• Journal of the Korean Wood Science and Technology
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• v.30 no.3
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• pp.12-17
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• 2002

The extracellular invertase (EC 3.2.1.26) (Candida utilis) preparation was obtained from the liquid medium after desalting and freeze drying. This prepared enzyme was used for the comparative purification on 4 activated matrices by liquid column affinity chromatography method. In this method there were used controlled porous glass (CPG) silanized covalently activated by keratin, silanized silica gel and silica gel covalently covered by keratin. It was found that the invertase purification process was better using both CPG matrices (silanized CPG and keratin activated CPG) than these with two silica gel supports. Also the elution coefficient of the invertase from the two CPG columns was about 93 to 94%. Two silica gel supports found to be superior in terms of purification efficiency. The invertase purification process was confirmed by PAGE electrophoresis.

• Advances in nano research
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• v.2 no.2
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• pp.89-98
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• 2014

A novel and simple method for the synthesis of nano-magnetite particles is disclosed. In the novel procedure, $Fe^{2+}$ is the only source of metal cation. Carboxymethylcellulose (CMC) is used as the structure directing agent. The phase analysis of the nano-particles was performed using XRD and electron diffraction techniques. Size and morphology analysis was performed using light scattering and TEM techniques. The effect of $NH_4OH$ solution (32 wt. %) at different CMC concentrations on the size distribution of the final magnetite powders is studied. An optimal base concentration exists for each CMC concentration leading to minimal agglomeration. There exists a minimum CMC concentration (0.0016 wt. %), lower than that no magnetite forms. It is shown that using the new method, it is possible to immobilize a lipase enzyme (Candida Rugosa) with immobilization efficiency larger than 98 % with a loading more than 3 times the reported value in the literature. The latter phenomenon is explained based on the agglomerate state of the nano-particles in the liquid phase.

• Advances in materials Research
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• v.6 no.2
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• pp.129-153
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• 2017

Platinum is a transition metal that is very resistant to corrosion. It is used as catalyst for converting methyl alcohol to formaldehyde, as catalytic converter in cars, for hydrocracking of heavy oils, in Fuel Cell devices etc. Moreover, Platinum compounds are important ingredient for cancer chemotherapy drugs. The nano forms of Platinum due to its unique physico-chemical properties that are not found in its bulk counterpart, has been found to be of great importance in electronics, optoelectronics, enzyme immobilization etc. The stability of Platinum nanoparticles has supported its use for the development of efficient and durable proton exchange membrane Fuel Cells. The present review concentrates on the use of Platinum conjugated with various metal or compounds, to fabricate nanocomposites, to enhance the efficiency of Platinum nanoparticles. The recent advances in the synthesis methods of different Platinum-based nanocomposites and their applications in Fuel Cell, sensors, bioimaging, light emitting diode, dye sensitized solar cell, hydrogen generation and in biosystems has also been discussed.

• Journal of Microbiology and Biotechnology
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• v.14 no.4
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• pp.698-706
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• 2004

$\beta$-Lactam antibiotics such as penicillin G, amoxicillin, and ampicillin were determined by a potentiometric biosensor system which exploited penicillinase immobilized on Immobilon cellulose nitrate membrane and a flat-bottomed pH electrode-as the biological component and transducer. The optimum reaction buffer for maximum sensitivity was found as 2 mM of sodium phosphate buffer (pH 7.2). The detection limit of the biosensor could be extended to 1 $\mu{M}$ of the analytes by increasing the enzyme loading for immobilization to 100 units/$m\ell$. The model samples spiked with each of the standard penicillins were measured for their biosensor responses and HPLC peak area, resulting in the relative responses of 82.1-103.5% and 79.5-106.1% for the biosensor method along with HPLC analysis, respectively. This result showed a good precision of the current biosensor method for screening the penicillin compounds.

• Proceedings of the Membrane Society of Korea Conference
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• 2005.05a
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• pp.131-135
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• 2005

• Journal of Microbiology and Biotechnology
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• v.16 no.10
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• pp.1523-1528
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• 2006

The optimization of a batch-type quartz crystal microbalance (QCM)-precipitation sensor measuring acetylcholinesterase (AChE) activity was conducted. To covalently bind AChE onto the gold electrode of a QCM surface, glutaraldehyde cross-linking to a cystamine self-assembled monolayer was tried at different cystamine concentrations. At the optimum conditions of the QCM-precipitation sensor, 0.1 M potassium phosphate buffer (pH 8.0), containing 0.01% Tween 80, was used as the reaction buffer, with the enzyme amount of 5 units for immobilization and the substrate concentration of 50 mg/ml. The current biosensor might find a future applicability to the sum parameter detection on organophosphorus and carbamate pesticides.

• 한국정보디스플레이학회:학술대회논문집
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• 2004.08a
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• pp.1193-1196
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• 2004

We have demonstrated the use of MWCNT as a nanoscale probe to monitor the activity of enzyme kinase. To immobilize the substrate peptide using carbodiimide chemistry, plasma or strong acid treatments were used to induce carboxyl groups on the sidewall of MWCNTs. After the susbtrate peptide immobilization, increase of conductance from MWCNT devices was observed. When peptide modified MWCNTs react with enzyme kinase, conductance decreases by several orders of magnitude, and this conductance change can be explained by the phosphorylation reaction of enzyme kinase. When the sample was incubated with phosphatase to dephosphorylate the substrate peptide, nearly complete recovery of the conductance signal has been observed. 4 for 6 devices appeared the same trends. So, we can confirm that we have monitored the kinase activity on the MWCNT surface by electrical detection.

• Journal of the Korea Organic Resources Recycling Association
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• v.28 no.4
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• pp.35-41
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• 2020

The immobilization of the hydroxylamine-oxidoreductase on the water channel surface was performed to investigate the efficacy of ammonia removal in turbulent flow. The reaction by this enzyme proceeds rapidly by converting hydroxylamine into nitrous acid. For the analysis of the effect, a dimensionless mass transfer governing equation was established with the physical properties based on room temperature. The ammonia diffusion coefficient in water and the kinematic viscosity coefficient of water were 2.45×10-9 ㎡/s and 1×10-6 ㎡/s, respectively. The distribution of ammonia concentration in the water was calculated with respect to the distance from the point at which exposure to ammonia began. The quantitative distribution with respect to the mixing depth was also found. Such a quantitative analysis can provide insight into whether the enzyme immobilized on the water channel surface can be effectively used for ammonia removal.

• Elastomers and Composites
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• v.41 no.4
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• pp.231-237
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• 2006

An enzyme electrode bound by butyl rubber was newly constructed for the determination of hydrogen peroxide and for the practical application as a biosensor. Then its electrochemical properties were investigated. It produced a hundreds-fold increased signal compared to the plant or animal tissue based biosensor studied previously and could be run at between $0.0{\sim}-1.00\;V$(vs. Ag/AgCl). The relationship between signal and electrode potential was linear in the experimental range of potential. It showed a detection limit of $3.0{\times}10^{-4}\;M$ and a very good linearity of Lineweaver-Burk plot giving the proof of a good enzyme immobilization. Especially, both the reproducibility of signal current due to its high sensitivity and mechanical stability presented a new possibility for the practical use of biosensor bound with butyl rubber.

• Applied Biological Chemistry
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• v.27 no.2
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• pp.112-118
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• 1984

Inverase was entrapped in calcium alginate gel. The immobilized beads had excellent uniform size and configuration. To screen the optimal conditions possessing high enzyme activity, effects of sodium alginate concentration, $CaCl_2$ concentration, and the incubation time of beads in $CaCl_2$ solution during the immobilization procedure were investigated. Immobilized beads prepared from the optimal conditions had 18.8 units per ml of gel, which is equivalent to 68% of the activity of soluble enzyme. Several kinetic parameters were determined: Km value. 143 mM; optimum pH, 4.5; optimum temperature, $50^{\circ}C$. Enzyme loading capacity was 150 mg per 20 ml gel. No significant decrease in sugar conversion was observed during the column operation for 6 days.