• BMB Reports
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• v.37 no.4
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• pp.394-401
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• 2004

The purpose of this paper is to suggest that the prominence of Haldane's explanation for enzyme catalysis significantly hinders investigations in understanding enzyme structure and function. This occurs despite the existence of much evidence that the Haldane model cannot embrace. Some of the evidence, in fact, disproves the model. A brief history of the explanation of enzyme catalysis is presented. The currently accepted view of enzyme catalysis -- the Haldane model -- is examined in terms of its strengths and weaknesses. An alternate model for general enzyme catalysis (the Shifting Specificity model) is reintroduced and an assessment of why it may be superior to the Haldane model is presented. Finally, it is proposed that a re-examination of many current aspects in enzyme structure and function (specifically, protein folding, x-ray and NMR structure analyses, enzyme stability curves, enzyme mimics, catalytic antibodies, and the loose packing of enzyme folded forms) in terms of the new model may offer crucial insights.

• Journal of Environmental Science International
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• v.31 no.3
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• pp.227-235
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• 2022

In this study, a biodegradation model of based on molecular cellulose was established. It is a mathematical, kinetic model, assuming that two major enzymes randomly break glycosidic bonds of cellulose molecules, and calculates the number of molecules by applying the corresponding probability and degradation reaction coefficients. Model calculations considered enzyme dose, cellulose chain length, and reaction rate constant ratio. Degradation increased almost by two folds with increase of temperature (5℃→25℃). The change of degradation was not significant over the higher temperatures. As temperature increased, the degradation rate of the molecules increased along with higher production of shorter chain molecules. As the reaction rates of the two enzymes were comparative the degree of degradation for any combinations of enzyme application was not affected much. Enzyme dose was also tested through experiment. While enzyme dose ranged from 1 mg/L to 10 mg/L, the gap between real data and model calculations was trivial. However, at higher dose of those enzymes (>15 mg/L), the experimental result showed the lower concentrations of reductive sugar than the corresponding model calculation did. We determined that the optimal enzyme dose for maximum generation of reductive sugar was 10 mg/L.

• Journal of Korea Technical Association of The Pulp and Paper Industry
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• v.31 no.3
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• pp.1-9
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• 1999

Effect of furnish on enzyme activity was investigated by using the three components (cellulose, enzyme, and cationic polyelectrolyte) model papermaking system. Avicel was used as a cellulose model compound to observe the effect of adsorption and desorption of enzyme with other component and the resultant change of particle size. As an experimental result, the enzyme loses considerably its apparent activity due to the adsorption onto cellulose and cationic polyelectrolyte. Activities of enzyme applied to the actual papermaking stocks having controlled fiber length showed different behavior in terms of pulp species UKP and KOCC stocks. That is, the enzyme activity in UKP was increased as fines content increased, however, vice versa in KOCC stock . This result can be considered to be the existence of various contaminants included in the fines of KOCC . The effect of possible contaminants such as inorganic materials, calcium ion, surfactant, and conductivity on enzyme activity were also investigated.

• Microbiology and Biotechnology Letters
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• v.23 no.4
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• pp.425-431
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• 1995

A kinetic model of the cyclodextrin formation in a heterogeneous enzyme reaction system using swollen extrusion starch as substrate was derived emphasing the structural features of extrusion starch. The degree of gelatinization, the ratio of accessible and inaccessible portion of extrusion starch, adsorption of CGTase on swollen starch, the structural transformation during reaction, and product inhibition caused by produced CDs were considered in deriving kinetic model. Various kinetic constants were also evaluated. The derived kinetic equation was numerically simulated, which result showed that the derived kinetic equations can be used to predict the experimental data reasonably well under the various experimental conditions. Kinetic model can be utilized for the optimization of enzyme reactor and the process development for CD production from swollen extrusion starch.

• Proceedings of the Korean Society for Applied Microbiology Conference
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• 1986.12a
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• pp.510.1-510
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• 1986

Many enzymes require the participation of readily dissociable coenzymes as NAD for thir catalytic activities. The continuous utilization of the enzymes requires the retention and regeneration of the coenzymes. For this purpose, several kinds of macromolecular NAD derivatives have been prepared by covalently attaching NAD to watersoluble polymers. We have prepared poly (ethylene glycol)-bound NAD (PEG-NAD) by coupling N$\^$6/-(2-carboxyethyl)-NAD to one terminal of ${\gamma}$ $\omega$-diaminoly (ethylene glycol) (Mr 3000) with water-soluble carbodiimide. PED-NAD thus obtained has one NAD moiety located at a terminal of the linear, flexible and hydrophilic chain of poly (ethylene glycol). PED-NAD has good coenzyme activity for various dehydrogenases and is applicable in a continuous enzyme reactor. To use these macromolecular NAD derivatives in an enzyme reactor, it si necessary to understand the behavior of the system in which the reactions of dehydrogenases are coupled by the recycling of the NAD derivative. We investigated the kinetic properties of a continuous enzyme reactor containing lactate dehydrogenase, alcohol dehydrogenase and PEG-NAD. The steady-state behavior of the enzyme reactor is explained by a simple kinetic model.

• Journal of Sensor Science and Technology
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• v.3 no.2
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• pp.16-23
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• 1994

Developed fiber-optic biosensor for the detection of organophosphorus compounds in a contaminated water needs the analysis of an enzyme kinetics and the transport phenomena in the reaction part to analyze the sensor signal and to design the sensor. The enzyme inhibition kinetics was investigated and the reactor model was proposed to design the reaction part in the proposed sensor. Since the acetylcholinesterase was inhibited by the organophosphorus compounds, experiments for enzyme inhibition reaction were performed from 0 to 2 ppm to be detected by the developed sensor, and irreversible enzyme inhibition kinetics was proposed. The reactor parts were divided into the two phases, i.e. bulk phase and immobilized enzyme layer, to analyze the flow and diffusion. Sensor signal was able to be analyzed based on the total reactor model established by linking the enzyme reaction kinetics. Based on the proposed model, the effects of loading enzyme amount and enzyme layer thickness on the magnitude of readout signal were simulated.

• Journal of The Korean Society of Grassland and Forage Science
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• v.36 no.3
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• pp.248-256
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• 2016

The present study investigated the effect of enzyme inclusion on silage quality using meta-analysis tool. A total of 16 research papers reporting the effect of enzyme application on silage quality were employed in the meta-analysis of this study. Mixed model for integrating quantitative results from multiple studies was used first to calculate the predicted error of each study. Individual error from the estimated model was the applied into standard deviation of each study to calculate the mean difference. Finally, summary effect was determined using standard mean difference (SMD) and inversed variance weighting. Mixed model analysis and SMD analysis showed the same effect patterns in all analysis items. Enzyme inclusion in silage significantly (p < 0.05) altered all silage quality characteristics investigated compared to control when enzyme was not included. Our results showed that enzyme treatment increased dry matter content, preserved crude protein effectively, and elevated water soluble carbohydrate content. However, the pH value, acetic acid, propionic acid, neutral detergent fiber, and acid detergent fiber contents in silage with enzyme inclusion were lower than those of the control.

• BMB Reports
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• v.37 no.5
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• pp.533-537
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• 2004

Previously published kinetic data on the interactions of seventeen different enzymes with their physiological substrates are re-examined in order to understand the connection between ground state binding energy and transition state stabilization of the enzyme-catalyzed reactions. When the substrate ground state binding energies are normalized by the substrate molar volumes, binding of the substrate to the enzyme active site may be thought of as an energy concentration interaction; that is, binding of the substrate ground state brings in a certain concentration of energy. When kinetic data of the enzyme/substrate interactions are analyzed from this point of view, the following relationships are discovered: 1) smaller substrates possess more binding energy concentrations than do larger substrates with the effect dropping off exponentially, 2) larger enzymes (relative to substrate size) bind both the ground and transition states more tightly than smaller enzymes, and 3) high substrate ground state binding energy concentration is associated with greater reaction transition state stabilization. It is proposed that these observations are inconsistent with the conventional (Haldane) view of enzyme catalysis and are better reconciled with the shifting specificity model for enzyme catalysis.

• Biotechnology and Bioprocess Engineering:BBE
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• v.6 no.2
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• pp.150-155
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• 2001

It has been observed that water, which is absolutely essential for enzyme activity, can induce the agglomeration of enzyme particles in organic media. Although enzyme agglomeration is significant in that it usually reduces enzyme activity and stability, little attention has been paid to the quantitative analysis of enzyme agglomeration behavior in nonaqueous biocatalytic systems. In this study, the effect of water and silica gel on enzyme agglomeration were investigated using Candida rugosa lipase and cyclohexane as a model enzyme and an organic medium. The extent of enzyme agglomeration was quantified by sieve analysis of freeze-dried agglomerates. Increasing the water content of the medium increased the size of the enzyme agglomerates, and it was found that water produced during the esterification reaction could also promote the agglomeration of enzyme particles suspended in organic media. On the other hand, the size of the enzyme agglomerates was remarkably reduced in the presence of silica gel at the same water content. We also show that this increase in the size of enzyme agglomerates results in lower reaction rates in organic solvents.

• KOREAN JOURNAL OF PACKAGING SCIENCE & TECHNOLOGY
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• v.21 no.1
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• pp.1-10
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• 2015

Enzyme kinetics-based respiration model can be effectively used for estimating respiration rate in $O_2$ consumption and $CO_2$ production of fresh produce as a function of $O_2$ and $CO_2$ concentrations. Arrhenius equation can be applied to describe the temperature dependence of the respiration rate. Parameters of enzyme kinetics-based respiration model and activation energy of Arrhenius equation were compiled from analysis of literature data and closed system experiment. They enable to estimate the respiration rate for any modified atmosphere conditions at temperature of interest and thus can be used for design of modified atmosphere packaging of fresh produce.