• 한국미생물·생명공학회지
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• 제19권2호
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• pp.186-192
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• 1991

It is very important to have a good kinetic model which considers the effects of both ammonium and glucose for the control and optimization of the poly-${\beta}$-hydroxybutyrate (PHB) fermentation. A kinetic model for the growth of Alcaligenes eutrophus and the biosynthesis of PHB under both ammonium and glucose limitation was proposed. Growth rate of residual biomass was expressed as a function of concentrations of residual biomass, glucose and ammonium having glucose inhibition. PHB production rate was expressed as a function of concentrations of residual biomass, glucose, ammonium and PHB content having ammonium and product inhibitions. Novel approaches were made to estimate the parameters in the model equations which considered two limiting substrates. Model parameters were evaluated by graphical and simplex methods. The proposed kinetic model fitted the data very well.

• 산업기술연구
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• 제3권
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• pp.33-38
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• 1983

The effect of various environmental conditions on the growth kinetics of Zymomonas mobilis were studied and the kinetic parameters were evaluated. The value of ${\mu}m$ was $0.45hr^{-1}$ and Ks was 0.23 g/L. Inhibition of growth at high glucose concentration was found to follow the threshold substrate inhibition. Threshold substrate concentration was 102 g/L and substrate inhibition constant was 196 g/L. The effects of yeast extract concentrations were found to follow the Monod equation. ${\mu}m$ value was $0.45hr^{-1}$ and Ks was 0.3 g/L at 20 g/L of glucose and $0.24hr^{-1}$ and 0.24 g/L respectively at 200 g/L of glucose. The optimum temperature was found to be $35^{\circ}C$ and the activation energy of growth was 7.7 Kcal/mole below $35^{\circ}C$ and -29 Kcal/mole above $35^{\circ}C$.

• 펄프종이기술
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• 제46권3호
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• pp.37-43
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• 2014

Kinetics of holocellulose hydrolysis in concentrated sulfuric acid was analyzed using $^1H$-NMR spectroscopy with different reaction time, temperature and acid concentration in secondary hydrolysis. In this work, reaction condition of secondary hydrolysis was similar to concentrated sulfuric acid process with electrodialysis or simulated moving bed chromatography process for sulfuric acid recycling. By $^1H$-NMR spectroscopy, acid hydrolyzates from higher secondary acid hydrolysis (25-35% acid concentration) was successfully analyzed without any difficulties in neutralization or adsorption of acid hydrolyzate to solid salt. Higher acid concentration, higher temperature and longer reaction time led to more cellulose for glucose conversion but accompanied with glucose to galactose isomerization, glucose to unknown compounds and degradation of glucose to organic acid via furans.

• Biotechnology and Bioprocess Engineering:BBE
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• 제9권1호
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• pp.52-58
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• 2004

An unstructured mathematical model for lactic acid fermentation was developed. This model was able to predict the inhibition effects of lactic acid and glucose and was con-firmed to be valid with various initial concentrations of lactic acid and glucose. Simulation of energy production was made using this mathematical model, and the relationship between the kinetics of energy metabolism and lactic acid production was also analyzed.

• 한국미생물·생명공학회지
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• 제19권1호
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• pp.70-75
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• 1991

Continuous and simultaneous production of gluconic acid and sorbitol from glucose and fructose was carried out by using glucose-fructose oxidoreductase and glucanolactonase of Zymomonas mobilis. In order to utilize the enzymes without purification, Zymomonas mobilis was permeabilized with toluene. Optimum conditions for permeabilization and reaction kinetics of permeabilized Zymomonas mobilis were studied. In batch operation with the permeabilized cells immobilized in alginate beads, about 90% conversion was obtained within 35 h reaction. Continuous production of gluconic acid and sorbitol using the immobilized permeabilized cells was carried out. Optimum conditions for continuous operation with the imn~obilized cells were; pH 6.2 and temperature $40^{\circ}C$. Maximum productivities for gluconic acid and sorbitol were about 14.5 g/l/h and 14.8 g/l/h respectively at the dilution rate of 0.075 $h^{-1}$ when 300 g/l each of substrates was fed.

• BMB Reports
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• 제34권4호
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• pp.285-292
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• 2001

Insulin stimulates glucose uptake in muscle and adipose tissue and thus maintains normal blood glucose level in our body. Derangement of this process causes many grave health problems. Insulin stimulates glucose transport primarily by recruiting GLUT4 from its intracellular storage sites to the plasma membrane. The process is complex and involves GLUT4 trafficking through multiple subcellular compartments (organelles) and many protein functions, details of which are poorly understood. This review summarizes a recent development to isolate and characterize the individual intracellular GLUT4 compartments and to illustrate how this compartmental analysis will help to identify the insulin-sensitive step or steps in the insulin-induced GLUT4 recruitment in rat adipocytes. The review does not cover the recent exciting development in identification of many proteins implicated in this process.

• 전기화학회지
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• 제11권3호
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• pp.147-153
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• 2008

Improvement of the selectivity of nonenzymatic glucose based on mesoporous platinum ($H_1$-ePt) by using A.C. impedance is reported. The idea of the present work is based on the novel effect of the mesoporous electrode that the apparent exchange current due to glucose oxidation remarkably grows although the reaction kinetics on the surface is still sluggish. It is expected that the enlarged apparent exchange current on the mesoporous electrode can raise the sensitivity of admittance in A.C. impedance to glucose concentration. At a low frequency, A.C. impedance could become more powerful. The admittance at 0.01 Hz is even more sensitive to glucose than to ascorbic acid while amperometry exhibits the inverse order of sensitivity. This is the unique behavior that is neither observed by A.C. impedance on flat platinum electrode nor obtained by amperometry. The study shows how the combination of A.C. impedance and nano-structured surface can be applied to the detection of sluggish reaction such as electrochemical oxidation of glucose.

• BMB Reports
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• 제38권5호
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• pp.584-590
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• 2005

Glucose 6-phosphate dehydrogenase (EC 1.1.1.49) was purified from Aspergillus aculeatus, a filamentous fungus previously isolated from infected tongue of a patient. The enzyme, apparently homogeneous, had a specific activity of $220\;units\;mg^{-1}$/, a molecular weight of $105,000{\pm}5,000$ Dal by gel filtration and subunit size of $52,000{\pm}1,100$ Dal by sodium dodecyl sulphate-polyacrylamide gel electrophoresis. The substrate specificity was extremely strict, with glucose 6-phosphate (G6P) being oxidized by nicotinamide adenine dinucleotide phosphate (NADP) only. At assay pH of 7.5, the enzyme had $K_m$ values of $6\;{\mu}m$ and $75\;{\mu}m$ for NADP and G6P respectively. The $k_{cat}$ was $83\;s^{-1}$. Steady-state kinetics at pH 7.5 produced converging linear Lineweaver-Burk plots as expected for ternary-complex mechanism. The patterns of product and dead-end inhibition suggested that the enzyme can bind NADP and G6P separately to form a binary complex, indicating a random-order mechanism. The enzyme was irreversibly inactivated by heat in a linear fashion, with G6P providing a degree of protection. Phosphoenolpyruvate (PEP), adenosinetriphosphate (ATP), and fructose 6-phosphate (F6P), in decreasing order, are effective inhibitors. Zinc and Cobalt ions were effective inhibitors although cobalt ion was more potent; the two divalent metals were competitive inhibitors with respect to G6P, with $K_i$ values of $6.6\;{\mu}m$ and $4.7\;{\mu}m$ respectively. It is proposed that inhibition by divalent metal ions, at low NADPH /NADP ratio, is another means of controlling pentosephosphate pathway.

• 한국미생물·생명공학회지
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• 제19권5호
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• pp.504-508
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• 1991

유전자 재조합된 동물 세포의 유가 배양시 $1.85\times 10^{-10}$(mmole/cell/h)의 비 glucose 소비속도와 $4.7\times 10^{-7}(\mu g/ceil/h)$의 erythropoetin (EPO)비 생산속도를 유지할 수 있었다. 또한 이같은 배양에서 회분 및 연속배양에서 보다 높은 세포수를 얻었으며 전 배양이 유사 안정상태에 도달하는 배양 후기에는 glutamolysis가 생육 공정에 매우 중요한 역활을 하고 있음이 확이됐다. 유가 배양시 13(mmloe/l)의 glucose 농도에서 생육 제한 현상이 일어났으며, 이같은 농도에 도달할 때까지는 glucose의 농도가 증가함에 따라 배양시간의 경과와 함께 EPO 생산성이 증가했다.

• 미생물학회지
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• 제18권2호
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• pp.59-66
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• 1980

Two strains S-P and S-P-2, both Streptomyces sp., have been isolated and were found to have relatively high specific enzyme activity compared to other organisms reported. The specific activity of the enzyme produced from these two strains were 0.25 and 0.2 international units respectively. The productivity of the enzyme achieved was about 50 IU/l/hr. Glucose isomerase form these strains was found to be stable under the temperature of heat treatment (at $65^{\circ}C$) for fixation of enzyme inside the dell. This organism has an advantage in that it did not require toxic metalic ion for enzyme activity and could utilize xylan in leu of xylose as an inducer. The optimal temperature and pH of enzymatic reaction purpose of using these data for the optimal operation and designing of enzyme reactor system. The reaction mechanism was found to follow the single substrate reversible reaction kinetics. The kinetic constants determined experimentally are : $K_{mf}=0.33M,\;K_{mb}=1.0M,\;V_{mf}=0.88{\mu}mole\;per\;min.,\;V_{mb}= 2.96{\mu}mole\;per\;min.\;and\;K_{eq}=0.74.