Immobilization of cellulase enzyme on superparamagnetic nanoparticles and determination of its activity and stability

Khoshnevisan, Kamyar; Bordbar, Abdol‐Khalegh; Zare, Davood; Davoodi, Daryoush; Noruzi, Masumeh; Barkhi, Mohammad; Tabatabaei, Meisam

doi:10.1016/j.cej.2011.04.039

Cited by 207 publications

(115 citation statements)

References 27 publications

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“…The free enzyme and the enzyme-MNP conjugates all displayed their best activity at 50°C ( Figure S7). This is in agreement with previous reports (Khoshnevisan et al 2011) and the magnitude of pigment extraction mediated by covalently conjugated nanobiocatalyst was high than that obtained via the free enzyme. The efficacy of uptake of the pigments released from orange peel by different solvents post-treatment with cellulase/pectinase-MNPs was also investigated.…”

Section: Optimization Of Parameters For Extractionsupporting

confidence: 83%

“…The loading efficiencies of cellulase and pectinase on iron oxide MNPs were found to be 78 % for chemically attached and 52 % for physically adsorbed. These loading efficiencies are comparable to previous reports where 95 % binding efficiency of cellulase on MNPs have been reported (Khoshnevisan et al 2011). The extraction of pigments from orange peels was followed by UV-visible spectroscopy that have been previously used for inferring the presence of specific carotenoids (Wrolstad et al 2005).…”

Section: Extraction Of Pigments From Orange Peelsupporting

confidence: 71%

“…The binding of cellulase/pectinase to Fe 3 O 4 nanoparticles was investigated by FTIR spectroscopy. As shown in Figure S4, the characteristic IR frequencies of the enzyme at 1550 and 1410 cm -1 were also observed in the APTES-linked samples suggesting attachment of enzymes to Fe 3 O 4 nanoparticles (Khoshnevisan et al 2011). High Resolution Transmission Electron Microscopy (HR-TEM) was used to study the shape of bare and enzyme functionalized MNPs.…”

Section: Resultsmentioning

confidence: 99%

“…We have developed stable iron oxide magnetic nano particles (MNPs) with size in the range of 60-110 nm. The hydrolytic enzymes cellulase and pectinase are immobilised on the magnetic iron oxide nano particles via reported conjugation strategies (Jordan et al 2011;Khoshnevisan et al 2011). The size and morphology of the enzyme-nanoparticle constructs were characterised by Atomic Force Microscopy (AFM), X-Ray Diffraction (XRD) and Transmission Electron Microscopy (TEM).…”

Section: Introductionmentioning

confidence: 99%

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Reusable nanobiocatalysts for the efficient extraction of pigments from orange peel

et al. 2016

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Nagpur mandarin orange (Citrus reticulata) peels were subjected to treatment with nanobiocatalysts in the form of cellulase and pectinase immobilized magnetic nanoparticles (MNPs). MNPs (Fe 3 O 4 ) with average diameter in range of 40-90 nm were immobilized with cellulase and pectinase through APTES and glutaraldehyde. Treatment followed by extraction into organic solvents resulted in 8-9 fold increase in extraction of carotenoidic pigments compared to use of free enzymes. Optimum pH and temperature for the process were determined to be 5.0 and 50°C, respectively. The nanobiocatalysts could be reused across three cycles with only 15 % drop in yield per cycle. Dinitrosalicylic acid assays showed that superior peel hydrolysis also led to greatest extent of pigment extraction.

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Section: Optimization Of Parameters For Extractionsupporting

confidence: 83%

Section: Extraction Of Pigments From Orange Peelsupporting

confidence: 71%

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Reusable nanobiocatalysts for the efficient extraction of pigments from orange peel

et al. 2016

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“…4 mL (0.5 mg/mL) of HRP enzyme solution was then added to glutaraldehyde treated MNPs in 6 mL of phosphate buffer and stirred gently for 2 -3 h to immobilize the enzyme [22][23][24]. The immobilized enzyme solution was stored in buffer solution at 4˚C until use.…”

Section: Immobilization Of Hrp Enzyme Onto Magnetic Nanoparticles Andmentioning

confidence: 99%

A Green Approach towards the Synthesis of Enantio Pure Diols Using Horse Radish Peroxidase Enzyme Immobilized on Magnetic Nanoparticles

Deepthi¹,

Prasad²,

Reddy³

et al. 2014

GSC

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Enantiopure epoxides and their corresponding chiral vicinal diols serve as valuable intermediates in the synthesis of biologically active pharma and agro-compounds and also value added fine chemicals. Biocatalysts are well known for their selective hydrolysis of racemic epoxides to give optically pure chiral diols. This study highlights an efficient process of synthesis of chiral vicinal diols in good yields and enantioselectiviy using horse radish peroxidase enzyme immobilized on the amine functionalized magnetic nano particles (Fe 3 O 4 nanoparticles) as enzyme carriers. It also facilitates separation of MNP-immobilized enzymes by applying external magnetic field. The immobilization of magnetic nano particles was confirmed by transmission electron microscope (TEM) and scanning electron microscope (SEM). The MNP-immobilized peroxidase enzyme improved stability of the enzyme and has shown broader substrate specificity in enantioselective hydrolysis of racemic epoxides, under mild and environmentally friendly conditions. The methodology MNP-immobilized enzyme developed in the synthesis of chiral diols has a potential for use in large-scale applications.

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Enzyme Immobilization

Bhardwaj

Agrawal

Verma

2023

Genomics Approach to Bioremediation

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Immobilization of cellulase enzyme on superparamagnetic nanoparticles and determination of its activity and stability

Cited by 207 publications

References 27 publications

Reusable nanobiocatalysts for the efficient extraction of pigments from orange peel

Reusable nanobiocatalysts for the efficient extraction of pigments from orange peel

A Green Approach towards the Synthesis of Enantio Pure Diols Using Horse Radish Peroxidase Enzyme Immobilized on Magnetic Nanoparticles

Enzyme Immobilization

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