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Materials-based Strategies for Multi-enzyme Immobilization and Co-localization a Review

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Co-Immobilization and Co-Localization of Multi-Enzyme Systems on Porous Materials

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Abstract

The immobilization of multi-enzyme systems on solid materials is chop-chop gaining interest for the construction of biocatalytic cascades with biotechnological applications in industry. The heterogenization and control of the spatial organization beyond porous materials of the system components are essentials to improve the performance of the process providing higher robustness, yield, and productivity. In this chapter, the co-immobilization and co-localization of a bi-enzymatic bio-redox orthogonal cascade with in situ cofactor regeneration are described. An NADH-dependent alcohol dehydrogenase catalyzes the asymmetric reduction of 2,2,2 trifluoroacetophenone using an NADH regeneration system consisting of a glutamate dehydrogenase and glutamic acid. Three unlike spatial organizations of the enzymes were compared in terms of cofactor-recycling efficiency. Furthermore, we demonstrated how the co-localization and uniform distribution (past controlling the enzyme immobilization rate) of the main and recycling dehydrogenases within the aforementioned porous particle lead to enhance the cofactor-recycling efficiency of the bi-enzymatic bio-redox systems.

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Figures (0) & Videos (0)

Keywords

Techniques:

Ultrafiltration, Confocal Microscopy, IMAC, HPLC, Cantankerous-linking

Models:

Thermus thermophilus HB27, Escherichia coli

Others:

Enzymes, Immobilization, Co-localization, Porous materials, Cofactor regeneration, Heterogeneous biocatalysis

Citations (2)

Related articles

References

  1. Fessner WD (2015) Systems biocatalysis: evolution and engineering of prison cell-gratuitous "artificial metabolisms" for preparative multi-enzymatic synthesis. New Biotechnol 32:658–664
  2. Köhler V, Turner NJ (2014) Artificial concurrent catalytic processes involving enzymes. Chem Commun 51:450–464
  3. Rollin JA, Tam TK, Zhang YHP (2013) New biotechnology paradigm: cell-free biosystems for biomanufacturing. Greenish Chem 15:1708–1719
  4. Zhu Z, Kin Tam T, Lord's day F, You C, Percival Zhang YH (2014) A high-energy-density saccharide biobattery based on a constructed enzymatic pathway. Nat Commun v:3026
  5. Jia F, Narasimhan B, Mallapragada Southward (2014) Materials-based strategies for multi-enzyme immobilization and co-localization: a review. Biotechnol Bioeng 111:209–222
  6. Schoffelen Southward, Van Hest JCM (2012) Multi-enzyme systems: bringing enzymes together in vitro. Soft Thing 8:1736–1746
  7. Huang X, Li Chiliad, Mann South (2014) Membrane-mediated cascade reactions by enzyme-polymer proteinosomes. Chem Commun fifty:6278–6280
  8. García-García P, Rocha-Martin J, Fernandez-Lorente G, Guisan JM (2018) Co-localization of oxidase and catalase inside a porous support to improve the elimination of hydrogen peroxide: oxidation of biogenic amines by amino oxidase from Pisum sativum. Enzym Microb Technol 115:73–fourscore
  9. Rocha-Martín J, Bdl R, Muñoz R, Guisán JM, López-Gallego F (2012) Rational co-immobilization of bi-enzyme cascades on porous supports and their applications in bio-redox reactions with in situ recycling of soluble cofactors. ChemCatChem 4:1279–1288
  10. Ji X, Su Z, Wang P, Ma G, Zhang Due south (2014) Polyelectrolyte doped hollow nanofibers for positional assembly of bienzyme organization for cascade reaction at O/Due west interface. ACS Catal four:4548–4559
  11. Bolivar JM, Hidalgo A, Sánchez-Ruiloba L, Berenguer J, Guisán JM, López-Gallego F (2011) Modulation of the distribution of small proteins within porous matrixes by smart-control of the immobilization rate. J Biotechnol 155:412–420
  12. Zheng Y-1000, Yin H-H, Yu D-F, Chen X, Tang X-50, Zhang X-J, Xue Y-P, Wang Y-J, Liu Z-Q (2017) Recent advances in biotechnological applications of alcohol dehydrogenases. Appl Microbiol Biotechnol 101:987–1001
  13. van der Donk WA, Zhao H (2003) Contempo developments in pyridine nucleotide regeneration. Curr Opin Biotechnol 14:421–426
  14. Bolivar JM, Cava F, Mateo C, Rocha-Martin J, Guisan JM, Berenguer J, Fernandez-Lafuente R (2008) Immobilization-stabilization of a new recombinant glutamate dehydrogenase from Thermus thermophilus. Appl Microbiol Biotechnol eighty:49–58
  15. Rocha-Martín J, Vega D, Bolivar JM, Hidalgo A, Berenguer J, Guisán JM, López-Gallego F (2012) Characterization and further stabilization of a new anti-prelog specific booze dehydrogenase from Thermus thermophilus HB27 for asymmetric reduction of carbonyl compounds. Bioresour Technol 103:343–350
  16. Mateo C, Bolivar JM, Godoy CA, Rocha-Martin J, Pessela BC, Curiel JA, Muñoz R, Guisan JM, Fernández-Lorente G (2010) Comeback of enzyme backdrop with a 2-pace immobilizaton procedure on novel heterofunctional supports. Biomacromolecules 11:3112–3117

Abstruse

The immobilization of multi-enzyme systems on solid materials is rapidly gaining interest for the construction of biocatalytic cascades with biotechnological applications in industry. The heterogenization and control of the spatial organization beyond porous materials of the system components are essentials to improve the functioning of the process providing college robustness, yield, and productivity. In this chapter, the co-immobilization and co-localization of a bi-enzymatic bio-redox orthogonal cascade with in situ cofactor regeneration are described. An NADH-dependent alcohol dehydrogenase catalyzes the asymmetric reduction of ii,2,2 trifluoroacetophenone using an NADH regeneration organisation consisting of a glutamate dehydrogenase and glutamic acid. Three different spatial organizations of the enzymes were compared in terms of cofactor-recycling efficiency. Furthermore, we demonstrated how the co-localization and uniform distribution (by controlling the enzyme immobilization rate) of the chief and recycling dehydrogenases inside the aforementioned porous particle lead to enhance the cofactor-recycling efficiency of the bi-enzymatic bio-redox systems.

less

Related manufactures

References

  1. Fessner WD (2015) Systems biocatalysis: development and applied science of cell-free "bogus metabolisms" for preparative multi-enzymatic synthesis. New Biotechnol 32:658–664
  2. Köhler V, Turner NJ (2014) Artificial concurrent catalytic processes involving enzymes. Chem Commun 51:450–464
  3. Rollin JA, Tam TK, Zhang YHP (2013) New biotechnology paradigm: cell-free biosystems for biomanufacturing. Green Chem 15:1708–1719
  4. Zhu Z, Kin Tam T, Sunday F, You C, Percival Zhang YH (2014) A loftier-energy-density sugar biobattery based on a constructed enzymatic pathway. Nat Commun v:3026
  5. Jia F, Narasimhan B, Mallapragada Southward (2014) Materials-based strategies for multi-enzyme immobilization and co-localization: a review. Biotechnol Bioeng 111:209–222
  6. Schoffelen S, Van Hest JCM (2012) Multi-enzyme systems: bringing enzymes together in vitro. Soft Affair viii:1736–1746
  7. Huang Ten, Li Thousand, Mann S (2014) Membrane-mediated cascade reactions past enzyme-polymer proteinosomes. Chem Commun 50:6278–6280
  8. García-García P, Rocha-Martin J, Fernandez-Lorente G, Guisan JM (2018) Co-localization of oxidase and catalase inside a porous back up to better the elimination of hydrogen peroxide: oxidation of biogenic amines past amino oxidase from Pisum sativum. Enzym Microb Technol 115:73–80
  9. Rocha-Martín J, Bdl R, Muñoz R, Guisán JM, López-Gallego F (2012) Rational co-immobilization of bi-enzyme cascades on porous supports and their applications in bio-redox reactions with in situ recycling of soluble cofactors. ChemCatChem 4:1279–1288
  10. Ji X, Su Z, Wang P, Ma K, Zhang S (2014) Polyelectrolyte doped hollow nanofibers for positional assembly of bienzyme arrangement for pour reaction at O/W interface. ACS Catal 4:4548–4559
  11. Bolivar JM, Hidalgo A, Sánchez-Ruiloba 50, Berenguer J, Guisán JM, López-Gallego F (2011) Modulation of the distribution of small proteins within porous matrixes by smart-control of the immobilization rate. J Biotechnol 155:412–420
  12. Zheng Y-G, Yin H-H, Yu D-F, Chen X, Tang X-L, Zhang X-J, Xue Y-P, Wang Y-J, Liu Z-Q (2017) Recent advances in biotechnological applications of alcohol dehydrogenases. Appl Microbiol Biotechnol 101:987–1001
  13. van der Donk WA, Zhao H (2003) Recent developments in pyridine nucleotide regeneration. Curr Opin Biotechnol 14:421–426
  14. Bolivar JM, Cava F, Mateo C, Rocha-Martin J, Guisan JM, Berenguer J, Fernandez-Lafuente R (2008) Immobilization-stabilization of a new recombinant glutamate dehydrogenase from Thermus thermophilus. Appl Microbiol Biotechnol 80:49–58
  15. Rocha-Martín J, Vega D, Bolivar JM, Hidalgo A, Berenguer J, Guisán JM, López-Gallego F (2012) Characterization and further stabilization of a new anti-prelog specific booze dehydrogenase from Thermus thermophilus HB27 for asymmetric reduction of carbonyl compounds. Bioresour Technol 103:343–350
  16. Mateo C, Bolivar JM, Godoy CA, Rocha-Martin J, Pessela BC, Curiel JA, Muñoz R, Guisan JM, Fernández-Lorente G (2010) Improvement of enzyme backdrop with a two-step immobilizaton process on novel heterofunctional supports. Biomacromolecules 11:3112–3117

Figures (0) & Videos (0)

Citations (2)

Keywords

Techniques:

Ultrafiltration, Confocal Microscopy, IMAC, HPLC, Cross-linking

Models:

Thermus thermophilus HB27, Escherichia coli

Others:

Enzymes, Immobilization, Co-localization, Porous materials, Cofactor regeneration, Heterogeneous biocatalysis

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Source: https://experiments.springernature.com/articles/10.1007/978-1-0716-0215-7_19

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