Lipase immobilization onto polyethylenimine coated magnetic nanoparticles assisted by divalent metal chelated ions

Motevalizadeh, Seyed Farshad; Khoobi, Mehdi; Sadighi, Armin; Khalilvand‐Sedagheh, Masoud; Pazhouhandeh, Mehrdad; Ramazani, Ali; Faramarzi, Mohammad Ali; Shafiee, Abbas

doi:10.1016/j.molcatb.2015.06.013

Cited by 77 publications

(34 citation statements)

References 60 publications

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“…Magnetic nanoparticles (MNPs) are widely used as supports for physical and chemical biomolecule immobilization [15][16][17], with usually a high load of ligands [18][19][20][21]. However, pure magnetite has a poor colloidal stability, particularly in neutral pH, so it needs stabilization and surface modification [22].…”

Section: Introductionmentioning

confidence: 99%

Chitosan–Collagen Coated Magnetic Nanoparticles for Lipase Immobilization—New Type of “Enzyme Friendly” Polymer Shell Crosslinking with Squaric Acid

Ziegler-Borowska

Chełminiak-Dudkiewicz

Siódmiak

et al. 2017

Catalysts

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This article presents a novel route for crosslinking a polysaccharide and polysaccharide/protein shell coated on magnetic nanoparticles (MNPs) surface via condensation reaction with squaric acid (SqA). The syntheses of four new types of collagen-, chitosan-, and chitosan-collagen coated magnetic nanoparticles as supports for enzyme immobilization have been done. Structure and morphology of prepared new materials were characterized by attenuated total reflectance Fourier-transform infrared (ATR-FTIR), XRD, and TEM analysis. Next, the immobilization of lipase from Candida rugosa was performed on the nanoparticles surface via N-(3-dimethylaminopropyl)-N -ethylcarbodiimide hydrochloride (EDC)/N-hydroxy-succinimide (NHS) mechanism. The best results of lipase activity recovery and specific activities were observed for nanoparticles with polymer shell crosslinked via a novel procedure with squaric acid. The specific activity for lipase immobilized on materials crosslinked with SqA (52 U/mg lipase) was about 2-fold higher than for enzyme immobilized on MNPs with glutaraldehyde addition (26 U/mg lipase). Moreover, a little hyperactivation of lipase immobilized on nanoparticles with SqA was observed (104% and 112%).

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Section: Introductionmentioning

confidence: 99%

Chitosan–Collagen Coated Magnetic Nanoparticles for Lipase Immobilization—New Type of “Enzyme Friendly” Polymer Shell Crosslinking with Squaric Acid

Ziegler-Borowska

Chełminiak-Dudkiewicz

Siódmiak

et al. 2017

Catalysts

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“…Generally, dissolved enzymes tend to gradually lose their activity over time. To prevent such reduction of enzyme activity as time elapses, immobilization is advocated as one of the best applicable protective methods . To investigate the storage stability of free and immobilized BM3, they were both stored at 4 °C for four weeks.…”

Section: Resultsmentioning

confidence: 99%

Covalent immobilization of cytochrome P450 BM3 (R966D/W1046S) on glutaraldehyde activated SPIONs

et al. 2018

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Selective hydroxylation of the C‐H bond of saturated hydrocarbon chains at room temperature is the signature of an invaluable biocatalyst, cytochrome P450 BM3 from Bacillus megaterium. Despite this remarkable ability, because of the enzyme's inherent low stability and dependence on electron supply by expensive NADPH, developing stable and economic BM3 systems is a challenging subject. To improve BM3 stability, facilitate its reuse, and reduce the process cost, this study suggests covalent immobilization of R966D/W1046S P450 BM3 on glutaraldehyde pre‐activated super paramagnetic iron oxide nanoparticles (SPIONs). This double mutant consumes less expensive cofactors like NADH and BNAH and its immobilization on magnetic support facilitates its separation and reuse. Free and immobilized enzyme performances were evaluated by 10‐pNCA hydroxylation and BM3 selectivity (hydroxylation at ω (1–3) positions of a fatty acid) was confirmed in a reaction involving myristic acid. The enzyme activity recovery was up to 60 % with 100 % enzyme binding efficiency. BM3‐SPIONs were easily separated from the reaction medium by applying a magnet, and recycled for 5 times, after which they could still present half of their initial activity. The enzyme storage stability was significantly improved: after one month of storage at 4 °C, the immobilized enzyme showed 80 % residual activity toward NADH while the soluble enzyme was inactive after a week. Binding an enzyme to fabricated SPIONs is a promising technique to increase enzyme stability and prevent downstream contamination in biocatalytic processes. In this context, BM3‐SPIONs can be a practical model system in cost‐effective large‐scale applications of such enzymes.

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“…The use of magnetic supports coated with ligands or peptides for interaction with the tagged proteins allows facile separation of the supported catalyst for reuse. Recently, lipases from Thermomyces lanuginosus and Rhizopus oryzae have been immobilized on magnetic nanoparticles with retention of activity and increase in stability relative to the free enzyme; this also allowed the facile separation and recovery of the enzyme . Lipases have also previously been immobilized on magnetic lauric acid‐stabilized particles for the resolution of menthol .…”

Section: Enabling Technologymentioning

confidence: 99%

The Impact of Recent Developments in Technologies which Enable the Increased Use of Biocatalysts

Foley

Maguire

2019

Eur J Org Chem

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While biocatalytic transformations are very powerful in enantioselective synthesis, frequently occurring under mild conditions, and proceed with extraordinary selectivity, there are practical challenges associated with the use of biocatalysis, such as limited substrate scope, stability, and reusability. Recent technological developments, for example immobilization, continuous flow, and molecular biology, all contribute towards enhancing the use of enzymes in synthesis.

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Lipase immobilization onto polyethylenimine coated magnetic nanoparticles assisted by divalent metal chelated ions

Cited by 77 publications

References 60 publications

Chitosan–Collagen Coated Magnetic Nanoparticles for Lipase Immobilization—New Type of “Enzyme Friendly” Polymer Shell Crosslinking with Squaric Acid

Chitosan–Collagen Coated Magnetic Nanoparticles for Lipase Immobilization—New Type of “Enzyme Friendly” Polymer Shell Crosslinking with Squaric Acid

Covalent immobilization of cytochrome P450 BM3 (R966D/W1046S) on glutaraldehyde activated SPIONs

The Impact of Recent Developments in Technologies which Enable the Increased Use of Biocatalysts

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