• 한국생물공학회:학술대회논문집
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• 2001.11a
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• pp.560-563
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• 2001

Geotrichum sp. MF01, isolated from oil-contaminated soil, utilized methyl ethyl ketone(MEK) as the sole source of carbon and energy. The strain MF01 showed a Michaelis-Menten kinetics on MEK, and the kinetic parameters determined for MEK degradation were; specific removal rate, $r_{max}$ = 0.14 $h^{-1}$; half-saturation constant, $K_m$ = 5.88 mM. The adsorption of MEK by heat-killed strain was 0.62 mg at 8.07 mg MEK indicating that the degradation was the primary removal mechanism over adsorption. Biodegradation of MEK was studied in a biofilter using perlite, vermiculite 0:1, v/v) as supporting material. During 57 days of biofilter operation, $^3h^{-1}$.

• Journal of Microbiology and Biotechnology
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• v.19 no.12
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• pp.1565-1568
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• 2009

Purified Helicobacter pylori urease displayed a sigmoid curve in the plot of velocity versus [S] at urea concentrations less than 0.1mM. Under conditions where preservatives, glycerol, or polyethylene glycol (PEG) were added to the enzyme reaction, the substrate hydrolysis was consistent with Michaelis-Menten kinetics, with a $K_m$ of $0.21\;{\pm}\;0.06\;mM$ and a $V_{max}$ of $1,200\;{\pm}\;300\;{\mu}mol\;min^{-1}\;mg^{-1}$. However, at saturating substrate concentrations, the kinetic parameters of H. pylori urease were unaffected by the presence of the preservatives, and enzyme catalysis conformed to Michaelis-Menten kinetics. The Hill coefficients of the enzyme-catalyzed urea hydrolysis in the presence and absence of PEG were 1 and 2, respectively. Based on these findings, we suggest that H. pylori urease may exist in aggregated and dissociated forms, each with intact function but differing kinetics that may be of importance in maximizing urea breakdown at varying urea concentrations in vivo.

• KSBB Journal
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• v.9 no.1
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• pp.40-47
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• 1994

A simplified mathematical model for the production of high-purity fructo-oligosaccharides by the mixed-enzyme system of fructosyl transferees and glucose oxidase was proposed and compared with the experimental results. The kinetic parameters including $K_m,\;V_{max}\;and\;K_{iG}$ were estimated at $40^{\circ}C$, in which $K_m$, values decreased and $K_{iG}$ and $V_{max}$ values increased compared with those of fructosyl transferees alone. The kinetics of the mixed-enzyme system was successfully described in the form of Michaelis-Menten equations. At the reasonable sucrose concentrations tested, the simulated sugar profiles were of good agreement with the experimental ones.

• Journal of Microbiology and Biotechnology
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• v.25 no.1
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• pp.66-73
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• 2015

The pabS gene of Agaricus bisporus 02 encoding a putative PABA synthase was cloned, and then the recombinant protein was expressed in Escherichia coli BL21 under the control of the T7 promoter. The enzyme with an N-terminal GST tag or His tag, designated GST-AbADCS or His-AbADCS, was purified with glutathione Sepharose 4B or Ni Sepharose 6 Fast Flow. The enzyme was an aminodeoxychorismate synthase, and it was necessary to add with an aminodeoxychorismate lyase for synthesizing PABA. AbADCS has maximum activity at a temperature of approximately 25℃ and pH 8.0. Magnesium or manganese ions were necessary for the enzymatic activity. The Michaelis-Menten constant for chorismate was 0.12 mM, and 2.55 mM for glutamine. H₂O₂ did distinct damage on the activity of the enzyme, which could be slightly recovered by Hsp20. Sulfydryl reagents could remarkably promote its activity, suggesting that cysteine residues are essential for catalytic function.

• Proceeding of EDISON Challenge
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• 2015.03a
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• pp.24-31
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• 2015

효소는 생명 현상을 구현하는 단백질 촉매인데 그 동안 효소의 촉매 반응 속도는 Michaelis-Menten(MM) 모델로 대부분 설명되어 왔다. 그러나 MM 모델은 실험으로 측정된 단일 효소 반응시간의 확률분포 모양을 설명할 수 없다. MM 모델에 반응계수의 정적 무질서 개념을 도입한 효소 반응 모델도 기질 농도에 따라 변화하는 효소 반응시간의 통계적 요동을 설명하지 못한다. 우리는 단일 효소 반응시간의 통계적 요동이 기질에 따라 변화하는 양상을 설명하기 위해 효소 반응을 구성하는 개별 화학반응을 단순히 푸아송 과정이 아닌 갱신과정(renewal process)으로 확장한 효소 반응 모델을 제안한다. 우리는 이 단일 효소 반응 모델과 기질에 따른 효소 반응시간 분산 변화 데이터를 비교하여 효소-기질 복합체의 지속시간 분포를 간단한 형태로 얻어내었다. 또한, 이 정보를 토대로 전산모사를 수행하여 효소 반응시간의 확률분포를 얻어내고, 실제 실험 결과 및 기존 이론들과 비교하였다. 뿐만 아니라 단일 효소 반응시간의 확률분포를 연속 시간 임의의 보행자(continuous time random walker)의 대기시간 확률분포(waiting time distribution)로 대응하면, 평균 제곱 변위가 시간에 따라 단순히 증가 하지 않는 고분자의 특이 수송(anomalous diffusion) 현상도 정량적으로 설명할 수 있었다.

• Korean Journal of Food Science and Technology
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• v.30 no.6
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• pp.1426-1431
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• 1998

The research was undertaken to characterize enzymatic properties of Streptomyces albus amylase expressed in recombinant Bacillus subtilis. Molecular weight and pI of the purified enzyme were estimated to be 50 kD by SDS-PAGE and 4.3 by isoelectric focusing. The optimum temperature and optimum pH were $45^{\circ}C$ and 6.0, respectively. D-and Z-value were estimated to measure thermostability of the purified enzyme. The Z-value was estimated $17.7^{\circ}C$, which is lower than typical amylase. Maltotetraose was produced as a major component from soluble starch in the early state of reaction but gradually degraded to maltose. Thin layer chromatography was also performed to analyze the reaction products. The parameters involved in Michaelis-Menten enzyme kinetics were found to be the maximum velocity of 0.37 mM/min and the Michaelis constant of 0.13%, respectively.

• The Journal of Korean Institute for Practical Engineering Education
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• v.2 no.1
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• pp.35-41
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• 2010

An enzyme-catalized reaction is usually characterized by a very large increase in the rate and high specificity. Kinetics of simple enzyme-catalized reactions are often referred to as Michelis-Menten kinetics. A chemical that interferes with an enzyme's activity is called inhibitor. There are two types of enzyme inhibitions (viz. reversible and irreversible). If an inhibitor attaches to the enzyme with weak bonds, such as hydrogen bonds, the inhibition is usually reversible. Many enzyme reactions are also inhibited reversibly by their corresponding products. The rate of substrate disappearance together with the rate of product formation may be written by nonlinear differential equations. In the present study, numerical analyses of simple enzyme kinetics and inhibited enzyme kinetics are reported for the purpose of undergraduate education in engineering.

• Korean Journal of Food Science and Technology
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• v.28 no.2
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• pp.273-278
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• 1996

The research was undertaken to characterize the reaction mode of transglucosidase (TG) from Aspergillus niger for the production of isomaltooligosaccharides such as isomaltose, panose and isomaltotriose. TG hydrolyzed maltose to glucose units and produced panose and glucose by transglucosylation. TG hydrolyzed panose to maltose and glucose when panose was used as an initial substrate. The reaction patterns of products when isomaltose, isomaltotriose or isomaltotetraose were used as substrates were different from the case when maltose was used as a substrate. Maltotriose and maltose showed the same formation pattern of products. TG also produced isomaltooligosaccharides from maltooligosaccharides. The production of panote by TG from maltose was mathematically described by Michaelis-Menten kinetics. The kinetic constants, $V_{max}$ (the maximum velocity) and $K_m$ (Michaelis constant), were estimated by Lineweaver-Burk plot to be 400 M/min and 21.4 mM, respectively.

• Journal of Life Science
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• v.11 no.3
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• pp.273-278
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• 2001

Removal of nitrogen compound from waste water is essential and often accomplished by biological process. Deni-trification bacterium. Paracoccus denitrificans(KCTC 2350) is employed to estimate the ability and the characteristics of denitrification. In the immobilized biological reactor system, the measurement of absolute amount of active strain in the reactor is comparatively difficult or impossible. In this study, strain immobilized denitrification reactor was designed with the unwoven texture wrapped peeped hole plastic tube to calculated the absolute amount of active strain by comparing the activity of the immobilized reactor adn the free cell reactor. The reactor system was continuous stirred tank reactor and the rate of substrate consumption was assumed to be Michaelis-Menten equation. As a result, we found that the amount of immobilized active strain was the half of the total active strain in the reactor and the time required to reach in the equilibrium state in the immobilized reactor system was shorter than that of the free cell reactor system.

• Korean Chemical Engineering Research
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• v.45 no.2
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• pp.133-142
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• 2007

As the environmental pollution caused by excessive uses of chemical fertilizers and pesticides is aggravated, organic farming using pasture and livestock manure is gaining an increased necessity. The application rate of the organic farming materials to the field is determined as a function of crops and soil types, weather and cultivation surroundings. When livestock manure is used for organic farming materials, the volatilization of ammonia from field-spread animal manure is a major source of atmospheric pollution and leads to a significant reduction in the fertilizer value of the manure. Therefore, an ammonia emission model should be presented to reduce the ammonia emission and to know appropriate application rate of manure. In this study, the ammonia emission rate from field-applied pig manure is predicted using an artificial neural network (ANN) method, where the Michaelis-Menten equation is employed for the ammonia emission rate model. Two model parameters (total loss of ammonia emission rate and time to reach the half of the total emission rate) of the model are predicted using a feedforward-backpropagation ANN on the basis of the ALFAM (Ammonia Loss from Field-applied Animal Manure) database in Europe. The relative importance among 15 input variables influencing ammonia loss is identified using the weight partitioning method. As a result, the ammonia emission is influenced mush by the weather and the manure state.