Development of l-asparaginase@hybrid Nanoflowers (ASNase@HNFs) Reactor System with Enhanced Enzymatic Reusability and Stability

Noma, Samir Abbas Ali; Yılmaz, Burcu Somtürk; Ulu, Ahmet; Özdemir, Nalan; Ateş, Burhan

doi:10.1007/s10562-020-03362-1

Cited by 23 publications

(9 citation statements)

References 46 publications

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“…The results show that the nanoflowers were not well developed at the lowest concentrations of phosphate buffer and pH values. Consequently, the nanoflowers present in the phosphate buffer at a concentration above 50 mM have more developed structures, especially at higher pHs, as explained in the literature (pH 7, 7.4, and 8) [23,25]. Therefore, the higher buffer the concentration, the higher the density of the petals in the nanoflowers in this analysis.…”

Section: Morphology Of Hnf-lipasesupporting

confidence: 57%

“…In the region of 1200-950 (cm −1 ), there is a robust characteristic peak that can be attributed to vibrations and elongations of P-O, found in the presence of phosphate groups [12,21,38]. The relatively small band at 530-670 (cm −1 ) was likely the phosphorus bridge bending vibrations, such as O=P-O, contributing to the phosphate groups [25,39]. Characteristic peaks are found due to the PO 4 −3 vibration, evidencing the existence of PBS-Cu 2+ in the analyzed nanoparticle (Figure 6).…”

Section: Ftir Of Hnf-lipasementioning

confidence: 99%

“…This increased concentration of anions and cations causes more molecular interactions between the compounds [27]. Thus, to expand the study on the influence of anions and cations on the activity of the biocatalyst, the protocol was carried out for different pH values, 6, 7, 7.4, and 8, in various concentrations of phosphate buffer (10,25,50, and 100 mM), as shown in Figure 2. However, no precipitate formed at pH 5 and 9, resulting in no formation of hNF-lipase.…”

Section: Activity Of Hnf-lipasementioning

confidence: 99%

“…There are no more comprehensive studies on the influence of current interactions on the formation of hybrid lipase nanoflowers (hNF-lipase) across buffer concentrations and pH values. Literature studies have reported the influence of pH on nanoflowers [22,[24][25][26]. In this sense, the reactions utilized different pH values (5)(6)(7)(8)(9) and concentrations of phosphate buffer (10-100 mM) to evaluate the interaction for obtaining the nanoflower.…”

Section: Introductionmentioning

confidence: 99%

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Experimental and Computational Analysis of Synthesis Conditions of Hybrid Nanoflowers for Lipase Immobilization

Souza,

Santos,

Freitas

et al. 2024

Molecules

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This work presents a framework for evaluating hybrid nanoflowers using Burkholderia cepacia lipase. It was expanded on previous findings by testing lipase hybrid nanoflowers (hNF-lipase) formation over a wide range of pH values (5–9) and buffer concentrations (10–100 mM). The free enzyme activity was compared with that of hNF-lipase. The analysis, performed by molecular docking, described the effect of lipase interaction with copper ions. The morphological characterization of hNF-lipase was performed using scanning electron microscopy. Fourier Transform Infrared Spectroscopy performed the physical–chemical characterization. The results show that all hNF-lipase activity presented values higher than that of the free enzyme. Activity is higher at pH 7.4 and has the highest buffer concentration of 100 mM. Molecular docking analysis has been used to understand the effect of enzyme protonation on hNF-lipase formation and identify the main the main binding sites of the enzyme with copper ions. The hNF-lipase nanostructures show the shape of flowers in their micrographs from pH 6 to 8. The spectra of the nanoflowers present peaks typical of the amide regions I and II, current in lipase, and areas with P–O vibrations, confirming the presence of the phosphate group. Therefore, hNF-lipase is an efficient biocatalyst with increased catalytic activity, good nanostructure formation, and improved stability.

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Section: Morphology Of Hnf-lipasesupporting

confidence: 57%

Section: Ftir Of Hnf-lipasementioning

confidence: 99%

Section: Activity Of Hnf-lipasementioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Experimental and Computational Analysis of Synthesis Conditions of Hybrid Nanoflowers for Lipase Immobilization

Souza,

Santos,

Freitas

et al. 2024

Molecules

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“…Besides, around 600 cm –1 , C–H bond deformation or bending for alkynes may be indicated . For the HRP@Fe 3 O 4 –NH 2 /hNFs, the Fe–O peak was observed at 555 cm –1 . − The strong bands at 1046 and 987 cm –1 were assigned to the Si–O–Si and Si–O stretching vibrations of APTES to the surface of magnetic NPs. , The absorption peaks at 964 cm –1 (symmetric stretching) and 623 cm –1 (bending) were ascribed to P–O vibrations and demonstrated the presence of phosphate groups. , In addition, the band around 1620 cm –1 was assigned to the presence of HRP. These results confirmed that Fe 3 O 4 –NH 2 /hNFs were successfully synthesized and HRP was immobilized on Fe 3 O 4 –NH 2 /hNFs.…”

Section: Resultsmentioning

confidence: 98%

Horseradish Peroxidase Immobilized onto Mesoporous Magnetic Hybrid Nanoflowers for Enzymatic Decolorization of Textile Dyes: A Highly Robust Bioreactor and Boosted Enzyme Stability

Bakar,

Akbulut,

Ulusal

et al. 2024

ACS Omega

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Recently, hybrid nanoflowers (hNFs), which are accepted as popular carrier supports in the development of enzyme immobilization strategies, have attracted much attention. In this study, the horseradish peroxidase (HRP) was immobilized to mesoporous magnetic Fe3O4–NH2 by forming Schiff base compounds and the HRP@Fe3O4–NH2/hNFs were then synthesized. Under optimal conditions, 95.0% of the available HRP was immobilized on the Fe3O4–NH2/hNFs. Structural morphology and characterization of synthesized HRP@Fe3O4–NH2/hNFs were investigated. The results demonstrated that the average size of HRP@Fe3O4–NH2/hNFs was determined to be around 220 nm. The ζ-potential and magnetic saturation values of HRP@Fe3O4–NH2/hNFs were −33.58 mV and ∼30 emu/g, respectively. Additionally, the optimum pH, optimum temperature, thermal stability, kinetic parameters, reusability, and storage stability were examined. It was observed that the optimum pH value shifted from 5.0 to pH 8.0 after immobilization, while the optimum temperature shifted from 30 to 80 °C. K m values were calculated to be 15.5502 and 7.6707 mM for free HRP and the HRP@Fe3O4–NH2/hNFs, respectively, and V max values were calculated to be 0.0701 and 0.0038 mM min–1. The low K m value observed after immobilization indicated that the affinity of HRP for its substrate increased. The HRP@Fe3O4–NH2/hNFs showed higher thermal stability than free HRP, and its residual activity after six usage cycles was approximately 45%. While free HRP lost all of its activity within 120 min at 65 °C, the HRP@Fe3O4–NH2/hNFs retained almost all of its activity during the 6 h incubation period at 80 °C. Most importantly, the HRP@Fe3O4–NH2/hNFs demonstrated good potential efficiency for the biodegradation of methyl orange, phenol red, and methylene blue dyes. The HRP@Fe3O4–NH2/hNFs were used for a total of 8 cycles to degrade methyl orange, phenol red, and methylene blue, and degradation of around 81, 96, and 56% was obtained in 8 h, respectively. Overall, we believe that the HRP@Fe3O4–NH2/hNFs reported in this work can be potentially used in various industrial and environmental applications, particularly for the biodegradation of recalcitrant compounds, such as textile dyes.

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Improved L‐Asparaginase Properties and Reusability by Immobilization onto Functionalized Carbon Xerogels

Barros,

Cristóvão,

Carneiro

et al. 2024

ChemPlusChem

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Enzyme immobilization can offer a range of significant advantages, including reusability, and increased selectivity, stability, and activity. In this work, a central composite design (CCD) of experiments and response surface methodology (RSM) were used to study, for the first time, the L‐asparaginase (ASNase) immobilization onto functionalized carbon xerogels (CXs). The best results were achieved using CXs obtained by hydrothermal oxidation with nitric acid and subsequent heat treatment in a nitrogen flow at 600 ºC (CX‐OX‐600). Under the optimal conditions (81 min of contact time, pH 6.2 and 0.36 g/L of ASNase), an immobilization yield (IY) of 100% and relative recovered activity (RRA) of 103% were achieved. The kinetic parameters obtained also indicate a 1.25‐fold increase in the affinity of ASNase towards the substrate after immobilization. Moreover, the immobilized enzyme retained 97% of its initial activity after 6 consecutive reaction cycles. All these outcomes confirm the promising properties of functionalized CXs as support for ASNase, bringing new insights into the development of an efficient, and stable immobilization platform for use in the pharmaceutical industry, food industry, and biosensors.

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Development of l-asparaginase@hybrid Nanoflowers (ASNase@HNFs) Reactor System with Enhanced Enzymatic Reusability and Stability

Cited by 23 publications

References 46 publications

Experimental and Computational Analysis of Synthesis Conditions of Hybrid Nanoflowers for Lipase Immobilization

Experimental and Computational Analysis of Synthesis Conditions of Hybrid Nanoflowers for Lipase Immobilization

Horseradish Peroxidase Immobilized onto Mesoporous Magnetic Hybrid Nanoflowers for Enzymatic Decolorization of Textile Dyes: A Highly Robust Bioreactor and Boosted Enzyme Stability

Improved L‐Asparaginase Properties and Reusability by Immobilization onto Functionalized Carbon Xerogels

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