• Journal of the Korean Society of Food Science and Nutrition
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• v.24 no.4
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• pp.563-569
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• 1995

Myrosinase from Korean cabbage(Bogdoli) was purified and its enzymatic properties were investigated. Myrosinase from the Korean cabbage was purified by DEAE Bio-Gel Sepharose, Concanavalin-A, and Mono-Q column chromatography and exhibited a 55KD molecular weight with a single band on the gel of SDS-PAGE. The enzyme was purified about 21-fold compared to its crude enzyme and a specific activity of purified enzyme was 15, 120units/mg. Optimum pH of the myrosinase was 7.0 in both phosphate and Tris-HCl buffer solutions, the enzyme was stable at pH 6.5~7.0. Optimum temperature of enzyme was 37~38$^{\circ}C$. The enzyme activity was significantly inhibited by Cu2+ and Hg2+, but enhanced by ascorbic acid, resulting in a maximum activity at 1mM ascorbic acid. Among the ascorbic acid analogues, dehydro-ascorbic acid did not affect, whereas others showed a little effect on the enzyme activity, but less than ascorbic acid itself. Reducing agents such as 2-mercaptoethanol and dithiothreitol had no effect on the enzyme activity, but the enzyme activity was enhanced when 2-mercaptoethanol was mixed with ascorbic acid.

• Journal of Microbiology
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• v.34 no.3
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• pp.270-273
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• 1996

Micrococcus luteus purine nucleoside phosphorylase (PNP) has been purified and characterized. The physical and kinetic properties have been described previously. Chemical modification of the enzyme was attempted to gain insight on the active site. The enzyme was inactivated in a time-dependent manner by the arginine- specific modifying reagent phenylglyoxal. There was a linear relationship between the observed rate of inactivation and the phenylglyoxal concentration. At 30 $^{\circ}C$ the bimolecular rate constant for the modification was 0.015 $min^{-1}mM^{-1}$ in 50 mM $NaHCO_3$ buffer, pH 7.5. The plot of logk versus log phenylglyoxal concentration was a strainght line with a slope value of 0.9, indicating that modification of one arginine residue was needed to inactivate the enzyme. Preincubation with saturated solutions of substrates protected the enzyme from inhibition of phenylglyoxal, indicating that reactions with phenylglyoxal were directed at arginyl residues essential for the catalytic functioning of the enzyme.

• Korean Journal of Food Science and Technology
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• v.46 no.5
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• pp.581-587
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• 2014

The antioxidant and alcohol-degrading enzyme activities of soybean sprout sugar solutions (oligosaccharide and sucrose, $50^{\circ}Bx$) were characterized under different soaking conditions. The ratio of sugar solution to sprout content was 25%, 50%, and 75% (w/w), and the soaking times studied were 1, 3, 6, 12, and 24 h. Higher 1,1-diphenyl-2-pycrylhydrazyl (DPPH) radical-scavenging activity was detected in case of the oligosaccharide solution, compared to the sucrose solution. A similar tendency was observed for alcohol-degrading enzyme activity. When the ratio of sugar solution to sprout content was 50% (w/w), the total phenol and flavonoid contents were found to be higher, compared to those observed at 20% (w/w). However, we did not observe a significant difference between 50% and 75% (w/w). Soaking time did not significantly affect the antioxidant and alcohol-degrading enzyme activities of the solutions. As a result, when oligosaccharide solution was used for soaking soy sprouts at a ratio of >50% (w/w), higher antioxidant and alcoholdegrading enzyme activities were observed.

• Korean Journal of Microbiology
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• v.23 no.4
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• pp.297-301
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• 1985

The dependence of activities of Aspergillus phoenicis on the culture conditions in the progesterone transformation reaction was investigated. In the beginning of the reaction, $6{\beta},\;11{\alpha}-dihydroxyprogesterone$ was not produced even at high concentration of $11{\alpha}-hydroxyprogesterone$. However, large amount of the product was obtained after the complete exhaustion of progesterone. When spores of A.phoenicis replaced mycelia as enzyme source, $11{\alpha}-hydroxyprogesterone$ was produced after a considerably long indyction period, and its maximum production rate followed the exponential growth phase. The $6{\beta}-hydroxylation\;of\;11{\alpha}-hydroxyprogesterone$ continued, even after the stationary growth phase. A. phoenicis showed high enzyme activity for these reactions when the phosphate buffer solutions were used in place of the ordinary culture medium. The buffer solutions of low pH gave more yield of $11{\alpha}-hydroxyprogesterone$ than those of high pH. However, the addition of flucose to the buffer solutions did not activate the transformation reaction. The presence of progesterone seems to be necessary for the induction of enzymes for the $6{\beta}-hydroxylation\;of\;11{\alpha}-hydroxyprogesterone\;since\;6{\beta},\;11{\alpha}-dihydroxyprogesterone$ is not produced in the reaction medium containing only $11{\alpha}-hydroxyprogesterone$ as a substrate.

• Textile Coloration and Finishing
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• v.24 no.1
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• pp.18-26
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• 2012

In this work, colorants extraction process from gromwell was studied for making powder form of colorants by solving the high viscosity problem of gromwell extracts. In order to do that, sugar extracted together with colorants must be pre-extracted. For sugar decomposition, gromwell roots were pretreated with various enzyme solutions. The total sugar content of pre-extract with enzyme solution was measured. Accordingly, the effects of enzyme type and pretreatment condition on sugar decomposition were investigated to find appropriate enzyme(amylase, hemicellulase, pectinase) and enzyme activity (100~1000unit), pre-extracted time(3~24hr). Color characteristics and dye uptake of dyed fabrics were evaluated. Gromwell colorants were assessed for their potential antimicrobial activities, which possibly expand their end use as functional pigments. The efficiency of removing sugar was increased in the order of hemicellulase, pectinase, amylase, $H_2O$. Gromwell colorants powder yield was in the range of 4.4% to 9.8% depending on pretreatment enzyme. Gromwell colorants produced RP color on the silk and wool fabrics with good dye uptake. Antimicrobial activity of gromwell colorants will greatly increase its potentiality for applying as functional natural colorants in the future.

• Journal of the Korean Society of Clothing and Textiles
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• v.26 no.7
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• pp.1085-1092
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• 2002

Changes in laundering habits and the efficacy claims made for oxygen bleach added to detergents necessitate a deeper investigation into the testing of the washing efficacy of detergents and washing process. The effect of the addition of a sodium percarbonate and bleach activator TAED to an enzyme containing detergent on the soil removal and antimicrobial properties were investigated with the measuring of residual H$_2$O$_2$. The addition of sodium percarbonates to enzyme containing detergent lowered the soil removal of EMPA 116 cloth. But sodium percarbonates had greater effects on that of colored stained cloths such as EMPA 115 and artificially soiled with wine and red pepper while they were presoaked at 20$^{\circ}C$ or higher for So minutes or longer. Most of hydrogen peroxide was remained after washing. Over 99.9% of Staphylococcus aureus on the cotton cloth was removed in every washing solutions, but the cloth washed with enzyme containing detergent or detergent with oxygen bleach didn't show the antimicrobial property.

• Mycobiology
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• v.42 no.1
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• pp.41-45
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• 2014

The effectiveness of three kinds of enzymes (chitinase, ${\beta}$-glucuronidase, and lysing enzyme complex), employed as elicitors to enhance the ${\beta}$-glucan content in the sawdust-based cultivation of cauliflower mushroom (Sparassis latifolia), was examined. The elicitors were applied to the cauliflower mushroom after primordium formation, by spraying the enzyme solutions at three different levels on the sawdust-based medium. Mycelial growth was fully accomplished by the treatments, but the metabolic process during the growth of fruiting bodies was affected. The application of a lysing enzyme resulted in an increase in the ${\beta}$-glucan concentration by up to 31% compared to that of the control. However, the treatment resulted in a decrease in mushroom yield, which necessitated the need to evaluate its economic efficiency. Although we still need to develop a more efficient way for using elicitors to enhance functional metabolites in mushroom cultivation, the results indicate that the elicitation technique can be applied in the cultivation of medicinal/edible mushrooms.

• Applied Biological Chemistry
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• v.14 no.3
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• pp.207-212
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• 1971

An enzyme preparation from a newly isolated Candida that showed a high lipase activity was subjected to examination of its reaction rate under various conditions. The original and a diluted enzyme solutions showed the zero order curve starting at the point of 50 minutes in time. When PVA was used as an emulsifyer more activity was observed than the case of gum arabic. The optimal temperature and pH were $37{\sim}40^{\circ}C$ and 7.0, respectively. Oleic acid as a fatty acid conferred on the enzyme an inhibitory action while calcium ion a positive one. Sodium cholate yielded an increase in reaction rate at the first stage.

• KSBB Journal
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• v.14 no.4
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• pp.465-469
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• 1999

Horseradish peroxidase(HRP) in organic solvent can be reactivated by evaporation. In order to measure the evaporation effect, the enzyme solutions were obtained by evaporation and dilution of organic solvent, respectively. Although two situations were thermodynamically identical, the activity from evaporation was higher than that from dilution. From the UV absorbance and the fluorescence intensity mesurements, it can be explained that reactivation of enzyme activity might be caused by reversible folding, and the enzyme obtained by evaporation was more refolded than that obtained by dilution.

• Applied Biological Chemistry
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• v.36 no.2
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• pp.86-92
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• 1993

Myrosinase from radish was purified by DEAE Bio-Gel, Con-A, and Superose-6 column. The purified myrosinase(II) possessed 2 subunits, and their molecular as determined by SDS-polyacrylamide gel electrophoresis were 53 and 39 KD, respectively. The specific activity of purified enzyme was 37,500 units/mg. The enzyme was purified approximately 44-fold compared to the crude enzyme. Optimum pH of the myrosinase was $6.5{\sim}7.0$ in phosphate and Tris-HCl buffer solutions. Optimum temperature of the enzyme was $37{\sim}38^{\circ}C$. The enzyme was stable at pH 7.0, and less than $30^{\circ}C$. Cu or Hg ion significantly inhibited the enzyme activity, but ascorbic acid enhanced, resulting in a maximum activity by 1 mM ascorbic acid. Among the ascorbic acid analogues, dehydroascorbic acid did not affect, whereas others showed a little effect, but less than ascorbic acid itself. Individual 2-mercaptoethanol and dithiothreitol (reducing agents) did not enhance the enzyme activity. but 2-mercaptoethanol effect was enhanced when mixed with ascorbic acid.