• Journal of the Korea Fashion and Costume Design Association
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• v.9 no.3
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• pp.47-57
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• 2007

This study focused on the properties natural dyeing and natural material and on the development of functional material for well-being in apparel industry. Comus officinalis Siebold et Zuccarini is used as natural dyeing material which had been reported that have curable effect for unbalanced immunity, geriatric diseases like urinary tract system, diabetes, hypertension, arthritis, tinnitus, hyperhidrosis and women's diseases like hypermenorrhea. And this material also has anti-cancer effect so that can restraint cancer cells. 3 kinds tester of cotton, wool and silk are dyed by boiled with each dye (flower, fruits, bark of tree) as first dyeing and dried in the shade. These testers are done by post-mordanting method. Aluminium Potassium(Alk(SO4)2), Cuprie Sulfate($CuSO4{\cdot}5H2O$), Stannous Chloride($SnCl2{\cdot}2H2O$), Ferrous Sulfate($FeCl2{\cdot}4H2O$), Titanium Sulfate 24% aqueous solution(Ti(SO4)2) are used as mordants. Dyeing results of Comus officinalis Siebold et Zuccarini flower and bark are shown as yellow color series. And dyeing result of fruits is pink color series. Silk shows the best dyeing property. As the point of view for dyeing property, Ti, Sn, Fe would be the properchoice for mordant. Following results are extracted in this study. Yellow color is resulted in dyeing with Cornus officinalis flower as non-mordanting condition. Yellowish red color is come from dyeing with Comus officinalis fruit as non-mordanting condition. Grayish yellow tone is resulted in dyeing with bark as non-mordanting condition. Orange tone color with Ti-mordanting, green tone color with Sn-mordanting and gray tone color with Fe-mordanting is resulted respectively. However light-fastness of Comus officinalis(flower, fruit, bark) is very low as 1 or 2 level in non-mordanting condition, Comus officinalis flower dyeing is turned out 3 or 4 level and fruit dyeing is 4 or 5 level, bark dyeing is 2 or 3 level with Ti-mordanting respectively. Eventually Comus officinalis fruit has the best light-colorfastness property among all of dyes. dry cleaning colorfastness of Cornus officinalis(flower, fruit, bark) is good as 4 or 5 level in Ti-mordanting condition, perspiration-colorfastness of Cornus officinalis(flower, fruit, bark) is good as 4 or 5 level in Ti-mordanting condition, With these results, this study could conclude that dye-ability, colorfastness problem is getting better after mordanting process and practical usage would be possible.

• KSBB Journal
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• v.19 no.1
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• pp.50-56
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• 2004

The aim of this work was to investigate the purification and characterization dixoygenases isolated from Delftia sp. JK-2, which could utilize aniline, benzoate, and p-hydroxybenoate as sole carbon and energy source. Catechol 1,2-dioxygenase (C1, 2O), catechol 2,3-dioxygenase(C2, 3O), and protocatechuate 4,5-dioxygenase(4,5-PCD) were isolated by benzoate, aniline, and p-hydroxybenzoate. In initial experiments, several characteristics of C1 ,2O, C2, 3O, and 4,5-PCD separated with ammonium sulfate precipitation, DEAE-sepharose, and Q-sepharose were investigated. Specific activity of C1 ,2O, C2, 3O, and 4,5-PCD were approximately 3.3 unit/mg, 4.7 unit/mg, and 2.0 unit/mg. C1 ,2O and C2, 3O demonstrated their enzyme activities to other substrates, catechol and 4-methylcatechol. 4,5-PCD showed the specific activity to the only substrate, protocatechuate, but the substrates(e.g., catechol, 3-methylcatechol, 4-methylcatechol, 4-chlorocatechol, 4-nitrocatechol) did not show any specific activities in this work. The optimum temperature of C1, 2O, C2, 3O, and 4,5-PCD were 30$^{\circ}C$, and the optimal pHs were approximately 8, 8, and 7, respectively. Ag$\^$+/, Hg$\^$+/, Cu$\^$2+/ showed inhibitory effect on the activity of C1, 2O and C2, 3O, but Ag$\^$+/, Hg$\^$+/, Cu$\^$2+/, Fe$\^$3+/ showed inhibitory effect on the activity of 4,5-PCD. Molecular weight of the C1, 2O, C2, 3O, and 4,5-PCD were determined to approximately 60 kDa,35 kDa, and 62 kDa by SDS-PAGE.

• Journal of Microbiology
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• v.33 no.2
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• pp.115-119
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• 1995

The alkaline protease of Xanthomonas sp. YL-37 has been purified, and the properties of the enzyme investigated. The alkaline protease of Xanthomonas sp. YL-37 was purified form crude enzyme by ammonium sulfate fractionation, CM-cellulose ion exchange chromatography, and Sephadex G-100 gel filtration. Through the series of chromatographies, the enzyme was purified to homogenecity with specific activity of 4.23 fold higher than that of the crude broth. The molecular weight of the purified protease has been estimated to be 62 KDa on SDS-polyacrylamide gel electrophoresis. The optimal pH and temperature for alkaline protease activity were 11.0 and 50.deg.C, respectively. The enzyme was stable between pH 5.0 and 10.0 and up to 50.deg.C. Enzyme activity was lost up to 50% on heating at 70.deg.C for 30 minutes. The activity of alkaline protease was inhibited by Cu$\^$2+/, Zn$\^$2+/, Hg$\^$2+/, PMSF, and activated by Mn$\^$2+/ and Ca$\^$2+/. The $K_{m}$ value for casein as a substrate was 4.0 mg/ml.

• BMB Reports
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• v.28 no.2
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• pp.170-176
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• 1995

Rhodanese from mouse liver was purified to near homogeneity by ammonium sulfate precipitation, CM-Sephadex ion exchange, hydroxyapatite and Sephacryl S-200-HR gel filtration chromatographies with a purification of 776 folds. The molecular weight was determined by Sephadex G-150 gel filtration and found to be 34.8 KDa. SOS-PAGE showed molecular weight 34 KDa and two identical subunits splitting by aging for 3 weeks at $-70^{\circ}C$ the molecular weight of which was 17 KDa. The optimal pH of enzyme activity was 9.4 and the pI value of the enzyme was 6.6. Rhodanese showed the optimal reaction temperature of $25^{\circ}C$ and near linear increasing pattern until 10 min. incubation. $K_m$ values of rhodanese for KCN and $Na_{2}S_{2}O_{3}$ as substrates were 12.5 mM and 8.3 mM, respectively. Rhodanese activity was inhibited by more than 70% at a concentration of 100 ${\mu}M$ of $Ni^{2+}$, $Zn^{2+}$, $Cd^{2+}$, $Hg^{2+}$ and $Cu^{2+}$. Other metal ions, such as $Mn^{2+}$, $Mg^{2-}$, $Ca^{2+}$, and $Fe^{2+}$ showed no effect on rhodanese activity.

• BMB Reports
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• v.30 no.2
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• pp.150-156
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• 1997

Tyrosinase was purified from Solanum melongena by ammonium sulfate precipitation, Sephadex G-150 and DEAE-Sephacel column chromatography. The molecular weight of the purified tyrosinase was approximately 88,600 daltons with 805 amino acid residues. The amino acid composition showed the characteristic high contents of glycine, glutamic acid and serine residues. The enzyme had high substrate specificity towards (+)-catechin. The $K_m$, value for L-DOPA was 20.8 mM. L-ascorbic acid, ${\beta}-mercapto-ethanol$, sodium diethyldithiocabamate, KCN and $NaN_3$ had strong inhibitory effects on enzyme activity. Sodium diethyldithiocabamate was a competitive inhibitor of the enzyme with a $K_i$ value of $5.2{\times}10^{-2}\;mM$. The optimum pH of the enzyme was 9.0 and the optimum temperature was $65^{\circ}C$ with L-DOPA as a substrate. In addition, the activity was enhanced by addition of $Ca^{+2}$ or $Cu^{+2}$, but decreased in the presence of $Fe^{2+},Fe^{3+}$ and $Zn^{2+}$ ions.

• The Journal of Internal Korean Medicine
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• v.11 no.1
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• pp.15-27
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• 1990

For the purpose of examing on the efficancy of the Boolwhangumjeonggisan and on the effect of the Boolwhangumjeonggisan, dropsy animals given water boil ding abstraction exgis power. What made an experiment, the motility of isolate ileume, anticathartic action, the action of gastric juice, tied pylous ulcer and inhibited vomitting. 1. Boolwhangumjeonggisan displayed great suppresion effect in regard to automatic movement of the motility of isolated of mice and displayed anti-acethylcholine action, antibarium chloride action. Thus, the origin of muscle relaxation for internal smooth muscle is admitted. 2. It displayed great rexation effect in regard to fraction of rat's stomach and displayed contentional effect in regard to a cetylcholine and barium chloride. 3. It decreased rat of barium sulfate transport through the small intestine of mice. 4. It recognized anti-cathartic action, rat suffered from leading diarrhea by caster oil. 5. Total activity, pepsin secretion decreased and increased the pH of stomach in Shay's method. 6. It recognized powerful prevention effect on tied pylous ulcer. 7. It inhibited vomitting by administration of CuSo4 in frog.

• Journal of Microbiology and Biotechnology
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• v.11 no.2
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• pp.242-250
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• 2001

A Gram-positive bacterium (strain JB-13) that was isolated from soil as a producer of cyclodextrin glucanotransferase (CGTase) [EC 2.4.1.19] was identified as Panibacillus sp. JB-13. This CGTase could catalyze the transglucosylation reaction from soluble starch to L-ascorbic acid (AA). A main product formed by this enzyme with ${\alpha}-glucosidase$ was identified as $2-O-{\alpha}-D-glucopyranosyl{\;}_{L}-ascorbic$ acid (AA-2G) by the HPLC profile and the elemental analysis. CGTase was purified to homogeneity using ammonium sulfate fractionation, ion-exchange chromatography on DEAE-Seohadex A-50, and gel chromatography on Sephacryl S-200HR. The molecular weight was determined to be 66,000 by both gel chromatography and SDS-PAGE. The isoelectric point of the purified enzyme was 5.3. The optimum pH and temperature was PH 7.0 and $45^{\circ}C$ respectively. The enzyme was stable in the range of pH 6-9 and at temperatures of $75{\circ}C$ or less in the presence of 15 mM ${CaCl_2}.\;{Hg^2+},\;{Mn^+2},{Ag^+},\;and\;{Cu^2+}$ all strongly inhibited the enzyme's activity.

• Microbiology and Biotechnology Letters
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• v.23 no.5
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• pp.573-579
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• 1995

A Bacillus strain capable of producing an extracellular malto-oligosaccharides forming $\alpha $-amylase was isolated from soil and designated as Bacillus sp. SUH4-2. The enzyme was purified by ammonium sulfate fractionation, DEAE-Toyopearl and Mono-Q HR 5/5 column chromatographies using a FPLC system. The specific activity of the enzyme was increased by 16.1-fold and the yield was 13.5%. The optimum temperature for the activity of $\alpha $-amylase was 60-65$\circ$C and more than 50% of initial activity was retained after the enzyme was incubated at 60$\circ$C for 40 min. The enzyme was stable over a broad pH range of 5.0-8.0 and the optimum pH was 5.0-6.0. The molecular weight of the enzyme was determined to be about 63.6 kD and isoelectric point was around 5.8. The enzyme activity was strongly inhibited by Mn$^{2+}$, Ni$^{2+}$, and Cu$^{2+}$ ; slightly by Ca$^{2+}$. The purified enzyme produced starch hydrolyzates containing mainly maltose and maltotriose from soluble starch. The starch hydrolyzates were composed of 11% glucose, 59% maltose, 25% maltotriose and 5% maltotetraose.

• Food Science and Preservation
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• v.7 no.2
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• pp.201-206
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• 2000

${\beta}$-Galactosidase was extracted and purified from strawberry. The purified ${\beta}$-Galactosidase from strawberry was investigated their physicochemical characteristics. ${\beta}$-Galactosidase was purified 25.74 fold from strawberry. The purification procedure include ammonium sulfate fraction, acetone powder treatment and gel and ion exchange chromatography. Yield of the enzyme purification was 18.11%. The purified enzyme has native molecular weight of 116,000 dalton. Vmax value and Km value of ${\beta}$-Galactosidase were 0.077 mM ONPG/ml/15mim and 1.75x10-2mM, respectively. The optimum temperature and pH of ${\beta}$-Galactosidase were 43$^{\circ}$C and pH 4.0, respectively. The ${\beta}$-Galactosidase activity was stable below 50$^{\circ}$C and at pH 4.0 to pH 6.0. Among the metal ions Ca and Mg were did not affect, whereas K, Cu and Zn show a little effect on the enzyme activity. The ${\beta}$-Galactosidase activities were inhibited by treatment with EDTA and SDS.

• The Research Journal of the Costume Culture
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• v.16 no.1
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• pp.158-165
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• 2008

The purpose of this study was to investigate the dyeing property and ultraviolet-cut ability on silk 100% and nylon 100% fabrics dyed with Rhus verniciflua extracts. This study was investigated K/S values, surface color, washing fastness, dry cleaning fastness and ultraviolet-cut ability of the silk and nylon fabrics dyed with Rhus verniciflua extracts under the various dyeing conditions. As mordanting were used Tin(II) Chloride dihydrate $(SnCl_2{\cdot}2H_2O)$, Copper(II) sulfate pentahydrate$(CuSO_5{\cdot}5H_2O)$, Iron(II)Chloride$(FeC_2{\cdot}4H_2O)$. pH was adjusted by sodium carbonate$(Na_2CO_3)$ and formic acid(HCOOH). The optimum dyeing temperature, dyeing time, and pH of the silk fabrics dyed with Rhus verniciflua extracts were $90^{\circ}C$, 100min, and in the nylon fabrics were $90^{\circ}C$, 45min. It were colored(munsell value) 6.4Y 7.5/4.1 in the silk fabrics and colored 4.3Y 6.6/5.9 in the nylon fabrics dyed with Rhus verniciflua extracts. Washing fastness and dry-cleaning fastness in the silk and nylon fabrics dyed with mordanting agent improved in $4{\sim}5$ grade. UV-A test showed that nylon fabrics a high rate of 92% with Rhus verniciflua extracts.