4-Chlorophenol biodegradation facilitator composed of recombinant multi-biocatalysts immobilized onto montmorillonite

Kwean, Oh Sung; Cho, Su Yeon; Yang, Jun Won; Cho, Wooyoun; Park, Sungyoon; Lim, Yejee; Shin, Min Chul; Kim, Han Suk; Park, Joonhong; Kim, Han Soo

doi:10.1016/j.biortech.2018.03.066

Cited by 30 publications

(6 citation statements)

References 39 publications

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“…To describe the kinetic behavior, v max , K m , and catalytic efficiency (K cat /K m ) were determined by the Michaelis-Menten model as described by Kwean et al (2018) with some modifications. The Michaelis-Menten model, as given in Eq.…”

Section: Enzymes Kinetic Parameter Analysismentioning

confidence: 99%

Immobilized cold-active enzymes onto magnetic chitosan microparticles as a highly stable and reusable carrier for p-xylene biodegradation

Miri,

Ravula,

Akhtarian

et al. 2024

Front. Environ. Eng.

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Stability and reusability properties are the two most important factors that determine an enzyme’s application in industry. To this end, cold-active crude enzymes from a psychrophile (xylene monooxygenase (XMO) and catechol 1,2-dioxygenase (C1,2D) were immobilized on magnetic chitosan microparticles for the first-time using glutaraldehyde as a linker. The potential application of enzyme-loaded magnetic particles to remove and detoxify dissolved p-xylene from water confirmed the synergistic mechanism of degradation for in-situ bioremediation in soil and water. Immobilization was optimized based on four variables, such as magnetic particle (MPs), chitosan, glutaraldehyde, and enzyme concentrations. The immobilized enzymes were characterized by Fourier Transform Infrared Spectroscopy (FTIR) and Scanning Electron Microscope (SEM). The immobilized enzymes showed improved pH tolerance ranging from 4.0 to 9.0, better temperature stability ranging from 5 to 50, higher storage stability (∼70% activity after 30 days of storage), and more importantly, reusability (∼40% activity after 10 repetitive cycles of usage) compared to their free form. Also, the immobilization of enzymes increased the effectiveness of the enzymatic treatment of p-xylene in soil (10,000 mg/kg) and water (200 mg/L) samples. As a result of the superior catalytic properties of immobilized XMO and C1,2D, they offer great potential for in situ or ex-situ bioremediation of pollutants in soil or water.

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Section: Enzymes Kinetic Parameter Analysismentioning

confidence: 99%

Immobilized cold-active enzymes onto magnetic chitosan microparticles as a highly stable and reusable carrier for p-xylene biodegradation

Miri,

Ravula,

Akhtarian

et al. 2024

Front. Environ. Eng.

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“…Various immobilization supports have been used for the immobilization of dioxygenases, such as sodium alginate [32], single-walled carbon nanotubes [33,34], multi-walled carbon nanotubes [35], Fe 3 O 4 nanoparticles [36], and fulvic-acid-activated montmorillonite [37]. Among these supports, magnetic nanoparticles (MNPs) stand out due to their attractive properties, such as their high surface-to-volume ratio and strong magnetization values, which facilitate their separation from the reaction mixture and thus the efficient re-use of the biocatalyst [38].…”

Section: Introductionmentioning

confidence: 99%

Characterization of Gentisate 1,2-Dioxygenase from Pseudarthrobacter phenanthrenivorans Sphe3 and Its Stabilization by Immobilization on Nickel-Functionalized Magnetic Nanoparticles

Asimakoula

Giannakopoulou

Lappa

et al. 2022

Applied Microbiology

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The aim of this study was the biochemical and kinetic characterization of the gentisate 1,2-dioxygenase (GDO) from Pseudarthrobacter phenanthrenivorans Sphe3 and the development of a nanobiocatalyst by its immobilization on Ni2+-functionalized Fe3O4-polydopamine magnetic nanoparticles (Ni2+-PDA-MNPs). This is the first GDO to be immobilized. The gene encoding the GDO was cloned with an N-terminal His-tag and overexpressed in E. coli. The nanoparticles showed a high purification efficiency of GDO from crude cell lysates with a maximum activity recovery of 97%. The immobilized enzyme was characterized by Fourier transform infrared spectroscopy (FTIR). The reaction product was identified by 1H NMR. Both free and immobilized GDO exhibited Michaelis–Menten kinetics with Km values of 25.9 ± 4.4 and 82.5 ± 14.2 μM and Vmax values of 1.2 ± 0.1 and 0.03 ± 0.002 mM*s−1, respectively. The thermal stability of the immobilized GDO was enhanced at 30 °C, 40 °C, and 50 °C, compared to the free GDO. Stored at −20 °C, immobilized GDO retained more than 60% of its initial activity after 30 d, while the free enzyme completely lost its activity after 10 d. Furthermore, the immobilized nanoparticle–enzyme conjugate retained more than 50% enzyme activity up to the fifth cycle.

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“…To overcome those disadvantages, immobilized enzymes for their satisfactory reusability have attracted heightened attention 1‐3 . Various carriers including, but not limited to, porous SiO 2 , 4‐6 inorganic oxides, 7,8 magnetic particles, 9‐13 and natural polymers, 14‐16 were applied for enzymes immobilization. However, the limited immobilized enzymes amount and loss of the enzyme activity hinder the development of immobilized enzymes.…”

Section: Introductionmentioning

confidence: 99%

Synthesis of post‐modified poly(ester‐amino) microspheres via aza‐Michael precipitation polymerization and its use for enzyme immobilization

Sun

Jiang

et al. 2021

Polymers for Advanced Techs

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Uniform poly(ester‐amino) microspheres (PEAs) were prepared by catalyst‐free aza‐Michael addition precipitation polymerization of trihydroxymethylpropyl triacrylate (TMPTA) and piperazine (PA) in acetonitrile. The effects of monomer feed ratio and concentration, polymerization temperature, and time on the size and morphology of PEAs were investigated. Monodisperse PEAs with size about 4 μm were successfully obtained at 2/3 molar ratio of TMPTA/PA and 4°C. The chemical structure of PEAs was characterized. There were amount of unreacted acrylate groups remained on the surface of PEAs prepared at the imino/acrylate molar ratio of 1/1.1, which provide lots of active sites for further chemical modification, especially for bioactivator immobilization. Laccase was used as an example to determine bio‐immobilization activity of PEAs. Immobilized laccase exhibited higher tolerance to pH and temperature. The immobilized laccase was used as biocatalyst for degradation of Malachite Green. About 53% of its initial catalytic activity was retained after 4 cycles of reuse.

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4-Chlorophenol biodegradation facilitator composed of recombinant multi-biocatalysts immobilized onto montmorillonite

Cited by 30 publications

References 39 publications

Immobilized cold-active enzymes onto magnetic chitosan microparticles as a highly stable and reusable carrier for p-xylene biodegradation

Immobilized cold-active enzymes onto magnetic chitosan microparticles as a highly stable and reusable carrier for p-xylene biodegradation

Characterization of Gentisate 1,2-Dioxygenase from Pseudarthrobacter phenanthrenivorans Sphe3 and Its Stabilization by Immobilization on Nickel-Functionalized Magnetic Nanoparticles

Synthesis of post‐modified poly(ester‐amino) microspheres via aza‐Michael precipitation polymerization and its use for enzyme immobilization

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