• Proceedings of the Korean Society for Applied Microbiology Conference
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• 1986.12a
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• pp.532.2-532
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• 1986

Alkaline protease which is an important enzyme used in detergents, leather tanning and food industry was produced by alkalophilic bacterium, Bacillus sp. KCTC 1723 isolated from soil. The maximum productivity of the enzyme in alkaline medium containing 1% sodium bicarbonate was obtained by incubating for 3 days at 37$^{\circ}C$. The optimum pH of the enzyme was 11.5 and calcium ion was effective on stabilization of the enzyme at high temperature. The enzyme was not inhibited by metal chelating agent such as El)TA but inhibited by diisopropyl fluorophosphate. Purification of the enzyme was carried out DEAE- and CM-cellulose column chromatographies and molecular weight of the purified enzyme was determined

• Journal of Conservation Science
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• v.35 no.4
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• pp.363-372
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• 2019

Animal glue has been used as a binder in Dancheong since the Joseon dynasty. Binders play an important role in determining the physical characteristics of a painting layer. The analysis of binders can be used to identify the materials and techniques used in traditional Dancheong. Binders can be investigated using physicochemical component analyses methods such as gas chromatography/mass spectrometry, pyrolysis-gas chromatography/mass spectrometry, and fourier transform infrared spectroscopy, but the detection characteristics vary depending on the degradation properties of the pigment and binder. Therefore, cross-validation using a combination of physicochemical analysis and enzyme immunoassay is used to increase the reliability of the results. In this study, we present an enzyme-linked immunosorbent assay (ELISA) as an example of an enzyme immunoassay as a method for analyzing animal glue, a traditional binder used in Korea. The applicability of ELISA was tested using commercial animal glue, in addition to animal glue produced using a variety of extraction conditions. The animal glue was analyzed in a Noerok-additionally coated-replica sample to evaluate the possibility of analyzing the animal glue in a paint layer mixed with pigment. Based on the results, we performed an assay on the use of animal glue in the Dancheong sample of the temples of the Joseon dynasty, that are estimated to have been built in the 17^th century.

• Geomechanics and Engineering
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• v.19 no.1
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• pp.21-28
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• 2019

Use of cement in stabilizing the sulfate-bearing clay soils forms ettringite/ thaumasite in the presence of moisture leads to excessive swelling and causes damages to structures built on them. The development and use of non-traditional stabilisers such as alkali activated ground granulated blast-furnace slag (AGGBS) and enzyme for soil stabilisation is recommended because of its lower cost and the non detrimental effects on the environment. The objective of the study is to investigate the effectiveness of AGGBS and enzyme on improving the volume change properties of sulfate bearing soil as compared to ordinary Portland cement (OPC). The soil for present study has been collected from Tilda, Chhattisgarh, India and 5000 ppm of sodium sulfate has been added. Various dosages of the selected stabilizers have been used and the effect on plasticity index, differential swell index and swelling pressure has been evaluated. XRD, SEM and EDX were also done on the untreated and treated soil for identifying the mineralogical and microstructural changes. The tests results show that the AGGBS and enzyme treated soil reduces swelling and plasticity characteristics whereas OPC treated soil shows an increase in swelling behaviour. It is observed that the swell pressure of the OPC-treated sulfate bearing soil became 1.5 times higher than that of the OPC treated non-sulfate soil.

• Journal of the Korean Society of Food Science and Nutrition
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• v.19 no.6
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• pp.577-582
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• 1990

Production and properties of invertase from Aspergillus niger were investigated. Inulin and sucrose were best carbon source and yeast extract was most suitable for the production of the enzyme among tested carbon and nitrogen sources. The enzyme among tested carbon and nitrogen sources. The enzyme was maximally produced by cultivating the organism at medium of pH 4.5 and temperature of 3$0^{\circ}C$ The optimum pH and temperature for the enzyme activity were pH 5.0 and temperature of 5$0^{\circ}C$, respectively. Among tested metal ions. Hg++, Cu++ and Ag+ ions Inhibited the enzyme activity drastically.

• The Korean Journal of Food And Nutrition
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• v.34 no.6
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• pp.612-620
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• 2021

To increase the utilization of Centella asiatica (CA), enzymes such as cellulase and pectinase were added and the physicochemical properties of the treated CA were analyzed. In addition, apple-CA jam was prepared using the enzyme-treated CA, which had the best antioxidant properties, and the physicochemical and sensory qualities of the jam were measured. There was a high content of ascorbic acid, polyphenols, flavonoids, reducing sugar, amino acid, minerals and DPPH radical scavenging activity in the enzyme-treated group. The antioxidant component and activity in the jam prepared by adding enzyme-treated CA increased with an increase in the amount of enzyme-treated CA. In the soluble solids, the higher the amount of enzyme-treated CA, the higher the value, but there was no significant difference in pH. The sensory evaluation of the jam, in particular the taste, showed that the highest preference was observed when the enzyme-treated CA was added in the range of 5.0~6.7%, and the control group showed the lowest preference. There was no significant difference in flavor and spreadability among the treatment groups, however, the control group showed the highest color preference. In the overall acceptability, when 5.0% of enzyme-treated CA was added, the highest acceptability was shown.

• Microbiology and Biotechnology Letters
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• v.20 no.2
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• pp.143-149
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• 1992

A bacterial strain No. 2, which highly produced a-glucosidase, was isolated from Kimchi and identified to be a similar species of Pediococcus halophilus. This enzyme was purified by protamine sulfate, ammonium sulfate fractionation, ion exchange and gel filtration. The maximal a-glucosidase activity was observed at pH 6.0 and this enzyme was stable at pH 6.0~ 7.5. The optimum temperature of this enzyme activity was $37^{\circ}C$, but enzyme activity was gradually lost above $37^{\circ}C$. This enzyme was activated by 10 mM MgCh and inhibited by 10 mM mercaptoethanol. The kinetics of PNPG(p-Nitrophenyl-a-D-glucopyranoside) and maltose were Kp0.52 mM/27.5 pg protein, $V_{max}$= 0.021 mM/min 27.5 ${\mu}g$ protein and $K_m$= 0.32 mMD7.5 ${\mu}g$ protein, $V_{max}$= 0.025 mM/min 27.5 ${\mu}g$ protein, respectively. The molecular weight of $\alpha$-glucosidase was about 37, 000.

• Journal of Ginseng Research
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• v.7 no.1
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• pp.80-87
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• 1983

In an endeavour to elucidate effects of ginseng on some characteristics of enzymes, malate dehydrogenase (EC 1.1.1.37) was chosen as a model enzyme and effects of ginseng saponin on the enzyme such as optimum pH, product inhibition, optimum temperature and the activity was investigated. The product inhibition by NADH-a reaction product of the enzyme-was increased 33% by 0.3% ginseng saponin. And the optimum pH of the enzyme was 8.3 but in the presence of 0.3% ginseng saponin it increased to 8.5. The enzyme activity and the optimum temperature was not affected by ginseng saponin in the concentration of 1.0% and 0.3%, respectively. In this work, the possibility of contribution of ginseng saponin to the adaptogen activity is suggested; Potentiation of the regulatory activity of an enzyme may contribute to the normalization of the physiological state and consequently may increase the nonspecific resistance of an organism.

• Proceedings of the Korea Technical Association of the Pulp and Paper Industry Conference
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• 2000.04a
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• pp.39-46
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• 2000

In pulp and papermaking process, enzymatic treatment of pulp fibres has been a topic of increasing interest in last decade. Lots of patents, papers and research reports were published on the application of enzymes in the fields of enzymatic bleaching, deinking, slime control, pitch control, waste water treatment and fibre modification. Cellulase and hemicellulase are the principal enzymes used for the modification of fibre property. This study was carried out for determinating the behaviors of enzyme to pulp fibres. A commercial enzyme, Denimax BT which is consisted with cellulase and hemicellulase, was treated to the kraft pulp produced from domestic hardwood mixtures. Results were mainly concentrated on the behaviors of freeness, drainability and fines content of fibres, and physical properties of paper with enzyme treatment. The freeness levels and dewatering ability were developed, and the fines contents were decreased. The creation of fines were controlled by the method of pre-enzyme treatment prior to fibre beating. The mechanical strength of paper, like tensile, burst, tear strength and folding endurance, were remarkably improved by the pre-enzyme treatment.

• Korean Journal of Microbiology
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• v.29 no.6
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• pp.345-352
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• 1991

A serine proteinase of molecular weight 60 kd was purified from culture supernatant of P. aeruginosa using DEAE-Trisacryl M ion-exchange and AcA 54 gel filtration column chromatography, and the properties of serine proteinase were characterized. By means of SDS-polyacrylamide gel electrophoresis, the molecular weight of the enzyme was 55 kd. The optimal pH for the activity of purified enzyme was 7.5. The activity of the purified enzyme was completely inhibited by Di-isopropylfluorophosphate(DFP) and N-.alpha.-p-tosyl-L-lysine choloromethyl detone(TLCK) but not by other proteinase inhibitors such as E-64, pepstatin A, 1, 10-phenanthroline. The purified enzyme was capable of degrading type I and type IV collagen. Antisera obtained from hymans infected with Pseudomonas aeruginosa reacted to the purified serine proteinase in immunoblots. These results indicate that the purified enzyme is trypsin-like serine proteinase and this enzyme of P. aeruginosa may play an important role in tissue damage as a spreading factor and may be useful for serodiagnosis of Pseudomonas infections.

• Journal of Microbiology and Biotechnology
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• v.6 no.6
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• pp.407-413
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• 1996

A novel type of extracellular phospholipase $A_1$ was isolated from Serratia sp. MK1 and purified to homogeneity by ammonium sulfate precipitation, anion exchange and gel filtration chromatography. The purified enzyme was a monomer with a molecular mass of about 43, 000 Da. This enzyme showed the highest lipolytic activity toward phosphatidylserine among the phosphoglycerides tested, and preferentially catalyzed the hydrolysis of the ester bond in phosphatidic acid to lyso-phosphatidic acid. Enzyme activity was completely inhibited by the addition of a chelating agent such as EDTA, and inhibited enzyme activity was fully recovered by the presence of $Ca^{2+}$. This implies that the enzyme requires $Ca^{2+}$ for activity. The enzyme was stable up to $70^{\circ}C$ when incubated for 1 h at pH 8.5, and the optimal pH and temperature were 8.5 and $50^{\circ}C$, respectively.