Enhancement of operational stability of chloroperoxidase from Caldariomyces fumago by immobilization onto mesoporous supports and the use of co-solvents

Muñoz-Guerrero, Fabio A.; Águila, Sergio; Vázquez-Duhalt, Rafael; Alderete, Joel B.

doi:10.1016/j.molcatb.2015.02.014

Cited by 16 publications

(4 citation statements)

References 59 publications

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“…It is an exceptional protein due to the variety of organic substrates it can accept to perform many different types of oxidation and chlorination reactions [41][42][43][44][45][46][47][48][49][50][51][52][53][54][55][56]. It has been used in previous studies for the degradation of organic molecules and synthesis of organic molecules, and it has been shown to be effective when co-immobilized with GOx [6,51,[57][58][59][60][61][62][63][64][65][66][67][68][69][70][71][72][73][74][75][76]. This study shows that the immobilization of this bienzymatic system via electrostatic interactions is not reusable and activity is almost eliminated after one cycle, presumably due to the leaching of enzymes [62].…”

Section: Introductionmentioning

confidence: 99%

Immobilization of a Bienzymatic System via Crosslinking to a Metal-Organic Framework

et al. 2022

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A leading biotechnological advancement in the field of biocatalysis is the immobilization of enzymes on solid supports to create more stable and recyclable systems. Metal-organic frameworks (MOFs) are porous materials that have been explored as solid supports for enzyme immobilization. Composed of organic linkers and inorganic nodes, MOFs feature empty void space with large surface areas and have the ability to be modified post-synthesis. Our target enzyme system for immobilization is glucose oxidase (GOx) and chloroperoxidase (CPO). Glucose oxidase catalyzes the oxidation of glucose and is used for many applications in biosensing, biofuel cells, and food production. Chloroperoxidase is a fungal heme enzyme that catalyzes peroxide-dependent halogenation, oxidation, and hydroxylation. These two enzymes work sequentially in this enzyme system by GOx producing peroxide, which activates CPO that reacts with a suitable substrate. This study focuses on using a zirconium-based MOF, UiO-66-NH2, to immobilize the enzyme system via crosslinking with the MOF’s amine group on the surface of the MOF. This study investigates two different crosslinkers: disuccinimidyl glutarate (DSG) and 1-ethyl-3-(3-dimethylaminopropyl)-carbodiimide (EDC)/N-hydroxysuccinidimide (NHS), providing stable crosslinking of the MOF to the enzymes. The two crosslinkers are used to covalently bond CPO and GOx onto UiO-66-NH2, and a comparison of the recyclability and enzymatic activity of the single immobilization of CPO and the doubly immobilized CPO and GOx is discussed through assays and characterization analyses. The DSG-crosslinked composites displayed enhanced activity relative to the free enzyme, and all crosslinked enzyme/MOF composites demonstrated recyclability, with at least 30% of the activity being retained after four catalytic cycles. The results of this report will aid researchers in utilizing CPO as a biocatalyst that is more active and has greater recyclability.

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Section: Introductionmentioning

confidence: 99%

Immobilization of a Bienzymatic System via Crosslinking to a Metal-Organic Framework

et al. 2022

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“…Furthermore, the stability, under both storage and operational conditions, e.g., towards denaturation by heat or organic solvents, can be enhanced [7]. Currently, a range of supports have been reported for the immobilization of CPO, such as mesoporous supports [6,8,9], solgels [10,11], multi-walled carbon nanotubes [12,13] and other inorganic or organic solid supports [14,15]. The binding of an enzyme to a support (carrier) can be physical, ionic, or covalent in nature.…”

Section: Introductionmentioning

confidence: 99%

Bienzymatic nanoreactors composed of chloroperoxidase–glucose oxidase on Au@Fe3O4 nanoparticles: Dependence of catalytic performance on the bioarchitecture

Gao

Jiang

et al. 2016

Materials & Design

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“…After the discovery of MPNs in 1992 by Beck et al , their potential application in protein confinement was developed in 1996 by Diaz and Balkus [ 4 , 5 ]. In recent years a wide range of interest has been directed to nanoporous materials for immobilization of native structure proteins [ 6 , 7 , 8 , 9 , 10 , 11 ]. Their relatively large pore diameters (2–40 nm), narrow pore size distribution, large pore volumes ( ca.…”

Section: Introductionmentioning

confidence: 99%

“…Their relatively large pore diameters (2–40 nm), narrow pore size distribution, large pore volumes ( ca. 1.5 cm 3 ·g −1 ) and a high surface area (up to 1200 m 2 ·g −1 ) enable their use as great candidates to match the size of the wide range of biologically active molecules [ 5 , 6 , 10 ]. In addition, they present an extremely stable structure, chemically, mechanically and thermally, with low toxicities owing to their inorganic silicate network that makes them ideal candidates for nanobiotechnology applications [ 12 , 13 , 14 , 15 , 16 , 17 ].…”

Section: Introductionmentioning

confidence: 99%

Combined Spectroscopic and Calorimetric Studies to Reveal Absorption Mechanisms and Conformational Changes of Protein on Nanoporous Biomaterials

Ahmadi

Farokhi

Padidar

et al. 2015

IJMS

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In this study the effect of surface modification of mesoporous silica nanoparticles (MSNs) on its adsorption capacities and protein stability after immobilization of beta-lactoglobulin B (BLG-B) was investigated. For this purpose, non-functionalized (KIT-6) and aminopropyl-functionalized cubic Ia3d mesoporous silica ([n-PrNH2-KIT-6]) nanoparticles were used as nanoporous supports. Aminopropyl-functionalized mesoporous nanoparticles exhibited more potential candidates for BLG-B adsorption and minimum BLG leaching than non-functionalized nanoparticles. It was observed that the amount of adsorbed BLG is dependent on the initial BLG concentration for both KIT-6 and [n-PrNH2-KIT-6] mesoporous nanoparticles. Also larger amounts of BLG-B on KIT-6 was immobilized upon raising the temperature of the medium from 4 to 55 °C while such increase was undetectable in the case of immobilization of BLG-B on the [n-PrNH2-KIT-6]. At temperatures above 55 °C the amounts of adsorbed BLG on both studied nanomaterials decreased significantly. By Differential scanning calorimetry or DSC analysis the heterogeneity of the protein solution and increase in Tm may indicate that immobilization of BLG-B onto the modified KIT-6 results in higher thermal stability compared to unmodified one. The obtained results provide several crucial factors in determining the mechanism(s) of protein adsorption and stability on the nanostructured solid supports and the development of engineered nano-biomaterials for controlled drug-delivery systems and biomimetic interfaces for the immobilization of living cells.

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Enhancement of operational stability of chloroperoxidase from Caldariomyces fumago by immobilization onto mesoporous supports and the use of co-solvents

Cited by 16 publications

References 59 publications

Immobilization of a Bienzymatic System via Crosslinking to a Metal-Organic Framework

Immobilization of a Bienzymatic System via Crosslinking to a Metal-Organic Framework

Bienzymatic nanoreactors composed of chloroperoxidase–glucose oxidase on Au@Fe3O4 nanoparticles: Dependence of catalytic performance on the bioarchitecture

Combined Spectroscopic and Calorimetric Studies to Reveal Absorption Mechanisms and Conformational Changes of Protein on Nanoporous Biomaterials

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