• Proceedings of the Korean Society for Applied Microbiology Conference
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• 1986.12a
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• pp.524.3-524
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• 1986

Carboxymethyl cellulase (CMCase) produced by cloned B. megaterium was found to contain 5.2% carbohydrate but no metal ion. The enzyme was isoelectric at pH 7.23 and was high is basic amino acids. The N-terminal of the enzyme was glutamic acid. The cellulolytic activity of this enzyme was extended to the small molecular substrates such as from cellotriose to cellopentaose. In additon, the enzyme showed transglycoslation activity. The pK values of the enzyme we estimated to be 4.4 and 6.7, andthat of the enzyme-substrate complex were 4.2 and 7.2, respectively. The enzyme was not affected by the treatment with iodoacetic acid, but the modification of enzyme with carbodiimide and diethyl pyrocarbonate resulted in a marked loss of the enzyme activity. These results suggest that the active site of enzyme essentially contains carboxylic and imidazole group of amino acid residues.

• The Korean Journal of Food And Nutrition
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• v.12 no.3
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• pp.265-270
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• 1999

The stabilization of Aspergillus sp. $\alpha$-amylase was attained by modification with periodate-oxidized sol-uble starch. The pH stability of modified enzyme was increased at pH 3~4 and 9~11 in the presence of $\alpha$-cyclodextrin($\alpha$-CD) compared with that of native enzyme. Thermal stability of the modified enzyme was increased. After treatment at 6$0^{\circ}C$ for 30min the activity remained 20% for the enzyme modified at pH 9.7 in the presence of $\alpha$-CD and tested in the presence of $\alpha$-CD 10% for the enzyme modified at pH 9.7 in the presence of $\alpha$-CD 0% for the native enzyme. The native enzyme and modified enzyme showed one peak in HPLC. The substrate specificity of the modified enzyme was not changed in HPLC analysis of reaction product.

• The Korean Journal of Food And Nutrition
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• v.16 no.2
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• pp.152-157
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• 2003

Serratia marcescens ATCC 25419 protease was purified to homogeneity by ammonium sulfate treatment, and DEAE-cellulose anion exchange chromatography. The specific activity of the enzyme was increased 448-fold during purification with an overall yield of 43.0%. Metal reactivation on the purified protease from S. marcescens was studied. S. marcescens protease was a metalloenzyme to be completely inhibited its activity by EDTA and the enzyme outstandingly inhibited by Hg, Fe, Cu, but the activity was increased approximately 20% by Co. The reactivation of the apoenzyme was effective with Mn, Co, Zn in pH range from 6 to 8. Among metalloenzymes prepared to the addition of Mn, Co, Zn to restore the degree of activity of native enzyme, Zn-enzyme was similar to the native enzyme in respects with enzyme activity, alkali-inactivation, thermo-stability.

• Bulletin of the Korean Chemical Society
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• v.1 no.1
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• pp.10-17
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• 1980

Penicillin amidohydrolase was partially purified from the fermented broth of Bacillus megaterium, and was immobilized on nylon fiber. The surface area of nylon fiber was increased by roughening it with fine sand and activated by acid treatment. The free amino groups on the nylon fiber exposed by such treatment were then utilized to immobilize the penicillin amidase. Enzymatic properties of penicillin amidohydrolase immobilized on the nylon fiber by covalent bonding and cross linking with glutaraldehyde were studied and compared with those of soluble enzyme. The optimal pH and temperature profile of immobilized enzyme showed only slightly broader peaks, and the values of kinetic constants, $K_m$, $K_{ia}$, and $K_{ip}$, of the immobilized enzyme are only slightly greater than those of the soluble enzyme. These results suggest that the mass transfer effect on the reaction rate for the penicillin amidase immobilized on nylon fiber is not so significant as the enzyme immobilized on some other support material like bentonite. The experimental results of batch reaction agreed well with the results of computer simulation for both the immobilized and soluble enzyme systems, confirming the validity of the rate equation derived which was based on the combined double inhibition by two reaction products.

• Journal of the Korean Society of Clothing and Textiles
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• v.28 no.7
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• pp.873-881
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• 2004

This research was aimed to investigate the effect of enzyme and the addition of chelators on rotting of the Kenaf bast. Enzyme rotting was effective only when the chelators were added with the enzyme. EDTA was a more effective chelator than oxalic acid under 1% concentration. There was no difference in the rotting effect under different enzyme concentration levels, and under different treatment time and temperature. Therefore, it was found that enzyme rotting can be carried out with low enzyme concentration(0.125%) at room temperature. Retting time can be shortened when higher enzyme concentration and higher temperature are applied. Cellulose I structure of kenaf fiber did not change after enzyme rotting, and different enzyme concentration did not affect the crytallinity structure. Non-cellulosic matters such as hemicellulose, lignin, and pectin were present in the descending order in the enzyme rotted kenaf fiber, and there were no differences in their amounts due to enzyme concentration levels. There was no difference in the dyeabilities of kenaf fiber rotted with different enzyme concentration levels. Enzyme rotted kenaf fiber showed better cyeability when pectin, lignin, and hemicellulose were removed.

• Journal of Nutrition and Health
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• v.33 no.6
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• pp.613-618
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• 2000

This study was to investigate the effect of dietary protein and fiber on the antioxidant enzyme activities of brain in acute or chronic ethanol-treated rats. Male Sprague-Dawley rats were fed on diets containing two levels of protein(7%, 20%) with two levels of fiber (5%, 10%) Rats were administered 40%(v/v) ethanol(5g/kg body weight)orally 90min before decaptiation in acute ethanol-treated groups and 25%(v/v) ethanol(5g/kg body weight) once a day for 5 weeks in chronic ethanol treated-groups. The rats were sacrificed after 5 weeks of feeding periods. Superoxide dismutase and gluthathione S-transferase activities were lower in chronic ethanol-treated groups than acute ethanol-treated groups whereas catalase and glutathuone peroxidase activities were significantly increased by chronic ethanol treatment. Low protein supplement accelerated to change of their activities however dietary fiber levels did not affect antioxidant enzyme activities. Chronic ethanol treatment and/or low protein supplement results in increasing the brain lipid peroxide content but in lowering glutathione level. (Korean J Nutrition 33(6) ; 613~618, 2000)

• Korean Journal of Fisheries and Aquatic Sciences
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• v.28 no.6
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• pp.728-735
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• 1995

The peptidyl prolyl cis-trans isomerase(PPlase, EC 5.2.2.8) from Bacillus stearothermophilus SIC1 was extracted from the cells treated with by lysozyme. PPlase was purified from the cell extracts by heat treatment, ammonium sulfate precipitation, ion exchange chromatography and finally gel filtration (FPLC). The purity of purified the enzyme after Superose 12 column chromatography was examined by sodium dodecyl sulfate polyacrylamide gel electrophoresis(SDS-PAGE). The molecular weight of the purified PPlase was estimated as 18,000 by SDS-PAGE. The 39 amino acid residues from the N-terminus were determined by the protein sequencer. The enzyme showed the optimum pH at 8.0 and was stable at the range of pH 7.0 to 8.0. The enzyme was considerably stable after heat treatment at $60^{\circ}C$ for 30 minutes, and the enzyme was quite stable up to $65^{\circ}C$. The presence of the PPlase in the refolding solution accelerated the isomerization rate of the assay peptide.

• Korean Journal of Food Science and Technology
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• v.48 no.6
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• pp.542-547
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• 2016

The thermal properties of ramie leaf ${\beta}$-amylase (RBA) were examined to develop a novel process for enzyme purification. The thermostability of RBA extract prepared from ramie leaf powder was examined at various temperatures. RBA activity decreased slightly, whereas other carbohydrate-active enzymes, such as $\small{D}$-enzyme, were rapidly inactivated during 30 min incubation at $60^{\circ}C$. When the heat-treated extract was incubated with various substrates, maltose was produced exclusively as the major product, whereas the untreated crude extract produced maltose and other maltooligosaccharides. In sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis, fewer protein bands were observed for the heat-treated extract than the untreated extract, indicating that the thermostable RBA was partially purified and other thermolabile enzymes were eliminated. Thus, the treatment of the RBA extract at $60^{\circ}C$ for 30 min resulted in 5.4-fold purification with a recovery yield of 90%.

• Proceedings of the Korea Technical Association of the Pulp and Paper Industry Conference
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• 1999.11b
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• pp.84-89
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• 1999

Treatment with the enzyme pectinase has been reported to lower the cationic demand of thermomechanical pulp(TMP) bleached with alkaline peroxide in the laboratory. We have extended this discovery to bleached TMP produced industrially, and shown that commercial enzyme preparations can treat pulp within 15 minutes at the at the temperature and pH values prevalent in paper mills. About half of the cationic demand in the bleached pulp can be destroyed by pectinase. Dynamic drainage jar experiments show that the enzyme treatment improves the effectiveness of several cationic polymers to increase retention in the absence of retention aids or with non-ionic polymers, and does not damage the strength properties of the pulp. Pectinase could be easily incorporated into paper machine stock preparation systems to lower the charges of cationic retention aids needed in furnishes containing peroxide-bleached mechanical pulp.

• Journal of Plant Biology
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• v.27 no.4
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• pp.241-251
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• 1984

The present study investigated the effects of triacontanol (TRIA) on plant growth and peroxisomal enzyme activities in radish seedlings. The optimum concentration of TRIA with respect to radish seedling bioassay was decided to 1.0mg $1^{-1}$. In comparison to untreated controls (including Tween 20 treatment), 1.0mg $1^{-1}$ TRIA treatment caused an increase in seed germination rate and root growth, but no stimulation in hypocotyl growth. Chlorophyll accumulation in cotyledon during carly development stage increased rapidly, and degradation of chlorophyll in later stage due to the cotyledon senesence was noticeably retarded. Increase of soluble protein content in cotyledon at early period of development was observed. Isocitrate lyase and catalase activity was not significantly different in both the treated and the untreated plants. But, glycolate oxidase activity was inhibited by TRIA down to 20% against controls. Also, the increase of the activity of peroxidase, a leaf-senescence marker enzyme, was continuously retarded over control for 8 days of development. Based on above results, TRIA was found to be active in both the growth and the peroxisomal enzyme activities of radish seedlings.