• Journal of the Korean Wood Science and Technology
• /
• v.27 no.1
• /
• pp.79-87
• /
• 1999

To use the agricultural residues as the raw material of molded packaging material, the packaging trays were manufactured from rice-straw pulp. The physical properties were measured to compare non-treated trays with the addition trays, such as the addition of starch, rosin size, carboxymethyl cellulose(CMC), polyethylene glycol(PEG), alkylketene dimer(AKD), polyacryl amide(PAM). The results were as follows : 1. In the addition of starch, air permeability at addition of 5% was highest. Bursting strength and tensile strength were smaller than non-treated trays. 2. In the addition of rosin size, air permeability, bursting strength and tensile strength were smaller than non-treated trays. 3. In the addition of CMC, air permeability was higher than non-treated trays. Bursting strength and tensile strength were similar to non-treated trays. 4. In the addition of PEG, air permeability was higher than non-treated trays. Bursting strength at addition of 3% was the highest and tensile strength was smaller than non-treated trays. 5. In the addition of AKD, air permeability at addition of 1% and 5% was higher than non-treated trays. Bursting strength and tensile strength were smaller than non-treated trays. 6. In the addition of PAM, air permeability at addition of 0.01% was the highest. Tensile strength at addition of 0.01% were higher than non-treated trays. 7. The water absorption of the trays decreased with increasing adding of natural additives.

• The Journal of Natural Sciences
• /
• v.9 no.1
• /
• pp.19-24
• /
• 1997

Using the PCR(polymerase chain reaction method), gone 1 of phage K11 coding for K11 phage RNA polymerase has been cloned and expressed under the control of lac promoter. K11 phage RNA polymerase was conventionally purified through the DEAE-sephacel and Affigel blue column chromatographies. The 0.2-0.3 M $NH_4Cl$ fractions of DAEA-sephacel column chromatography showed K11 phage RNA polymerase activity and further purification with Affigel blue column chromatography showed nearly single protein band on SDS-polyacryl amide gel. K11 phage RNA polymerase, which is one of the T7 group phage RNA polymerase (E. coil phage T7, T3 and Salmonella tyhimurium phage SP6 RNA polymerase), shares high degrees of homology with the other T7 group phage RNA polymerase. Previously we constructed T7 and SP6 promoter variants and revealed promoter specificity of T7 and SP6 RNA polymerase (Lee and Kang, 1993). To investigate the promoter specificity of K11 RNA polymerase in vitro K11 promoter activity was measured with SP6 promoter variants. The SP6 promoter variant share highest degrees of sequence homology with K11 promoter sequence show strongest promoter activity.

• The Korean Journal of Mycology
• /
• v.30 no.2
• /
• pp.113-118
• /
• 2002

A Carboxymethyl Cellulase (CMCase) has been isolated and purified from the edible mushroom, Stropharia rugosoannulata. The molecular weight of CMCase was estimated to be 54 kDa by SDS polyacryl amide gel electrophoresis. The maximum activity of the purified CMCase was observed at pH 4.0 and $40^{\circ}C$, and stable for pH 3.0 to 11.0 to maintain 40% activity. The CMCase activity was activated by $AgNO_{3},\;MgSO_{4},\;and\;KCl$. However, its activity was inhibited by 1,10-phenanthroline, KCN and L-cysteine. Also, the enzyme activity was decreased by the addition of EDTA, suggesting that the purified CMCase is metalloenzyme.

• The Korean Journal of Mycology
• /
• v.26 no.4 s.87
• /
• pp.583-588
• /
• 1998

A fibrinolytic enzyme has been isolated from the edible honey mushroom, Armillariella mellea and purified. The apparent molecular mass of purified enzyme was estimated to be 19800Da by SDS polyacryl amide gel electrophoresis and 19900Da by gel filtration, indicating that it was a monomer. The enzyme was optimal at pH 7, suggesting that the purified enzyme was a neutral proteinase. It shows the maximum fibrinolytic activity at $55^{\circ}C$, is completely inactivated above $65^{\circ}C$, and still indicates 40% of activity at $37^{\circ}C$. The fibrinolytic activity has been decreased by the addition of EDTA. Fifteen amino acid sequence was determined by protein sequencing techniques.

• Applied Biological Chemistry
• /
• v.27 no.2
• /
• pp.129-134
• /
• 1984

Change of protein component in soybean sprout grown at four temperatures was investigated by polyacrylamide gel electrophoresis. Main bands were identified using purified seed globulins. Electrophoretogram showed 5 main bands (a. b, c, d, and p) and 10 minor bands in seed and maximum number (19) of bands (8 main band including 0 and 11 minor) at 4th day after germination in cotyledon. All bands appeared in axis protein but resolution was poor. In cotyledon, a component (most rapidly) and b+c+d component decreased while o+p component and other minor components were increased at 6th day and decreased thereafter. In axis all components increased rapidly, especially in minor components and b+c+d component. High growing temperature accelerated decrease in cotyledon and increase in axis of protein, especially for 11S. The a component was identified as 7S, b+c+d as 11S and o+p as 2S globulin.

• Journal of Applied Biological Chemistry
• /
• v.54 no.4
• /
• pp.231-237
• /
• 2011

A gene encoding a putative alanine racemase in Xanthomonas. oryzae pv. oryzae was cloned, expressed and characterized. Expression of the cloned gene was performed in Escherichia coli BL21(DE3)pLys using a pET-21(a) vector harbouring $6{\times}histidine$ tag. Purification of the recombinant alanine racemase by affinity chromatography resulted in major one band by sodium dodecyl sulfate polyacryl amide gel electrophoresis analysis, showing about 45 kDa of molecular weight. The alanine racemase gene, cloned in this experiment, appears to be constitutively expressed in X. oryzae, as analyzed by reverse transcriptase polymerase chain reaction. The enzyme was the most active toward L-alanine and secondly D-alanine, showing a racemic reaction, thus the enzyme is considered as an alanine racemase. The enzyme was considerably activated by addition of pyridoxal-5-phosphate (PLP), showing that 75% increase in activity was observed at 0.3 mM, compared with control. D-Cysteine as well as L-cysteine significantly inhibited the enzyme activity. The inhibitions by cysteines were more prominent in the absence of PLP, showing 9 and 5% of control activity at 2 mM of addition, respectively. The enzyme was the most active at pH 8.0 and more stable at alkaline pHs than acidic pH condition.

• Journal of the Korean Society of Food Science and Nutrition
• /
• v.21 no.2
• /
• pp.187-194
• /
• 1992

Rhizopus oryzae CJ-2114 was selected for its strong polygalacturonase activity among various strains of mold found in soil. It was found that the production of polygalacturonase reached to maximum when the wheat bran medium containing 1% albumin, 1% sorbitol and 0.2% (NH$_4$)$_2$C$_2$O$_4$was cultured for 96 hrs at 3$0^{\circ}C$. Polygalacturonase was purified 11.13 fold from Rhizopus oryzae CJ-2114. The purification procedures include ammonium sulfate treatment, gel filtration on Sephadex G-75, G-150 and DEAE-cellulose ion exchange chromatography. Yield of the enzyme purification was 40.3% .Purified enzyme was confirmed as a single band by the polyacrylamide gel electrophoresis. When the purified enzyme was applied to SDS-poly-acrylamide gel electrophoresis, the molecular weight was estimated to be 47,000. The amino acid composition indicated relatively high contents of glutamic acid and glyrine.

• Applied Biological Chemistry
• /
• v.41 no.1
• /
• pp.6-12
• /
• 1998

To extract insoluble proteins and to improve functional properties of abolished proteins, a protease producing Aspergillus sp. MS-18 was isolated from soil. The enzyme was purified and its enzymological characteristics were investigated. It was found that production of protease reached to the maximum when the wheat brae medium containing, 3% arabinose, 0.5% polypepton, 0.1% $(NH_4)_2SO_4$ and 0.2% magnesium chloride was cultured for 3 days. Protease was purified 16.9 folds after ion exchange chromatography and gel filtration and the specific activity was 340.4 unit/mg. Purified enzyme was confirmed as a single band by the polyacrylamide gel electrophoresis. The molecular weight of protease was estimated to be 30,000. Crystalization form of purified protease was a stick shape with rounding edges. The optimum pH and temperature for the protease activity were 9.0 and $60^{\circ}C$, respectively. The enzyme was stable in pH 7.0-12.0 at $50^{\circ}C$. The activity of purified enzyme was inhibited by $Hg^{2+}$, $Cu^{2+}$, $Zn^{2+}$ and $Pb^{2+}$, whereas it was activited by $Na^+$, $Mg^{2+}$ and $Mn^{2+}$. The activity of the protease was inhibited by the treatment with ethylenediaminetetraacetic acid and phenylmethane sulfonyl fluoride. The result suggests that the purified enzyme is a serine protease with metal ion at active site. Km and Vmax of purified protease were $29.33\;{\mu}mole/L$ and $5.13\;{\mu}g/min$, respectively.

• Journal of Bio-Environment Control
• /
• v.14 no.3
• /
• pp.190-195
• /
• 2005

This research was conducted to investigate the changes in soil chemical properties of root media as influenced by incorporation rate of a polyacryl amide hydrogel, Stocksorb C. The pH at 5 weeks after treatment in four root media such as peatmoss + vermiculite (1:1, v/v; PV), peatmoss + composted rice hull (1:1; PR), peatmoss + composted saw dust (1:1; PD) and peatmoss + composted pine bark (1:1; PB) containing STSB were in the range from 7.04 to 7.30, which was too high. Elevated incorporation rate of STSB resulted in increase of EC in soil solution of four root media with linear and quadratic response. The concentrations of $NH_4^+-N,\;NO_3^--N,\;PO_4-P^{3-},\;K^+,\;Ca^{2+}and\;Mg^{2+}$ in four kinds of root media increased as incorporation rates of STSB were elevated. But the $NO_3^-$-N concentrations in PS media were lower than those in other there root media tested. The Fe concentrations in PV, PR and PS media increased as incorporation rates of STSB were elevated, but those in PB medium did not show significant different. The concentrations of $Fe^{2+},\;Mn^{2+},\;Zn^{2+}and\;Cu^{2+}$ in PS media were higher than those in other three root media.

• Microbiology and Biotechnology Letters
• /
• v.26 no.4
• /
• pp.316-322
• /
• 1998

An ${\alpha}$-D-galactosidase (${\alpha}$-D-galactoside galactohydrolase, EC 3. 2. 1. 22) from sunflower seed was purified by affinity chromatography using N-$\varepsilon$-aminocaproyl-${\alpha}$-D-galactopyranosylamine coupled to sepharose and its properties were examined. The specific activity of the purified enzyme, tested with p-nitrophenyl-${\alpha}$-D-galactopyranoside as substrate, was 291.66 units/mg protein, representing an 115-folds purification of the original crude extract. The final preparation obtained from by Sephadex G-25 chromatography showed a single band on SDS-polyacrylamide gel electrophoresis. The molecular weight was determined to be 42,000 by SDS-polyacrylamide gel electrophoresis. The purified galactosidase showed maximum activity at pH 4.5 and 55$^{\circ}C$, and was stable in the pH and temperature ranges of 4.0 to 5.0 and 30 to 55$^{\circ}C$, respectively. The enzyme activity was inhibited by Ag$\^$2+/, Hg$\^$2+/ and Co$\^$2+/. The enzyme activity was not affected considerably by treatment with other metal compounds. The enzyme liberated galactose from melibiose, raffinose, copra galactomannan, guar gum and locust bean gum by TLC, and also the hydrolysis rate of substrate was compared by HPLC.