• Bulletin of the Korean Chemical Society
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• v.27 no.10
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• pp.1681-1684
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• 2006

• Macromolecular Research
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• v.16 no.7
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• pp.651-658
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• 2008

Poly(butylene succiate) (PBS), poly(butylene succinate-co-L-lactate) (PBSL), and poly(butylene succinate-co-6-hydroxycaproate) (PBSCL) polymers were degraded by lipase $PS^{(R)}$, and the enzymatic degradation mechanism of PBS was analyzed in detail. The enzymatic degradation of PBS gave 4-hydroxybutyl succinate (4HBS) as the main product. An exo-type hydrolysis mechanism was proposed based on this observation. The terminal chain of PBS had conformational similarity to ordinary tri- and diglycerides and could be incorporated as a substrate in the active site of this lipase. The surface adsorption of the lipase was much larger on PBS and its copolymer films than on the other polyester films because the lipase adhered quite strongly to the polymer terminal through a specific adsorption mechanism. Kinetic analysis showed that the total number of surface adsorption points per unit area of PBSL and PBSCL copolymers was larger than that of the PBS homopolymer.

• KSBB Journal
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• v.5 no.2
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• pp.133-139
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• 1990

A simple and convenient method was introduced to determine the kinetic parameters for various enzymatic reaction kinetics. The method based on integrated formular can be applied to the parameter estimations from a single experiment. A modified three-parameter model was applied for the parameter estimation in reversible reaction and the equilibrium substrate concentration could be also estimated. It is possible to identify the enzymatic reaction pattern by inspecting the parameter values and the square of the correlation coefficient.

• Proceedings of the Korean Society for Applied Microbiology Conference
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• 1978.10a
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• pp.206.4-206
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• 1978

By utilizillg whole cell enzyme of the Xantho-monas citri IFO 3835, cephalexin is synthesized directly from 7-amino-deacetoxy cephalosporanic acid (7-ADCA) and phenyl glycine methyl ester (PGM). To date, cephalexin has been manufactu-red by chemical process involving fairly large number of steps to protect the amino group of phenly glycine and carboxyl group of 7-ADCA. However, the enzymatic process involves only a single step with 85％ conversion in 90 minutes. The fermentation variables studied indicate that oxygen transfer is limiting step in the enzyme production. Optimum conditions for enzymatic reaction were 37 C, pH 6.0, and the optimum substrate molar ratio of PGM to 7-ADCA was 2. Other variables that are related to the biochemical properties of whole cell enzyme temperature stability, pH stability, kinetic constants, reusing effect, enzyme loading effect were also evaluated.

• Proceedings of the Korean Society for Applied Microbiology Conference
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• 2000.10a
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• pp.168-175
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• 2000

• Korean Journal of Fisheries and Aquatic Sciences
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• v.22 no.6
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• pp.391-396
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• 1990

Changes in electric resistance was measured to carry out the kinetic analysis of milk gellation upon addition of rennet. Using pasteurized milk and commercial rennin, kinetic properties were investigated during milk gellation in terms of initial hydrolysis and coagulation steps. Specially designed reactor with two platinum electrodes was used throughout the experiments. As a function of either milk concentrations or reaction temperatures, gel time exhibited directly proportional relations: on the contrary, gel time was inversely pro-portional to enzyme concentration. Activation energies for enzymatic degradation and cogulation were 16.3, 4.6 and 34, 8.6 Kcal/mol, repectively. This simple analytical method proved to be very effective to characterize the mechanism of milk gellation. Moreover, unlike other methods, this method reguired simple apparatus and short time of analysis.

• Molecules and Cells
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• v.39 no.1
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• pp.26-30
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• 2016

Peroxiredoxins are ubiquitous thiol proteins that catalyse the breakdown of peroxides and regulate redox activity in the cell. Kinetic analysis of their reactions is required in order to identify substrate preferences, to understand how molecular structure affects activity and to establish their physiological functions. Various approaches can be taken, including the measurement of rates of individual steps in the reaction pathway by stopped flow or competitive kinetics, classical enzymatic analysis and measurement of peroxidase activity. Each methodology has its strengths and they can often give complementary information. However, it is important to understand the experimental conditions of the assay so as to interpret correctly what parameter is being measured. This brief review discusses different kinetic approaches and the information that can be obtained from them.

• Journal of Microbiology
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• v.40 no.1
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• pp.33-37
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• 2002

An enzymatic reaction for the production of D-alanine from D-aspartic acid and pyruvate as substrates by a thermostable D-amino acid aminotransferase (D-AAT) was investigated at various conditions In the temperature range of 40-70$\^{C}$ and pH range of 6.0-9.5. The D-AAT was produced with recombinant E. coli BL21, which hosted the chimeric plasmid pTLK2 harboring the D-AAT from the novel thermophilic Bacillus sp. LK-2. The enzyme reaction was shown to follow the Ping Pong Bi Bi mechanism. The K$\_$m/ values for D-aspartic acid and pyruvate were 4.38 mar and 0.72 mM, respectively. It was observed that competitive inhibition by D-alanine, the product of this reaction, was evident with the inhibition constant K$\_$i/ value of 0.1 mM. A unique feature of this reaction scheme is that the decorboxylation of oxaloacetic acid, one of the products, spontaneously produces pyruvate. Therefore, only a catalytic amount of pyruvate is necessary for the enzyme conversion reaction to proceed. A typical time-course kinetic study skewed that D-alanine up to 88 mM could be produced from 100 mM of D-aspartic acid with a molar yield of 1.0.

• KSBB Journal
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• v.11 no.2
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• pp.151-158
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• 1996

For the effective ethanol fermentation, the high concentration of sugar as the substrate of microbial fermentation is required. The most important reason in the inefficient hydrolysis; the easy deactivation of enzyme by temperature or shear stress and the severe inhibition effects of its products. In our work, we comprehended the kinetic characteristics of cellulose and ${\beta}$-glucosidase in the progress of hydrolysis, and observed the potential inhibitory effects of the hydrolyzed products and the deactivation of enzymes. We also tried to present the kinetic model of enzymatic hydrolysis of cellulose, which is applicable to process at the high concentration of sugar. Cellulase and ,${\beta}$-glucosidase exhibit diverse kinetic behaviors. At a level of only 5g/$\ell$ of glucose, the ${\beta}$-glucosidase activity was reduced by more than 70%. This result means that ${\beta}$-glucosldase was the most severely inhibited by glucose. Also at l0g/$\ell$ of cellobiose, the cellulose lost approximately 70% of its activity. ${\beta}$-glucosldase was more sensitive to deactivation than cellulose by about 1.6 times. The comprehensive kinetic model in the range of confidence was obtained and the agreement between the model prediction and the experimental data was reasonably good, testifying to the validity of the model equations used and the associated parameters.

• Journal of the Korean Society of Food Science and Nutrition
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• v.27 no.6
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• pp.1143-1147
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• 1998

Enzymatic characterization of peroxidase(E.C. 1.11.1.7) from soybean sprouts was investigated. The optimum pH of the purified peroxidase was 7.0 and relatively stable at pH 6.0~7.0. And the optimum temperature was 50oC. The enzyme was most active with guaiacol as a substrate, followed by (＋)catechin, pyrogallol and p phenylenediamine. The Km values for guaiacol and H2O2 were 4.2mM and 2.5mM, respectively. L Ascorbic acid and 2 mercaptoethanol greatly inhibited the enzyme activity, while Cu2+, Co2+ and Ni2+ activated the enzyme.