Potential antioxidant activity of multienzymatically hydrolyzed corncob

Sandoval-Cárdenas, Diana Issell; Pérez, Ana Angélica Feregrino; Favela-Camacho, Sarai E.; Arredondo-Ochoa, Teresita; Escamilla‐García, Monserrat; Regalado‐González, Carlos; Amaro-Reyes, Aldo

doi:10.1007/s11756-021-00977-6

Cited by 4 publications

(4 citation statements)

References 38 publications

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“…No protein was detected in the supernatant, which confirmed the purely covalent immobilization of these enzymes on Fe 3 O 4 /APTES–GLA [ 5 , 34 ]. The spherical shape and size of nanoparticles, including magnetic supports, highly influenced enzyme immobilization properties such as IY and RA [ 17 , 35 , 36 ]. Previously, the covalent immobilization of LAD on various supports, including Anberlites, Eupergit, Duolite, and multi-wall carbon nanotubes, showed a lower IY than that of Fe 3 O 4 nanoparticles [ 36 ].…”

Section: Resultsmentioning

confidence: 99%

“…In the sequential co-immobilization of enzymes, the immobilization of Nox at the second stage on the initially immobilized LAD (IY and RA of 91.4% and 98.8%, respectively) showed an IY of 96.0%, with an overall loading of 122 mg (91.4 mg of LAD and 30.7 mg of Nox) per g of Fe 3 O 4 /APTES–GLA nanoparticles ( Table 3 ). Here, a minor alteration in the conversion efficiency of l -arabinitol to l -xylulose by mixed and sequential co-immobilization might be associated with different extents of steric hindrance in these co-immobilization procedures [ 15 , 35 ]. Previously, a lower IY of 83% was reported for xylose dehydrogenase (XDH) and alcohol dehydrogenase (ADH) co-immobilized at a ratio of 2:1 on magnetic silica nanoparticles [ 40 ].…”

Section: Resultsmentioning

confidence: 99%

“…Fe 3 O 4 @SiO 2 –NH 2 nanoparticles showed a low loading of 28 mg/g of support for the co-immobilization of glucose dehydrogenase and (R)-1-phenylethanol dehydrogenase [ 41 ]. In contrast, multi-enzyme (Endo-1,4-β-D-glucanase, xylanase, and amylase) immobilization in a spherical shape with a size of 25 nm Fe 3 O 4 nanoparticles-based synthesized magnetic composite offers a lower loading of 14.7 mg of soluble protein/g of support [ 35 ]. One advantage of immobilized enzymes is that their application offers minor risk of product contamination with negligible allergenicity [ 15 ].…”

Section: Resultsmentioning

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: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

See 1 more Smart Citation

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

Patel,

Gupta,

Karuppanan

et al. 2024

IJMS

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“…The interaction of surface functional groups of the composite along adsorbed Hg 2+ may form agglomerates, thus enhancing the surface roughness. In addition, the co-precipitation method for synthesis of Fe 3 O 4 nanoparticles used in this study has shown signals corresponding to the planes characteristic of Fe 3 O 4 and regular, defined, and polyhedral shapes, such as tetra-, hexa-, and octahedrons [ 22 , 40 ].…”

Section: Resultsmentioning

confidence: 99%

Sargassum@magnetite Composite EDTA-Functionalized for the Potential Removal of Mercury

et al. 2023

Self Cite

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Sargassum spp. affects the Caribbean shores; thus, its remotion or valorization is a priority. This work aimed to synthesize a low-cost magnetically retrievable Hg+2 adsorbent functionalized with ethylenediaminetetraacetic acid (EDTA) based on Sargassum. The Sargassum was solubilized to synthesize by co-precipitation a magnetic composite. A central composite design was assessed to maximize the adsorption of Hg+2. The solids yield magnetically attracted mass, and the saturation magnetizations of the functionalized composite were 60.1 ± 17.2%, 75.9 ± 6.6%, and 1.4 emu g−1. The functionalized magnetic composite yielded 29.8 ± 0.75 mg Hg+2 g−1 of chemisorption after 12 h, pH 5, and 25 °C achieving 75% Hg+2 adsorption after four reuse cycles. Crosslinking and functionalization with Fe3O4 and EDTA created differences in surface roughness as well as the thermal events of the composites. The Fe3O4@Sargassum@EDTA composite was a magnetically recovered biosorbent of Hg2+.

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Research Progress on Lignocellulosic Biomass Degradation Catalyzed by Enzymatic Nanomaterials

Luo

Liu

et al. 2022

Chemistry An Asian Journal

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Lignocellulose biomass (LCB) has extensive applications in many fields such as bioenergy, food, medicines, and raw materials for producing value-added products. One of the keys to efficient utilization of LCB is to obtain directly available oligo-and monomers (e. g., glucose). With the characteristics of easy recovery and separation, high efficiency, economy, and environmental protection, immobilized enzymes have been developed as heterogeneous catalysts to degrade LCB effectively. In this review, applications and mechanisms of LCB-degrading enzymes are discussed, and the nanomaterials and methods used to immobilize enzymes are also discussed. Finally, the research progress of lignocellulose biodegradation catalyzed by nano-enzymes was discussed.

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Potential antioxidant activity of multienzymatically hydrolyzed corncob

Cited by 4 publications

References 38 publications

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

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

Sargassum@magnetite Composite EDTA-Functionalized for the Potential Removal of Mercury

Research Progress on Lignocellulosic Biomass Degradation Catalyzed by Enzymatic Nanomaterials

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