode Surfaces by Thiol–Ene Click Chemistry

Nanobiocatalyst advancements and bioprocessing applications

Immobilisation of enzymes on mesoporous silicate materials

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