Coriolus versicolor laccase-based inorganic protein hybrid synthesis for application in biomass saccharification to enhance biological production of hydrogen and ethanol

Patel, Sanjay K.S.; Gupta, Rahul; Kim, In-Won; Lee, Jung-Kul

doi:10.1016/j.enzmictec.2023.110301

Cited by 8 publications

(13 citation statements)

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“…The nanoparticles (200 mg) were washed and functionalized with GLA (1 M) for 2 h at room temperature to provide aldehyde groups on their surfaces, as previously described [ 6 ]. APTES activation of nanoparticle surfaces was evaluated in toluene supplemented with APTES (2%, v / v ) at room temperature for 12 h [ 33 ].…”

Section: Methodsmentioning

confidence: 99%

“…Unbound enzymes were separated in the supernatant by centrifugation for 10 min at 10,000× g (4 °C). The protein concentration in the supernatant was measured using the Bradford method [ 6 ]. The IY and RA were calculated as follows: IY (%) = ratio of immobilized enzyme to added enzyme × 100, RA (%) = ratio of immobilized enzyme to free enzyme activity × 100.…”

Section: Methodsmentioning

confidence: 99%

“…The initial conversion rate was considered 100%. Furthermore, the leaching (%) of enzymes was measured as the ratio of total protein content in the supernatant to the initial enzymes bound on the nanoparticles × 100 [ 6 ].…”

Section: Methodsmentioning

confidence: 99%

“…The presence of His-tagged recombinant enzymes is helpful for easy purification and immobilization, especially in affinity-based systems [ 1 , 3 ]. Various enzymatic immobilization procedures have been demonstrated, including (i) encapsulation, (ii) adsorption on supports, (iii) covalent immobilization, (iv) cross-linking using linkers such as glutaraldehyde (GLA), or combinations of these methods, such as covalent immobilization followed by cross-linking [ 4 , 5 , 6 , 7 ]. Each method has its own advantages and disadvantages for the immobilization of certain enzymes.…”

Section: Introductionmentioning

confidence: 99%

“…Each method has its own advantages and disadvantages for the immobilization of certain enzymes. 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 ].…”

Section: Introductionmentioning

confidence: 99%

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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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Section: Methodsmentioning

confidence: 99%