• Analytical Science and Technology
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• v.14 no.3
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• pp.286-289
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• 2001

The effect of pH and the substrate concentration on the sensing ability of the chicken peroxidase enzyme electrode was examined quanititatively. Using the new Michaelis-Menten equation, to which pH concept was introduced, enabled to calculate all kinds of dissociation constant related to chicken peroxidase and subsequently to determine the optimum pH of the sensor.

• Biotechnology and Bioprocess Engineering:BBE
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• v.8 no.5
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• pp.294-298
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• 2003

Endocrine-disrupting phenolic compounds in the water were degraded by laccase from Trametes sp. followed by activated sludge treatment. The effect of temperature on the degradation of phenolic compounds and the production of organic compounds were investigated using endocrine-disrupting chemicals such as bisphenol A, 2.4-dichlorophenol, and diethyl phthalate. Bisphenol A and 2.4-dichlorophenol disappeared completely after the laccase treatment, but no disappearance of diethyl phthalate was observed. The Michaelis-Menten type equation was proposed to represent the degradation rate of bisphenol A by the lacasse under various temperatures. After the laccase treatment of endocrine-disrupting chemicals, the activated sludge treatment was attempted and it could convert about 85 and 75% of organic compounds produced from bisphenol A and 2.4-dichlorophenol into H$_2$O and CO$_2$, respectively.

• Journal of Microbiology and Biotechnology
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• v.16 no.9
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• pp.1355-1361
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• 2006

The simultaneous saccharification and fermentation (SSF) process consists of concurrent enzymatic saccharification and fermentation. In the present cybernetic model, the saccharification process, which is based on the modified Michaelis-Menten kinetics and enzyme inhibition kinetics, was combined with the fermentation process, which is based on the Monod equation. The cybernetic modeling approach postulates that cells adapt to utilize the limited resources available to them in an optimal way. The cybernetic modeling was suitable for describing sequential growth on multiple substrates by Brettanomyces custersii, which is a glucose- and cellobiose-fermenting yeast. The proposed model was able to elucidate the SSF process in a systematic manner, and the performance was verified by previously published data.

• Journal of the Korean Applied Science and Technology
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• v.9 no.1
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• pp.7-13
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• 1992

Lipases catalyzed the transesterification reaction between esters and various primary and secondary alcohols in a 99% organic medium, porcine pancreatic, yeast, mold lipases can vigorously act as catalysts in a number of nearly anhydrous organic solvents. Various transesterification reactions catalyzed by porcine pancreatic lipase in hexane obey Michaelis-Menten kinetics. The dependence of the catalytic activity of the enzyme in organic media on the pH of the aqueous solution from which it was recovered is bell-shaped, with the maximum coinciding with the pH optimum of the enzymatic activity in water. The catalytic power exhibited by the lipases in organic solvents is comparable to that displayed in water. In addition to transesterification, lipases Can catalyze several other processes in organic media.

• Bulletin of the Korean Chemical Society
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• v.23 no.8
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• pp.1057-1061
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• 2002

The Hafnia alvei aspartase activity with acetic anhydride treatment gradually increased and reached 7.5-fold that of the native one. The activity of the acetylated aspartase was a little higher than that of the native enzyme, indicating that the cooperativity between a substrate and enzyme is increased. The optimum temperature of the native asparatse was $45^{\circ}C$, and that of the acetylated enzyme shifted to $40^{\circ}C.$ The pH vs. the activity profile of the acetylated asparatse was also different from that of the native enzyme. The initial velocity pattern of the acetylated aspartase intersects to the left of the ordinate, indicating the sequential kinetic mechanism other than a rapid equilibrium ordered one. The reciprocal plots for aspartate of the native aspartase were curved, but those of the acetylated aspartase were linear, indicating the Michaelis-Menten kinetics. The helical content of the acetylated aspartase was rather decreased to $9{\textperthousand}$ than that $(63{\textperthousand})$ of the native one.

• Korean Journal of Microbiology
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• v.26 no.2
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• pp.122-128
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• 1988

The enzymatic properties of soil cellobiohydrolase were examined and compared with those of cellobiohydrolase-active extracts from soil in the forms of enzyme-humic complex and humicfree enzyme, and cellobiohydrolase partially pruified from Aspergillus niger. The pH optima of soil cellobiohydrolase and cellobiohydrolase-humic complex were greater by 1.5-3.0 pH units than those of cellobiohydrolase in humic-free extract and from A. niger. Soil cellobiohydrolase and cellobiohydrolase-humic complex were remarkably resistant to thermal denaturation and proteolysis. These results confirm that cellobiohydrolase in soil is atable in conditions which rapidly inactivate microbial cellobiohydrolase and that its stability is due to the immobilization of this enzyme by association with humic substances. The Michaelis-Menten constants (Km) for soil, cellobiohydrolase-humic complex, humic free extract and cellobiohydrolase from A. niger were 22.1mg/ml, 11.3mg/ml, 10.6mg/ml and 4.5 mg/ml of Avicel, respectively.

• KSBB Journal
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• v.19 no.2
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• pp.143-147
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• 2004

Biodegradation of dimethyl sulfide (DMS) was studied in a batch culture using Gordonia sihwaniensis PKL-1 isolated from a compost biofilter after 100 days of operation for the removal of volatile organic compounds. Optimal pH and temperature for the removal of DMS were 7 and $25^{\circ}C$, respectively. The Michaelis-Menten kinetic constants for DMS removal, $\upsilon_{max}$ and $K_s$, were 0.0016 mg/(mg-protein)ㆍhr, and 8.05 mg/L, respectively.

• Bulletin of the Korean Chemical Society
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• v.25 no.12
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• pp.1889-1892
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• 2004

The peroxidase activity of cytochrome c was studied by using a chromogen, 2,2'-azinobis-(2-ethylbenzthiazoline-6-sulfonate) (ABTS). Initial rate of ABTS oxidation formation was linear with respect to the concentration of cytochrome c between 2.5-10 ${\mu}$M and $H_2O_2$ between 0.1-0.5 mM. The optimal pH for the peroxidase activity of cytochrome c was 7.0-8.5. The peroxidase activity retained about 40% of the maximum activity when exposed at 60 $^{\circ}C$. for 10 min. The peroxidase activity showed a typical Michaelis-Menten kinetics for $H_2O_2$ which Km value was 29.6 mM. Radical scavengers inhibited the peroxidase activity of cytochrome c. The peroxidase activity was significantly inhibited by the low concentration of iron chelator, deferoxamine. The results suggested that the peroxidase activity was associated with iron in the heme of cytochrome c.

• Bulletin of the Korean Chemical Society
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• v.22 no.7
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• pp.689-692
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• 2001

An imprinting technique with labile covalent interactions has been developed in the design of new polymer catalysts. The template monomer 2 was prepared and copolymerized with DVB or EDMA to provide the polymer with a cavity having the shape of th e transition state of the reaction as well as binding sites for the substrate and catalytic functionalities. The rate of hydrolysis of diphenyl carbonate (1) in the presence of the imprinted polymer IP-DVB-THF was found to be 120 times faster than the background uncatalyzed reaction. A Km of 32 mM and a kcat of 1.8 ${\times}$ 10-3min-1 were observed from Michaelis-Menten kinetics with the imprinted polymer IP-DVB-THF.

• Nuclear Engineering and Technology
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• v.53 no.1
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• pp.142-147
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• 2021

Hydrogen peroxide is a radiolysis product of water formed under gamma-irradiation; therefore, its reliable detection is crucial in the nuclear industry for spent fuel management and coolant chemistry. This study proposes an electrochemical sensor for hydrogen peroxide detection. Cysteamine (CYST), gold nanoparticles (GNPs), and horseradish peroxidase (HRP) were used in the modification of a gold electrode for fabricating Au/CYST/GNP/HRP sensor. Each modification step of the electrode was investigated through electrochemical and physical methods. The sensor exhibited strong sensitivity and stability for the detection and measurement of hydrogen peroxide with a linear range of 1-9 mM. In addition, the Michaelis-Menten kinetic equation was applied to predict the reaction curve, and a quantitative method to define the dynamic range is suggested. The sensor is highly sensitive to H₂O₂ and can be applied as an electrochemical H₂O₂-sensor in the nuclear industry.