The influence of synthesis conditions on enzymatic activity of enzyme-inorganic hybrid nanoflowers

Li, Yue; Fei, Xu; Liang, Liwen; Tian, Jing; Xu, Ling; Wang, Xiuying; Wang, Yi

doi:10.1016/j.molcatb.2016.08.001

Cited by 58 publications

(22 citation statements)

References 43 publications

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“…This effect may be explained by the increase of nucleation sites, i.e., imidazole groups confined on the surface of the protein, that will induce a faster mineralization on individual particles. Indeed, similar results are reported in the synthesis of protein‐inorganic nanoflowers: the higher concentration of free protein is seeded,—which, in turn, means the overall increase of nucleation points—the smaller hybrids are achieved …”

Section: Resultssupporting

confidence: 74%

Imidazole‐Grafted Nanogels for the Fabrication of Organic–Inorganic Protein Hybrids

Rodriguez‐Abetxuko

Morant‐Miñana

López‐Gallego

et al. 2018

Adv Funct Materials

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Here, a platform for the development of highly responsive organicinorganic enzyme hybrids is provided. The approach entails a first step of protein engineering, in which individual enzymes are armored with a porous nanogel decorated with imidazole motifs. In a second step, by mimicking the biomineralization mechanism, the assembly of the imidazole nanogels with CuSO 4 and phosphate salts is triggered. A full characterization of the new composites reveals the first reported example in which the assembly mechanism is triggered by the sum of Cu(II)-imidazole interaction and Cu 3 (PO 4 ) 2 inorganic salt formation. It is demonstrated that the organic component of the hybrids, namely the imidazole-modified polyacrylamide hydrogel, provides a favorable spatial distribution for the enzyme. This results in enhanced conversion rates, robustness of the composite at low pH values, and a remarkable thermal stability at 65 °C, exhibiting 400% of the activity of the mineralized enzyme lacking the organic constituent. Importantly, unlike in previous works, the protocol applies to the use of a broad range of transition metal cations (including mono-, di-, and trivalent cations) to trigger the mineralization mechanism, which eventually broadens the chemical and structural diversity of organic-inorganic protein hybrids.

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Section: Resultssupporting

confidence: 74%

Imidazole‐Grafted Nanogels for the Fabrication of Organic–Inorganic Protein Hybrids

Rodriguez‐Abetxuko

Morant‐Miñana

López‐Gallego

et al. 2018

Adv Funct Materials

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“…202,203 This method has motivated a major interest in exploiting them as a potential matrix for biomolecule immobilization because of their simple synthesis, high efficiency, great promise of enhancing biomolecule stability, activity and even selectivity. [204][205][206] The formation of the organic-inorganic hybrid nanoflowers comprehend the following steps: nucleation, growth and completion. 207,208 The formation of hybrid nanoflowers is shown in Figure 1 (I).…”

Section: Organic -Inorganic Hybrid Nanoflowermentioning

confidence: 99%

Design of Immobilized Enzyme Biocatalysts: Drawbacks and Opportunities

Reis

Sousa

Serpa

et al. 2019

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The enzymatic processes are increasingly highlights, especially in the synthesis of chemical products with high added value. The enzyme immobilization can improve industrial biocatalytic processes. The immobilization of enzymes provides the production of efficient, stable biocatalysts, possibility of reuse and easy purification of the products, when compared to the free enzymes. There is a growing research for more efficient methods of enzyme immobilization. In this context, the choice of support and immobilization strategy can significantly improve the final enzymatic properties. In this review paper, we aimed to discuss the versatility of biocatalysts immobilized enzymes design, focusing on the opportunities and disadvantages for each method presented. They discussed the recent development of enzyme immobilization methods and applications relating the final properties of the produced biocatalysts with the desired goals.

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“…Several authors have suggested that an increase of the net negative charge of the enzyme molecules at higher pH had a positive effect on the binding affinity of metal ions, promoting biomineralization by increasing nucleation points [ 26 ]. Furthermore, previous works have reported that an increase in pH yielded less ordered and less compact nanoflower structures [ 26 , 27 ]. This could favor the diffusion of substrates and products in and out from the biocatalyst, explaining the increase in specific activity at higher pHs.…”

Section: Resultsmentioning

confidence: 99%

Development of a Hybrid Bioinorganic Nanobiocatalyst: Remarkable Impact of the Immobilization Conditions on Activity and Stability of β-Galactosidase

et al. 2021

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Hybrid bioinorganic biocatalysts have received much attention due to their simple synthesis, high efficiency, and structural features that favor enzyme activity and stability. The present work introduces a biomineralization strategy for the formation of hybrid nanocrystals from β-galactosidase. The effects of the immobilization conditions were studied, identifying the important effect of metal ions and pH on the immobilization yield and the recovered activity. For a deeper understanding of the biomineralization process, an in silico study was carried out to identify the ion binding sites at the different conditions. The selected β-galactosidase nanocrystals showed high specific activity (35,000 IU/g biocatalyst) and remarkable thermal stability with a half-life 11 times higher than the soluble enzyme. The nanobiocatalyst was successfully tested for the synthesis of galacto-oligosaccharides, achieving an outstanding performance, showing no signs of diffusional limitations. Thus, a new, simple, biocompatible and inexpensive nanobiocatalyst was produced with high enzyme recovery (82%), exhibiting high specific activity and high stability, with promising industrial applications.

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The influence of synthesis conditions on enzymatic activity of enzyme-inorganic hybrid nanoflowers

Cited by 58 publications

References 43 publications

Imidazole‐Grafted Nanogels for the Fabrication of Organic–Inorganic Protein Hybrids

Imidazole‐Grafted Nanogels for the Fabrication of Organic–Inorganic Protein Hybrids

Design of Immobilized Enzyme Biocatalysts: Drawbacks and Opportunities

Development of a Hybrid Bioinorganic Nanobiocatalyst: Remarkable Impact of the Immobilization Conditions on Activity and Stability of β-Galactosidase

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