Stability and enzyme activity of lysozyme in the presence of Fe3O4 nanoparticles

Shareghi, Behzad; Farhadian, Sadegh; Zamani, N.; Salavati‐Niasari, Masoud; Gholamrezaei, Sousan

doi:10.1007/s00706-015-1520-x

Cited by 31 publications

(14 citation statements)

References 55 publications

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“…Overall, this finding proposed the distinguished behavior of AuNP-IL2 and AuNP-IL3 in comparison to other AuNP-IL1 and AuNP-IL4. This work is also virtuously irrespective of the previous study in magnetic NPs, which quenched the fluorescence spectra of Lyz.…”

Section: Resultsmentioning

confidence: 64%

“…However, for the higher concentration (10 nM) of naked AuNPs, no endothermic peak for the heat capacity change of Lyz is observed, even after three repetitions. Although the thermal stability of Lyz at higher concentrations of naked AuNPs is undefined, the increment at a lower concentration is still more pronounced as compared to the effect of iron oxide magnetic NPs on Lyz, as shown by Shareghi et al…”

Section: Resultsmentioning

confidence: 97%

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Ionic Liquid-Modified Gold Nanoparticles for Enhancing Antimicrobial Activity and Thermal Stability of Enzymes

Kumar

Sindhu

Venkatesu

2021

ACS Appl. Nano Mater.

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The synthesis of nanoparticles using ionic liquids (ILs) has attracted intensive research; however, synthesis and surface tailoring of gold nanoparticles (AuNPs) using ILs for enzyme immobilization have not yet been reported. Herein, we synthesized the various IL-modified AuNPs using different ILs, which are having common cation 1-ethyl-3-methyl-imidazolium (EMIM) and variable anions [BF 4−1 (AuNP-IL1), (CH 3 OSO 3 ) −1 (AuNP-IL2), (CH 3 CH 2 OSO 3 ) −1 (AuNP-IL3), and Cl −1 (AuNP-IL4)] by reduction of gold salt. The formation of IL modified AuNPs has been confirmed using UV−vis, zeta-potential, FTIR, and transmission electron microscopy (TEM). Thereafter, the centrifuged IL-modified AuNPs are being immobilized with a lysozyme (Lyz) enzyme to evaluate the effect of different AuNP covering groups (capping agent and IL's anions) for Lyz microbial activity, thermal and structural stabilities through interaction studies, spectroscopic techniques, and morphology investigation by TEM. AuNP-IL1 has increased the microbial activity of Lyz up to 2.6 fold at the concentration of 4 nM, and AuNP-IL2 is highly efficient to dextrously preserve enzyme activity against packaging for 4 weeks. The higher Michaelis−Menten constant (K M ) has been observed for Lyz immobilized in the AuNP-IL2 due to higher binding with the AuNP-IL2. Apparently, the higher specific constant (K cat /K M ) of immobilized Lyz has been observed in the case of AuNP-IL3 and shows more specific binding of Lyz with this particular IL-mediated AuNPs. The significant thermal stability enhancement about 8.11 °C is observed for transition temperature (T m ) of Lyz in the presence of sulfur group-containing IL-modified AuNPs like AuNP-IL2 and AuNP-IL3, which depends on the specific interacting ability of these AuNPs with Lyz. Therefore, the study reveals the variant character of sulfur-containing IL-modified AuNPs for higher activity and thermal and structural stability of Lyz. Surprisingly, this has created a way to monitor sulfur and hydrophobic interactions on AuNPs for enzyme immobilization through means of controlling surface modifications and interactions.

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Section: Resultsmentioning

confidence: 64%

Section: Resultsmentioning

confidence: 97%

Ionic Liquid-Modified Gold Nanoparticles for Enhancing Antimicrobial Activity and Thermal Stability of Enzymes

Kumar

Sindhu

Venkatesu

2021

ACS Appl. Nano Mater.

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“…The results discussed in this paper demonstrate a strong stabilizing effect. While the conjugation with polymers or particles is a well-known approach to improve stability of enzymes, − our results show the stability of the conjugates for up to 115–150 °C, which significantly exceeds the thermal stability limits achieved with previously proposed stabilizing methods, ,, including the examples of enzyme conjugation methods tested on lysozyme, trypsin, organophosphorus hydrolase, human carbonic anhydrase II, and sarcosine oxidase …”

Section: Introductionmentioning

confidence: 63%

Thermal Stabilization of Enzymes with Molecular Brushes

et al. 2017

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Herein, we report a conjugation strategy, where we utilize a poly(ethylene oxide) cylindrical molecular brush architecture to design a self-assembled structure for thermal stabilization of enzymes. We demonstrate that the proposed architecture of the moderately stiff polymer ligand results in a significant improvement of biocatalytic activity and thermal stability of lysozyme and trypsin that retain their activity, even upon heating to 100 °C and above. The molecular brush is bound via epoxy functional groups to the amino groups of the lysine on the surface of the enzyme globule, promoting the formation of stiff and crowded cages around the enzymes and preventing the water molecules access to the enzyme and enzymes agglomeration. The molecular dynamic simulations show that the high concentration of poly(ethylene oxide) in the vicinity of the enzyme is critical for their stability. Monitoring of lysozyme–molecular brush conjugates for 6 and 12 months in lyophilized form and in solution, respectively, has shown that the conjugation does not compromise the shelf life of the enzyme.

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Section: Stability and Of Immobilized And Free Chitosanasesmentioning

confidence: 96%

“…The immobilized chitosanases exhibited better stability compared to free chitosanases. The results suggested that MNPs protected the enzyme from alkaline and acid to enhance the pH stability [26], which could widen its application in the industry. Sometimes in industrial applications, a higher reaction temperature can enhance the productivity [27], so the thermal stability of enzymes is important for its industrial application.…”

Section: Stability and Of Immobilized And Free Chitosanasesmentioning

confidence: 96%

Immobilization of Chitosanases onto Magnetic Nanoparticles to Enhance Enzyme Performance

et al. 2018

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In this study, chitosanase cloning from Streptomyces albolongus was fermented and purified by a Ni-NTA column. Fe3O4-SiO2 magnetite nanoparticles (MNPs) were synthesized by the co-precipitation method coating with silica via a sol-gel reaction and were then amino functioned by treating with 3-aminopropyltriethoxysilane. Chitosanases were immobilized onto the surface of MNPs by covalent bonding (MNPs@chitosanase). Transmission electron microscopy (TEM), Fourier transform infrared spectrometer (FT–IR), and magnetic measurements were used to illustrate the MNPs and immobilized chitosanase. The optimal conditions of immobilization were studied. The thermal, pH, and stabilities of immobilized chitosanase were tested and the results showed that the stabilities were significantly enhanced compared with free chitosanase. After being recycled 10 times, the residual activity of the immobilized chitosanase was 43.7% of the initial activity.

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Stability and enzyme activity of lysozyme in the presence of Fe3O4 nanoparticles

Cited by 31 publications

References 55 publications

Ionic Liquid-Modified Gold Nanoparticles for Enhancing Antimicrobial Activity and Thermal Stability of Enzymes

Ionic Liquid-Modified Gold Nanoparticles for Enhancing Antimicrobial Activity and Thermal Stability of Enzymes

Thermal Stabilization of Enzymes with Molecular Brushes

Immobilization of Chitosanases onto Magnetic Nanoparticles to Enhance Enzyme Performance

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