• Journal of Microbiology and Biotechnology
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• v.26 no.7
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• pp.1234-1241
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• 2016

Methanol is a versatile compound that can be biologically synthesized from methane (CH₄) by methanotrophs using a low energy-consuming and environment-friendly process. Methylocella tundrae is a type II methanotroph that can utilize CH₄ as a carbon and energy source. Methanol is produced in the first step of the metabolic pathway of methanotrophs and is further oxidized into formaldehyde. Several parameters must be optimized to achieve high methanol production. In this study, we optimized the production conditions and process parameters for methanol production. The optimum incubation time, substrate, pH, agitation rate, temperature, phosphate buffer and sodium formate concentration, and cell concentration were determined to be 24 h, 50% CH₄, pH 7, 150 rpm, 30℃, 100 mM and 50 mM, and 18 mg/ml, respectively. The optimization of these parameters significantly improved methanol production from 0.66 to 5.18 mM. The use of alginate-encapsulated cells resulted in enhanced methanol production stability and reusability of cells after five cycles of reuse under batch culture conditions.

• Journal of Microbiology and Biotechnology
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• v.15 no.2
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• pp.234-238
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• 2005

Glucose oxidase was immobilized on the carboxylated multi-wall carbon nanotubes (MWNT-COOHs) in the presence of a coulping reagent, 1-ethy1-3-(3-dimethylaminopropy1) carbodiimide. Significant amounts of glucose oxidase were also immobilized on MWNT-COOHs without the coupling reagent. Various conditions for the immobilization of glucose oxidase were optimized. Optimal pH for the maximal activity of the immobilized glucose oxidase shifted to 7 from the optimal pH of 6 for the maximal activity of free enzyme due to the carboxy1 groups on the surface of MWNT-COOHs. An electrode of graphite rod with a diameter of 6 mm was fabricated using the immobilized glucose oxidase. The cyclic voltammetry study of the enzyme electrode revealed that the oxidation of glucose and subsequent transfer of electrons from the oxidation of glucose to the electrode were possible by the immobilized glucose oxidase without a mediator, implying that the enzyme electrode can be utilized for the development of biofuel cells.

• Advances in environmental research
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• v.3 no.4
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• pp.337-353
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• 2014

The determination of the effectiveness of the immobilization of blasting dust (waste generated in galvanic activities) in cement matrix, as well of mechanical, physical and microstructural properties of concrete paving blocks produced with partial replacement of cement was the objective of this work. The results showed that blasting dust has high percentage of silica in the composition and very fine particle size, characteristics that qualify it for replacement of cement in manufacturing concrete blocks. The replacement of Portland cement by up to 5% residues did not cause a significant loss in compressive strength nor increase in water absorption of the blocks. Chemical tests indicated that there is no problem of leaching or solubilization of contaminants to the environment during the useful life of the concrete blocks, since the solidification/stabilization process led to the immobilization of waste in the cement mass. Therefore, the use of blasting dust in the manufacture of concrete paving blocks is promising, thus being not only an alternative for proper disposal of such waste as well as a possibility of saving raw materials used in the construction industry.

• 한국생물공학회:학술대회논문집
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• 2003.10a
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• pp.654-654
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• 2003

• 한국생물공학회:학술대회논문집
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• 2005.04a
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• pp.302-302
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• 2005

• Korean Journal of Chemical Engineering
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• v.35 no.11
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• pp.2220-2231
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• 2018

Lipase from Candida rugosa was immobilized on $MgO{\cdot}SiO_2$ hybrid grafted with amine, thiol, cyano, phenyl, epoxy and carbonyl groups. The products were analyzed using Fourier transform infrared spectroscopy, nuclear magnetic resonance, low-temperature $N_2$ sorption and elemental analysis. Additionally, the degree of coverage of the oxide material surface with different functional groups and the number of surface functional groups were estimated. The Bradford method was used to determine the quantity of immobilized enzyme. The largest quantity of enzyme (25-28 mg/g) was immobilized on the hybrid functionalized with amine and carbonyl groups. On the basis of hydrolysis reaction of p-nitrophenyl palmitate to p-nitrophenol, it was determined how the catalytic activity of the obtained biocatalysts is affected by pH, temperature, storage time, and repeated reaction cycles. The best results for catalytic activity were obtained for the lipase immobilized on $MgO{\cdot}SiO_2$ hybrids with amine and carbonyl groups. The biocatalytic system demonstrated activity above 40% in the pH range 4-10 and in the temperature range $30-70^{\circ}C$. Lipase immobilized on the $MgO{\cdot}SiO_2$ systems with amine and epoxy groups retains, respectively, around 80% and 60% of its initial activity after 30 days of storage, and approximately 60-70% after 10 reaction cycles.

• Journal of Microbiology and Biotechnology
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• v.27 no.4
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• pp.768-774
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• 2017

Horseradish peroxidase (HRP) catalyzes the oxidation of aromatic compounds by hydrogen peroxide via insoluble polymer formation, which can be precipitated from the wastewater. For HRP immobilization, poly(lactic-co-glycolic acid) (PLGA) fine carrier supports were produced by using the Nano Spray Dryer B-90. Immobilized HRP was used to remove the persistent 2,4-dichlorophenol from model wastewater. Both extracted (9-16 U/g) and purified HRP (11-25 U/g) retained their activity to a high extent after crosslinking to the PLGA particles. The immobilized enzyme activity was substantially higher in both the acidic and the alkaline pH regions compared with the free enzyme. Optimally, 98% of the 2,4-dichlorophenol could be eliminated using immobilized HRP due to catalytic removal and partly to adsorption on the carrier supports. Immobilized enzyme kinetics for 2,4-dichlorophenol elimination was studied for the first time, and it could be concluded that competitive product inhibition took place.

• Journal of Microbiology and Biotechnology
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• v.17 no.1
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• pp.5-14
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• 2007

Nanotechnology is the creation and utilization of materials, devices, and systems through the control of matter on the nanometer. The technology has been applied to biodevices such as bioelectronics and biochips to improve their performances. Nanoparticles, such as gold (Au) nanoparticles, are the most widely used of the various other nanotechnologies for manipulation at the nanoscale as well as nanobiosensors. The immobilization of biomolecules is playing an increasingly important role in the development of biodevices with high performance. Nanopatteming technology, which is able to increase the density of chip arrays, offers several advantages, including cost lowering, simultaneous multicomponent detection, and the efficiency increase of biochemical reactions. A microftuidic system incorporated with control of nanoliter of fluids is also one of the main applications of nanotechnologies. This can be widely utilized in the various fields because it can reduce detection time due to tiny amounts of fluids, increase signal-to-noise ratio by nanoparticles in channel, and detect multi-targets simultaneously in one chamber. This article reviews nanotechnologies such as the application of nanoparticles for the detection of biomolecules, the immobilization of biomolecules at nanoscale, nanopatterning technologies, and the microfluidic system for molecular diagnosis.

• Applied Chemistry for Engineering
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• v.17 no.6
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• pp.565-574
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• 2006

The trend towards the application of single enantiomers of chiral compounds is undoubtedly increasing. Among the various methods to obtain one single enantio-riched compound selectively, enantioselective catalysis is the most attractive method. Especially, it is important to increase the activity, selectivity and lifetime of usually expensive chiral catalysts with a minute quantity in the enantioselective synthesis. Immobilization of active homogeneous catalysts is a fashionable topic in asymmetric catalysis, providing the inherent advantage of easy separation and better handling properties. Many different ways have been investigated to improve the enantioselectivity of products and to recycle the catalysts. This review mainly focused on the present scope and limitations of different types of enantioselective heterogeneous catalysts.

• KSBB Journal
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• v.32 no.1
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• pp.35-45
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• 2017

In this work the optical fiber glucose and lactate biosensors were developed by using fluorescent dye and enzyme immobilized on the end tip of an optical fiber. 3-Glycidyloxypropyl)methyldiethoxysilane (GPTMS), (3-Aminopropyl) trimethoxysilane (APTMS) and Methyltrimethoxysilane (MTMS) were used to immobilize glucose oxidase (GOD), lactate oxidase (LOD) and ruthenium(II) complex (tris(4,7-diphenyl-1,10-phenanthroline) ruthenium(II), $Ru(dpp)_3^{2+}$) as oxygen sensitive fluorescent dye. MTMS sol-gel was an excellent supporting material for the immobilization of $Ru(dpp)_3^{2+}$, GOD, and LOD on the optical fiber. Storage stability of the optical fiber glucose sensor was kept constant over 20 days, while the optical fiber lactate sensor had constant storage stability over 17 days. The optical fiber glucose and lactate biosensors also maintained good operational stability for 20 hours and 14 hours, respectively. The activities of the immobilized enzymes were most excellent at pH 7 and at $25^{\circ}C$. On-line monitoring of glucose and lactate in a simulated process was performed with the optical fiber glucose and lactate biosensors. On-line monitoring results were agreed with those of off-line data measured with high performance liquid chromatography (HPLC).