• Journal of Korea Technical Association of The Pulp and Paper Industry
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• v.37 no.3
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• pp.17-22
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• 2005

The cleaning efficiency of papermaking felt which is contaminated with fiber fines and various micro-materials was investigated and compared between the application of enzyme and commercial detergent. It was found that the cleaning efficiency by the treatment of acidic-based detergent was more efficient than that of alkaline-based one in the conventional commercial detergent. it was also observed that the treatment design of first acidic-based detergent treatment to second alkaline-based detergent procedure was better in the cleaning efficiency, compared to alkaline based-to-acidic based one. The cleaning property of felt with enzyme was resulted in good cleaning efficiency, without any addition of surfactant. Especially, the enzyme treatment under alkaline condition (pH 10) showed a better cleaning result than that under acidic condition(pH 5). The addition of nonionic surfactant to the enzyme increased the cleaning efficiency of felt and decreased the cationic demand of wastewater. These results showed more favour than the application of conventional commercial detergent.

• Asian-Australasian Journal of Animal Sciences
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• v.16 no.5
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• pp.677-684
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• 2003

Twenty eight multiparous lactating cows were utilized in an experiment to evaluate the response to an exogenous fibrolytic enzyme on their lactational performance during early lactation period (in terms of milk production, milk composition, feed intake, milking efficiency, body weight change) and the exact time of this response. Cows were randomized into two groups (14 each) with similar parities and were fed a concentrate ration of barley, ground corn, soybean meal, and wheat bran and roughage ration of alfalfa hay. One of the two groups was supplemented with the fibrolytic enzyme immediately after parturition up to 100 post partum. The experiment was of two phases with 50 days each. The enzyme, which has a cellulase/hemicellulase activity (derived from Trichoderma group), was added to the concentrate part of the ration in a dry powder form. Milk production, 3.5% fat corrected milk, energy corrected milk were higher (p<0.05) for cows fed treated diet. At the same time, No differences were observed in percentages of milk components, feed intake, body weight, body weight change, or rectal temperature for the whole experimental period or during any of the two phases. Efficiency of milk production was higher (p<0.05) for treatment group cows than for that of the control ones. However, efficiency was better during the second phase than during the first phase. Feeding enzyme treated diets to dairy cows improved lactational performance during early 100 day of the lactation period. However, the first 50 days of lactation looked to be the critical.

• Journal of Korea Technical Association of The Pulp and Paper Industry
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• v.47 no.1
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• pp.59-65
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• 2015

In this study, we evaluated optimum condition of enzyme with pH and temperature for preparation of microfibillated cellulose(MFC). Well-known endo-glucanase, three enzymes were used and CMC was used for substrate. Enzyme activity was evaluated using DNS method and absorbance with UV/VIS spectrophotometer. The enzyme shown the greatest activity was reacted with pulps at optimum condition for 1 hour and treated pulps beated until 100 mL CSF. Enzyme B and Enzyme L was the higher enzyme activity below 0.1% concentration and Enzyme N was the lowest enzyme activity. At various pH and temperature conditions, enzyme activity of Enzyme B was higher than the others at the same concentration. Especially enzyme activity at $50^{\circ}C$ of Enzyme B was almost not changed over pH 6.0. Optimum condition of three enzyme was pH 6 or pH 7 and $50^{\circ}C$ or $60^{\circ}C$. Also beating efficiency of enzyme treated pulps with Enzyme B is 55.6%.

• Journal of Microbiology and Biotechnology
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• v.8 no.4
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• pp.318-324
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• 1998

A ${\beta}$-galactosidase with high transgalactosylic activity was purified from a Bacillus species, registered as KFCC10855. The enzyme preparation showed a single protein band corresponding to a molecular mass of 150 kDa on SDS-PAGE and gave a single peak with the estimated molecular mass of 250 kDa on Sephacryl S-300 gel filtration, suggesting that the enzyme is a homodimeric protein. The amino acid and sugar analyses revealed that the enzyme is a glycoprotein, containing 19.2 weight percent of sugar moieties, and is much more abundant in hydrophilic amino acid residues than in hydrophobic residues, the mole ratio being about 2:1. The pI and optimum pH were determined to be 5.0 and 6.0, respectively. Having a temperature optimum at $70^{\circ}C$ for the hydrolysis of lactose, the enzyme showed good thermal stability. The activity of the enzyme preparation was markedly increased by the presence of exogenous Mg (II) and was decreased by the addition of EDTA. Among the metal ions examined, the most severely inhibitory effect was seen with Ag (I) and Hg (II). Further, results of protein modification by various chemical reagents implied that 1 cysteine, 1 histidine, and 2 methionine residues occur in certain critical sites of the enzyme, most likely including the active site. Enzyme kinetic parameters, measured for both hydrolysis and transgalactosylation of lactose, indicated that the enzyme has an excellent catalytic efficiency for formation of the transgalactosylic products in reaction mixtures containing high concentrations of the substrate.

• Journal of Biomedical Engineering Research
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• v.27 no.5
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• pp.267-273
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• 2006

Numerical analysis was performed on the enzyme transport and the flow fields in order to predict the effectiveness of urokinase injection regimens in clot dissolution. The species and momentum transport equations were numerically solved for the case of uniform perfusion of enzyme into a fibrin clot for an arterial thrombus and a deep vein thrombus models. In order to predict the thrombus lysis efficiency of continuous and forced intermittent injections, enzyme perfusion and clot lysis were simulated for the different injection velocities. Intermittent injection showed faster clot lysis compared to continuous perfusion, and lysis efficiency was increased as injection velocity increased.

• Journal of Korea Technical Association of The Pulp and Paper Industry
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• v.47 no.6
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• pp.57-65
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• 2015

Microfibrillated cellulose (MFC) or Nanofibrillated cellulose (NFC) has been used to reduce the use of raw pulp and to improve paper strength. The problem of MFC preparation is high manufacturing cost. In this study, it was carried out to prepare MFC after enzyme beating and estimated properties of MFC. Endo-D was the best beating efficiency among three type of endo-glucanase. As the grinder pass number increased, the viscosity and the fines of MFC suspension increased while the crystallinity and the porosity of MFC sheet decreased. Also enzyme beating MFC was higher value in the crystallinity and lower value in the viscosity than non-enzyme MFC. In addition, the aspect ratio of MFC was the highest at 5 pass. MFC addition improved the handsheet strength and the air permeability but worsened the drainage.

• Biomolecules & Therapeutics
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• v.27 no.6
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• pp.577-583
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• 2019

Human cytochrome P450 2C9 is a highly polymorphic enzyme that is required for drug and xenobiotic metabolism. Here, we studied eleven P450 2C9 genetic variants-including three novel variants F69S, L310V, and Q324X-that were clinically identified in Korean patients. P450 2C9 variant enzymes were expressed in Escherichia coli and their bicistronic membrane fractions were prepared The CO-binding spectra were obtained for nine enzyme variants, indicating P450 holoenzymes, but not for the M02 (L90P) variant. The M11 (Q324X) variant could not be expressed due to an early nonsense mutation. LC-MS/MS analysis was performed to measure the catalytic activities of the P450 2C9 variants, using diclofenac as a substrate. Steady-state kinetic analysis revealed that the catalytic efficiency of all nine P450 2C9 variants was lower than that of the wild type P450 2C9 enzyme. The M05 (R150L) and M06 (P279T) variants showed high $k_{cat}$ values; however, their $K_m$ values were also high. As the M01 (F69S), M03 (R124Q), M04 (R125H), M08 (I359L), M09 (I359T), and M10 (A477T) variants exhibited higher $K_m$ and lower $k_{cat}$ values than that of the wild type enzyme, their catalytic efficiency decreased by approximately 50-fold compared to the wild type enzyme. Furthermore, the novel variant M07 (L310V) showed lower $k_{cat}$ and $K_m$ values than the wild type enzyme, which resulted in its decreased (80%) catalytic efficiency. The X-ray crystal structure of P450 2C9 revealed the presence of mutations in the residues surrounding the substrate-binding cavity. Functional characterization of these genetic variants can help understand the pharmacogenetic outcomes.

• Asian-Australasian Journal of Animal Sciences
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• v.19 no.10
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• pp.1470-1477
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• 2006

One hundred and sixty crossbred pigs ($6.62{\pm}0.36kg$) weaned at day $18{\pm}1$ were used to investigate the effects of lactitol and tributyrin on performance, small intestinal morphology and enzyme activity. The pigs were assigned to one of five dietary groups (4 pens/diet with 8 pigs/pen) and were fed the negative control diet or the negative control diet supplemented with 10 g/kg glutamine (as a positive control), or 3 g/kg lactitol (${\beta}$-D-galactopyranosyl-($1{\rightarrow}4$)-D-sorbitol), or 5 g/kg tributyrin (butanoic acid 1,2,3-propanetriyl ester), or 3 g/kg lactitol+5 g/kg tributyrin. Body weight and feed intake were measured weekly during the 4-week study. On day 7, four pigs per dietary treatment were sacrificed to examine small intestinal morphology and enzyme activity. The results showed that: (1) Compared with the negative control diet, the positive control diet improved weight gain and feed efficiency during weeks 1-2 and over the entire study (p<0.05), and also decreased duodenal and ileal crypt depth (p<0.05), but did not alter intestinal enzyme activity (p>0.05). Lactitol improved feed efficiency during weeks 3-4 and over the entire study (p<0.05), but did not improve weight gain and feed intake, intestinal morphology or enzyme activity (p>0.05). Tributyrin improved weight gain and reduced feed/gain during weeks 3-4 and over the entire study. Tributyrin significantly decreased crypt depth in the duodenum and ileum, and increased duodenal lactase and ileal maltase activity (p<0.05). Lactitol+tributyrin increased weight gain during weeks 3-4 and over the entire study, and improved feed efficiency during weeks 1-2 and 3-4 and over the entire study (p<0.05). Lactitol+tributyrin increased the jejunal villus height, and decreased the duodenal and ileal crypt depth (p<0.05). Lactitol+tributyrin also increased jejunal lactase and sucrase activity (p<0.05). (2) Compared with the positive control, tributyrin improved weight gain and reduced feed/gain during weeks 3-4 (p<0.05), decreased the ileal crypt depth, and improved the duodenal lactase and sucrase activity (p<0.05). Lactitol+ tributyrin improved weight gain during weeks 3-4, improved feed efficiency during weeks 3-4 and over the entire study, increased the ileal villus height, and increased jejunal lactase, sucrase and maltase activity (p<0.05). These results showed that tributyrin improved performance, intestinal morphology and enzyme activity, while the effect of lactitol was very limited. These results also showed that, compared with glutamine, tributyrin was more effective in improving intestinal morphology and enzyme activity, and tributyrin exerted a superior effect in improving performance as weaning progressed. These observations suggest that, as a chemical for repairing intestinal atrophy, glutamine and tributyrin should be used in the first and second periods of the starter phase, respectively.

• Asian-Australasian Journal of Animal Sciences
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• v.27 no.5
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• pp.700-705
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• 2014

A 12-week feeding trial was conducted with 87 g rainbow trout to evaluate the effects on growth performances, feed efficiency and nutrient digestibility of adding ${\beta}$-mannanase and ${\alpha}$-galactosidase enzymes, solely or in combination. Seven diets were prepared by adding ${\beta}$-mannanase, ${\alpha}$-galactosidase and mixed enzyme at two different levels (1 g/kg and 2 g/kg) to control diet (without enzyme) including soybean meal. Mixed enzymes (1 g/kg, 2 g/kg) were prepared by adding ${\beta}$-mannanase and ${\alpha}$-galactosidase at the same doses (0.5+0.5 g/kg and 1+1 g/kg). At the end of the experiment, addition of ${\beta}$-mannanase, ${\alpha}$-galactosidase and mixed enzyme to diet containing 44% soybean meal had no significant effects on growth performance and gain:feed (p>0.05). In addition, adding ${\beta}$-mannanase, ${\alpha}$-galactosidase and mixed enzyme in different rations to trout diets had no affect on nutrient digestibility and body composition (p>0.05).

• Journal of Photoscience
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• v.11 no.3
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• pp.121-127
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• 2004

The${\beta}$-glucosidases occur widely in all living organisms and has in general a tendency to form oligomers of varying numbers of subunits or aggregates, although the functional implications of such diverse oligomerization schemes remain unclear. In particular, the assembly mode of the oat ${\beta}$-glucosidase is very unique in that it multimerizes by linear stacking of a hexameric building block to form long fibrillar multimers. Some structural proteins such as actin and tubulin assemble into long fibrils in a helical fashion and several enzymes such as GroEL and Pyrodictium ATPase functional complexes, 20S proteasome of the archaebacterium Thermoplasma acidophilum, and lutamine synthetase fromblue-green algae, assemble into discrete oligomers upto 4 stacked rings to maintain their enzymatic activities. In particular, oat ${\beta}$-glucosidase exists in vivo as a discrete long fibrillar multimer assembly that is a novel structure for enzyme protein. It is assembled by linear stacking of hollow trimeric units. The fibril has a long central tunnel connecting to the outer medium via regularly distributed side fenestrations. The enzyme active sites are located within the central tunnel and multimerization increases enzyme affinity to the substrates and catalytic efficiency of the enzyme. Although it is suggested that oligomerization may contribute to the enzyme stability and catalytic efficiency of ${\beta}$-glycosidases, the functional implications of such diverse oligomerization schemes remain unclear so far.