Study of Molecular Conformation and Activity-Related Properties of Lipase Immobilized onto Core–Shell Structured Polyacrylic Acid-Coated Magnetic Silica Nanocomposite Particles

Esmaeilnejad-Ahranjani, Parvaneh; Kazemeini, Mohammad; Singh, Gurvinder; Arpanaei, Ayyoob

doi:10.1021/acs.langmuir.5b03614

Cited by 56 publications

(31 citation statements)

References 48 publications

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“…Afterwards, powder X-ray diffraction (PXRD) was conducted to characterize the immobilized enzyme ( Figure 2). All diffraction peaks indicated the presence of magnetite nanoparticles with an inverse spinel phase in the core of the nanoparticles, which is consistent with a previous report [21]. Through the comparison of these PXRD patterns, the crystal structure of the Fe 3 O 4 nanoparticles did not suffer any changes upon coating with polydopamine shell and enzyme immobilization.…”

Section: Characterization Of Immobilized Lipase Qlm On Polydopamine-csupporting

confidence: 89%

“…Arpanaei et al once constructed a poly(acrylic acid)-coated Fe 3 O 4 cluster@SiO 2 for lipase immobilization, in which complicated procedures were performed through the covalent attachment via N-(3-dimethyl aminopropyl)-N-ethyl carbodiimide hydrochloride (EDC) and N-hydroxysuccinimide (NHS) chemistries [21]. Compared with the polymeric layer, the reaction between the polydopamine layer and the lipase was spontaneous and rapid, leading to the enzyme immobilization on Fe 3 O 4 nanoparticles soon after mixing.…”

Section: Characterization Of Immobilized Lipase Qlm On Polydopamine-cmentioning

confidence: 99%

“…Typical strategies for immobilizing lipase on iron oxide nanoparticles have been dependent on surface grafting through low molecular weight linkers or polymers harboring amino or epoxy groups, which would achieve the immobilization of lipases in a covalent manner [16,17]. However, their applications have been limited by the agglomeration into bigger objects and the sensitivity to acidic and oxidative conditions [18][19][20][21][22]. Additionally, the activity of lipases decreased significantly upon immobilization owing to the influence on enzyme conformation or the access of substrates to the enzyme's active site [23].…”

Section: Introductionmentioning

confidence: 99%

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Immobilization of Thermostable Lipase QLM on Core-Shell Structured Polydopamine-Coated Fe3O4 Nanoparticles

et al. 2017

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Abstract:Here, core-shell structured polydopamine-coated Fe 3 O 4 nanoparticles were constructed to immobilize thermostable lipase QLM from Alcaligenes sp. Systematical characterization indicated that lipase QLM was successfully immobilized on the surface of nanoparticles with an enzyme loading of 21.4 ± 1.47 mg/g immobilized enzyme. Then, the immobilized enzyme was demonstrated to possess favorable catalytic activity and stability in the ester hydrolysis, using p-nitrophenyl caprylate as the substrate. Further, it was successfully employed in the kinetic resolution of (R, S)-2-octanol, and satisfactory enantioselectivity and recyclability could be obtained with an enantiomeric ratio (E) of 8-15 over 10 cycle reactions. Thus, core-shell structured polydopamine-coated Fe 3 O 4 nanoparticles can be potentially used as a carrier for enzyme immobilization to improve their activity, stability, and reusability, which is beneficial for constructing efficient catalysts for industrial biocatalysis.

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Section: Characterization Of Immobilized Lipase Qlm On Polydopamine-csupporting

confidence: 89%

Section: Characterization Of Immobilized Lipase Qlm On Polydopamine-cmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Immobilization of Thermostable Lipase QLM on Core-Shell Structured Polydopamine-Coated Fe3O4 Nanoparticles

et al. 2017

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“…Here, the partial structural loss of immobilized lipase can be correlated to the involvement of surface carboxyl group of enzyme in covalent linkage that lead to alteration of hydrogen bond among functional groups to some extent and leading to smaller change in enzyme structure. 53,54 Fluorescence analysis…”

Section: Structural Characterization Of Aunps-nh 2 -Lipase CD Analysismentioning

confidence: 99%

Facile fabrication of lipase to amine functionalized gold nanoparticles to enhance stability and activity

2017

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Among various techniques of immobilization, EDC/NHS cross linking is a simple and single step process for covalent coupling between enzymes and nanoparticles. Here we describe immobilization of lipase on amine functionalized gold nanoparticles (AuNPs-NH 2 ) to attain enhanced activity and stability. To achieve a suitable orientation, it is necessary to understand the contribution of different functional groups on the enzyme's surface. Therefore, the crystal structure of lipase was analyzed using a computational method (PyMOL) to find the exposed acidic amino acid residues that can be exploited for conjugation. Confirmation of conjugation (AuNP-NH 2 -lipase) was determined by various techniques such as agarose gel electrophoresis, zeta measurement, FTIR-spectroscopy and TEM. Further, catalytic parameters (V max , K M,app , K cat , and K cat /K M,app ) have been studied to establish activity enhancement upon immobilization. The data also suggested that, AuNP-NH 2 -lipase has desirable improved parameters such as temperature and storage stability. The thermodynamic parameters for the kinetics of deactivation IntroductionEnzymes have wide application in food, detergent, medicine, diagnostics, energy and many other industrial sectors due to their catalytic activity under mild conditions, specicity, costeffectiveness and greener production conditions. 1,2 However industrial application of free enzymes is restricted due to high lability, poor stability and problems in their recovery and reuse. 3Immobilization is the effective way to overcome these limitations and extend the horizon of their applications.4 Various methods of immobilization include physical adsorption, ionic interaction, covalent bonding between support and enzyme or entrapment within the different matrices.5 Hydrophobic interactions, ionic interactions, hydrogen bonds, van der Waals interactions and solvation are the major forces responsible for non-covalent interactions. Except for covalent attachment, the above mentioned techniques mainly rely on weak interactions, therefore enzymes are prone to detachment from the support surface with time. Covalent bonding mediated immobilization helps in improving enzyme activity at the cost of loss of conformational integrity.6 A very simple method of crosslinking biomolecules to nanoparticles relies on EDC/NHS coupling in which carbodiimides mediate formation of amide bond between carboxy and amine groups.7 High solubility in water, ease to remove byproducts, zero length cross linking molecule and single step reaction provides an edge over other methods in EDC/NHS coupling.8 Several enzymes have been conjugated using this strategy, but they lack in their structure based consideration prior to immobilization. Improper orientation aer immobilization ultimately affects activity; therefore, it is highly essential to understand the structure of protein before immobilization. One of the rationale approaches is to exploit specic surface amino acids for conjugating enzymes with the nanosurface so that the catalytic p...

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“…56 Lipase generally shows a severe decrease in catalytic activity after immobilization which rises from the increased mass-transfer limitations between the enzyme and substrate, the fractional blocking of enzyme active sites or alternation of native enzyme structure during the immobilization process. [110][111][112][113] Interfacial activation concept has developed as an elegant approach to enhance the activity of immobilized lipase over the recent years. 114 It has been well-documented that the lipase molecule possesses a flexible configuration in which the active site is covered by a hydrophobic and movable region of the lipase molecule, called the "lid".…”

Section: Interfacial Activationmentioning

confidence: 99%

Synthesis of novel mesoporous materials as high-performance adsorbents

Kalantari¹

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The rapid growth of nanotechnology has brought in advanced technologies. One demonstrative case is nanoadsorbents which are defined as nanostructured materials with a high affinity to adsorb substances. Owing to their exclusive features such as adjustable structural properties, tunable surface chemistry, and short diffusion distance, nanoadsorbents have shown great promise in catalysis and water treatment to host various species. However, the effectiveness of typical nanoadsorbents is generally restricted by the inadequate textural properties or functionalities. Therefore, it is essential to develop highly effective nanostructured adsorbents to host various substances. Polycyclic aromatic hydrocarbons (PAHs) are an important family of organic pollutants composed of fused benzene rings. They have been categorized as priority pollutants due to their toxic, mutagenic, and carcinogenic properties. Adsorption has recently found to be a promising technology to remove PAHs in a cost-effective and green manner. Nonetheless, the performance of proposed adsorbents is typically poor because of the inadequate textural and functional properties. Therefore, developing novel adsorbents with tailored features for superior removal of PAHs is crucial. Lipase has found key industrial applications as shows astonishing catalytic performance in a green manner. However, the effectiveness of free lipase is significantly reduced by its limited activity and low stability. Immobilization of lipase on nanomaterials is a promising approach to improve lipase catalytic performance. Nonetheless, lipase shows a severe decrease in catalytic activity after immobilization. Thus, developing an effective approach to improve the catalytic performance of lipase remains an ongoing challenge. This project emphases on the synthesis of innovative mesoporous materials with rationally designed textural properties and functionality as high-performance adsorbents. The advanced nanoadsorbents have shown excellent performances to host various species with significantly improved adsorption performance. The main achievements in this thesis are listed below. In the first part of this thesis, organic-based nanomaterials were developed for adsorption of PAHs. First, rattle-type magnetic mesoporous hollow carbon (RMMHC) were synthesized through a surfactant-free synthesis approach. It was demonstrated that the textural properties of RMMHC nanoparticles can be adjusted by changing the carbonization temperature. The adsorption capacity of the optimized sample towards di (2-ethylhexyl) phthalate reaches as high as 783.1 mg g-1 while retaining 89% of its initial adsorption IV Declaration by author This thesis is composed of my original work, and contains no material previously published or written by another person except where due reference has been made in the text. I have clearly stated the contribution by others to jointly-authored works that I have included in my thesis. I have clearly stated the contribution of others to my thesis as a whole, including statistical a...

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Study of Molecular Conformation and Activity-Related Properties of Lipase Immobilized onto Core–Shell Structured Polyacrylic Acid-Coated Magnetic Silica Nanocomposite Particles

Cited by 56 publications

References 48 publications

Immobilization of Thermostable Lipase QLM on Core-Shell Structured Polydopamine-Coated Fe3O4 Nanoparticles

Immobilization of Thermostable Lipase QLM on Core-Shell Structured Polydopamine-Coated Fe3O4 Nanoparticles

Facile fabrication of lipase to amine functionalized gold nanoparticles to enhance stability and activity

Synthesis of novel mesoporous materials as high-performance adsorbents

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