Multienzymatic Catalysis and Enzyme Co-Immobilization

Fernandez-Lafuente, Roberto

doi:10.3390/catal13121488

Cited by 1 publication

(1 citation statement)

References 41 publications

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“…The key benefits of enzyme immobilization methods include (i) easy biocatalyst separation; (ii) abatement of downstream processing; (iii) superior recycling of biocatalysts; (iv) improved stability, relative to higher temperatures, pH, or solvents; and (v) feasibility for use with other enzymes via co-immobilization [ 5 , 6 , 7 ]. Significant disadvantages include (i) lower activity and reaction rates compared to free enzymes, (ii) surplus cost of immobilization supports, (iii) fouling, and (iv) disposal of exhausted immobilized biocatalysts through incineration or environmental issues due to material toxicity [ 1 , 4 , 8 , 9 , 10 ]. Such issues can potentially be solved by the selective use of immobilization methods, supports, and protein engineering-based approaches in specific enzyme immobilization [ 11 ].…”

Section: Introductionmentioning

confidence: 99%

Sequential Co-Immobilization of Enzymes on Magnetic Nanoparticles for Efficient l-Xylulose Production

Patel,

Gupta,

Karuppanan

et al. 2024

IJMS

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Multi-enzymatic strategies have shown improvement in bioconversion during cofactor regeneration. In this study, purified l-arabinitol 4-dehydrogenase (LAD) and nicotinamide adenine dinucleotide oxidase (Nox) were immobilized via individual, mixed, and sequential co-immobilization approaches on magnetic nanoparticles, and were evaluated to enhance the conversion of l-arabinitol to l-xylulose. Initially, the immobilization of LAD or Nox on the nanoparticles resulted in a maximum immobilization yield and relative activity of 91.4% and 98.8%, respectively. The immobilized enzymes showed better pH and temperature profiles than the corresponding free enzymes. Furthermore, co-immobilization of these enzymes via mixed and sequential methods resulted in high loadings of 114 and 122 mg/g of support, respectively. Sequential co-immobilization of these enzymes proved more beneficial for higher conversion than mixed co-immobilization because of better retaining Nox residual activity. Sequentially co-immobilized enzymes showed a high relative conversion yield with broader pH, temperature, and storage stability profiles than the controls, along with high reusability. To the best of our knowledge, this is the first report on the mixed or sequential co-immobilization of LAD and Nox on magnetic nanoparticles for l-xylulose production. This finding suggests that selecting a sequential co-immobilization strategy is more beneficial than using individual or mixed co-immobilized enzymes on magnetic nanoparticles for enhancing conversion applications.

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