The development and evaluation of β-glucosidase immobilized magnetic nanoparticles as recoverable biocatalysts

Park, Hee Joon; Driscoll, Ashley J.; Johnson, Patrick A.

doi:10.1016/j.bej.2018.01.017

Cited by 31 publications

(11 citation statements)

References 44 publications

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“…There are two major objectives in modifying the surface of magnetic supports. One is focused on the functionalization of the supports with such groups as aldehyde, amine, diimide, carboxyl, hydroxyl, etc., for further attachment of enzymes and other modifying molecules [ 71 , 72 , 73 , 74 , 75 , 76 , 77 , 78 , 79 ]. Functional groups can be provided via the attachment of difunctional molecules, polymers, dendrimers, or oligomers (aptamers) [ 80 , 81 , 82 , 83 ].…”

Section: Surface Modifying Agentsmentioning

confidence: 99%

“…The other objective of the surface modification deals with tuning the hydrophobicity–hydrophilicity balance for better compatibility of the enzyme, support, and the substrate [ 73 , 76 , 77 , 83 , 85 , 86 ]. Lipase is a typical enzyme requiring surface modification due to its high affinity to hydrophobic molecules.…”

Section: Surface Modifying Agentsmentioning

confidence: 99%

“…Such a modification was possible due to the high affinity of His-tag to Ni ions. At the same time, His-tag easily attached tobacco etch virus (TEV) protease, enhancing compatibility between the support and the enzyme (Figure 8 The other objective of the surface modification deals with tuning t hydrophilicity balance for better compatibility of the enzyme, suppo [73,76,77,83,85,86]. Lipase is a typical enzyme requiring surface mo high affinity to hydrophobic molecules.…”

Section: Surface Modifying Agentsmentioning

confidence: 99%

“…Functional ionic liquids have been reported as modifying agent lization on a magnetic support [85,86]. The authors coated magnetite (CS), attached an imidazole-containing ionic liquid (IL), and then im The other objective of the surface modification deals with tuning the hydrophobicityhydrophilicity balance for better compatibility of the enzyme, support, and the substrate [73,76,77,83,85,86]. Lipase is a typical enzyme requiring surface modification due to its high affinity to hydrophobic molecules.…”

Section: Surface Modifying Agentsmentioning

confidence: 99%

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Magnetic Nanoparticle-Containing Supports as Carriers of Immobilized Enzymes: Key Factors Influencing the Biocatalyst Performance

Matveeva

Bronstein

2021

Nanomaterials

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In this short review (Perspective), we identify key features of the performance of biocatalysts developed by the immobilization of enzymes on the supports containing magnetic nanoparticles (NPs), analyzing the scientific literature for the last five years. A clear advantage of magnetic supports is their easy separation due to the magnetic attraction between magnetic NPs and an external magnetic field, facilitating the biocatalyst reuse. This allows for savings of materials and energy in the biocatalytic process. Commonly, magnetic NPs are isolated from enzymes either by polymers, silica, or some other protective layer. However, in those cases when iron oxide NPs are in close proximity to the enzyme, the biocatalyst may display a fascinating behavior, allowing for synergy of the performance due to the enzyme-like properties shown in iron oxides. Another important parameter which is discussed in this review is the magnetic support porosity, especially in hierarchical porous supports. In the case of comparatively large pores, which can freely accommodate enzyme molecules without jeopardizing their conformation, the enzyme surface ordering may create an optimal crowding on the support, enhancing the biocatalytic performance. Other factors such as surface-modifying agents or special enzyme reactor designs can be also influential in the performance of magnetic NP based immobilized enzymes.

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Section: Surface Modifying Agentsmentioning

confidence: 99%

Section: Surface Modifying Agentsmentioning

confidence: 99%

Section: Surface Modifying Agentsmentioning

confidence: 99%

Section: Surface Modifying Agentsmentioning

confidence: 99%

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Magnetic Nanoparticle-Containing Supports as Carriers of Immobilized Enzymes: Key Factors Influencing the Biocatalyst Performance

Matveeva

Bronstein

2021

Nanomaterials

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“…Researchers are employing current technologies and developing modern applications that utilize enzymes immobilized onto nanoparticles (Chauhan & Pundir, 2011). Currently, several enzymes used in biotechnology, like BglA, have been covalently immobilized on magnetic nanoparticles (MNPs) using many different ligands (Fawze et al., 2020; Park et al., 2018; Verma et al., 2013). In addition, the physical characteristics of nanoparticles such as boost diffusion and particle mobility can impact on the inherent catalytic activity of attached enzymes (Peetla & Labhasetwar, 2015) and magnetic field capability revealed a mechanism for recovery efficiency of the enzyme complex thereby preventing the enzyme contamination of the final product (Eichwald & Walleczek, 1998).…”

Section: Introductionmentioning

confidence: 99%

Large batch production of Galactooligosaccharides using β‐glucosidase immobilized on chitosan‐functionalized magnetic nanoparticle

et al. 2020

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β-glucosidase (BglA) immobilization from Thermotoga maritima on magnetic nanoparticles (MNPs) functionalized with chitosan (Cs) were efficiently investigated to improve lactose conversion and galactooligosaccharides (GOS) production. We used a batch method in order to improve the conversion of lactose to GOS. The efficiency and yield of immobilization were 79% and immobilized BglA was effectively recycled via a magnetic separation procedure through a batch-wise GOS with no activity lessening. Furthermore, analyses were done through screening kinetics of enzyme activity, sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), Fourier transform infrared spectroscopy (FT-IR), and transmission electron microscopy (TEM). Proposed methodology of immobilization shows a potential application as it is stable which was proved through many methods including pH, temperature, heat treatment, storage, and kinetics of the enzyme. GOS and residual enzyme activity showed to be 28.76 and 40.44%, respectively. However, free enzyme synthesis of GOS yield was just 24% after 12 hr. This study proposed applying magnet in the immobilization process of BglA on Cs-MNPs to produce GOS as new method for immobilizing enzyme in a biostable and cost-efficient way. Practical applications This paper focus on immobilization of BglA from T. maritima onto MNPs functionalized with CS to investigate their further possibility improving lactose conversion and GOS production. Interestingly, a successful immobilization of Tm-BglA on the substrates were achieved in Cs-MNPs. The obtained results from enzyme activity, SDS-PAGE, FT-IR, and TEM showed that the high binding capacity of BglA to Cs-MNPs was successfully obtained. Furthermore, the binding efficiency calculation indicated that the immobilized BglA-Cs-MNPs conserved 40.44% of its native activity at the end of its 6th repeated use. In addition, magnetic separation technique was successfully employed for reuse of the immobilized BglA for repetitive batch-wise GOS without significant loss of activity. How to cite this article: Alnadari F, Xue Y, Almakas A, et al. Large batch production of Galactooligosaccharides using β-glucosidase immobilized on chitosan-functionalized magnetic nanoparticle.

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Magnetically separable spent coffee grounds as a potential novel support for the covalent immobilization of β‐glucosidase for cellobiose hydrolysis

Bhardwaj,

Mishra,

Ghosh

et al. 2024

J of Chemical Tech & Biotech

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BACKGROUNDThe industrial‐scale application of enzymes faces obstacles due to elevated costs and difficulties in stability and reuse. In this study, magnetic spent coffee grounds, an ecotoxic waste, have been utilized successfully for the first time to immobilize β‐glucosidase to overcome these challenges.RESULTSThe spent coffee grounds were magnetized and amine‐functionalized, followed by characterization using various techniques. Under optimized conditions, forming an imine bond between the functionalized support and β‐glucosidase resulted in a 62% immobilization yield (92.81 mg g−1 enzyme loading) and 12.5 U mg−1 activity after immobilization. A relatively small kinetic change was observed in the Km value (902 to 946 μmol L−1) after immobilization, suggesting minimal hindrance by AMSCG3 on substrate access or product release. Moreover, Glu@AMSCG3 showed exceptional stability (>90% residual activity) within a pH range of 3 to 6 after 2 h of incubation at 25 °C. A residual activity of 87.94% was maintained even at 80 °C and pH 5 after 2 h of incubation compared to the free β‐glucosidase, which showed only 6.5% residual activity at the same temperature. When cellobiose was hydrolyzed using Glu@AMSCG3 under optimum conditions, 91.33% cellobiose conversion was achieved initially, and over 79% conversion was maintained for 10 reusability cycles.CONCLUSIONThe improved stability of β‐glucosidase after covalent immobilization on amine‐modified magnetically separable spent coffee grounds indicates their potential as a support matrix for application in enzyme immobilization. © 2024 Society of Chemical Industry (SCI).

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The development and evaluation of β-glucosidase immobilized magnetic nanoparticles as recoverable biocatalysts

Cited by 31 publications

References 44 publications

Magnetic Nanoparticle-Containing Supports as Carriers of Immobilized Enzymes: Key Factors Influencing the Biocatalyst Performance

Magnetic Nanoparticle-Containing Supports as Carriers of Immobilized Enzymes: Key Factors Influencing the Biocatalyst Performance

Large batch production of Galactooligosaccharides using β‐glucosidase immobilized on chitosan‐functionalized magnetic nanoparticle

Magnetically separable spent coffee grounds as a potential novel support for the covalent immobilization of β‐glucosidase for cellobiose hydrolysis

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