• 한국정보디스플레이학회:학술대회논문집
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• 2004.08a
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• pp.885-888
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• 2004

We have prepared and investigated the properties of photoinitiator-free photosensitive polyimide gate insulatos for organic thin-film transistors (OTFTs). The precursor was prepared from a dianhydride, 3,3',4,4'-Benzophenone tetracarboxylic dianhydride (BTDA) and novel aromatic diamine, 7-(3,5-diaminobenzoyloxy) coumarine (DA-CM). Photo-patternability of the polyimide precursor film and surface morphology of the films before and after photo-patterning process were investigated and negative pattern with a resolution of 50 ${\mu}m$ was obtained nicely. In addition, we have fabricated OTFTs with pentacene and photosensitive polyimide as a semiconductor and a gate insulator; respectively. According to the device geometry, the ${\mu}$, current modulation ratio and subthreshold swing of the devices were around 0.2${\sim}$0.4 $cm^2$/Vs, more than $10^5$ and around 3${\sim}$5 V/dec, respectively.

• Journal of Microbiology and Biotechnology
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• v.13 no.4
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• pp.487-494
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• 2003

2,3-Dihydroxybiphenyl 1,2-dioxygenase (23DBDO), an enzyme of the biphenyl biodegradation pathway encoded by the bphC gene of Comnmonas sp. SMN4, was expressed and purified using column chromatographies. SDS-PAGE of purified 23DBDO showed a single band with a molecular mass of 32 kDa, which was consistent with the data from the gel filtration chromatography (GFC). The purified enzyme exhibited a maximum 23DBDO activity at pH 9.0 and was stable at pH 8.0. The enzyme showed maximum activity at $40^{\circ}C$ and maintained activity at $30^{\circ}C$ for 24 h. Kinetic parameters represented by Michaelis-Menten constants such as $K_m\;and\;V_{max}$ values for various substrates were determined by Lineweaver-Burk plots: The purified enzyme 23DBDO from Comamonas sp. SMN4 had the highest catalytic activity for 2,3-dihydroxybiphenyl and 3-methylcatechol, and had very poor activity with catechol and 4-methylcatechol.

• Asian-Australasian Journal of Animal Sciences
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• v.19 no.1
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• pp.137-143
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• 2006

The purpose of this study was to prepare a binder containing porcine blood transglutaminase (TGase), thrombin and fibrinogen. Extracted TGase, thrombin and fibrinogen were used alone or mixed with different proportions of their volume (v/v/v) by nine combinations as follows were 0.5:1:15, 0.5:1:20, 0.5:1:25, 1:1:15, 1:1:20, 1:1:25, 1.5:1:15, 1.5:1:20 and 1.5:1:25, respectively. Five ml of each combination were mixed with 0.6 ml of 0.25 M calcium chloride before experiment. After storage at 4C for 0, 1, 2, 3, 4 and 5 weeks, enzyme activity, total plate count, pH value, and SDS-PAGE of TGase, thrombin and fibrinogen were tested and pH value, clotting time and gel strength of the nine combination binders were determined. The results showed that total plate count of thrombin and pH value of TGase were significantly higher (p<0.05) than in other treatments. SDS-PAGE results showed that purified TGase, thrombin and fibrinogen from porcine blood plasma compared with commercial products (Sigma) had the same band patterns and nine different combination binders had no significant effect. Enzymatic activity of TGase and thrombin decreased as storage time increased. Total plate count of TGase, thrombin and fibrinogen and clotting time of the binder increased as storage time increased. The higher amount of fibrinogen in combinations, the stronger the gel strength.

• Journal of Microbiology and Biotechnology
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• v.22 no.3
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• pp.331-338
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• 2012

A novel gene coding for an endo-${\beta}$-1,4-mannanase (manA) from Bacillus subtilis strain G1 was cloned and overexpressed in P. pastoris GS115, and the enzyme was purified and characterized. The manA gene consisted of an open reading frame of 1,092 nucleotides, encoding a 364-aa protein, with a predicted molecular mass of 41 kDa. The ${\beta}$-mannanase showed an identity of 90.2-92.9% ${\leq}95%$) with the corresponding amino acid sequences from B. subtilis strains deposited in GenBank. The purified ${\beta}$-mannanase was a monomeric protein on SDS-PAGE with a specific activity of 2,718 U/mg and identified by MALDI-TOF mass spectrometry. The recombinant ${\beta}$-mannanase had an optimum temperature of $45^{\circ}C$ and optimum pH of 6.5. The enzyme was stable at temperatures up to $50^{\circ}C$ (for 8 h) and in the pH range of 5-9. EDTA and most tested metal ions showed a slightly to an obviously inhibitory effect on enzyme activity, whereas metal ions ($Hg^{2+}$, $Pb^{2+}$, and $Co^{2+}$) substantially inhibited the recombinant ${\beta}$-mannanase. The chemical additives including detergents (Triton X-100, Tween 20, and SDS) and organic solvents (methanol, ethanol, n-butanol, and acetone) decreased the enzyme activity, and especially no enzyme activity was observed by addition of SDS at the concentrations of 0.25-1.0% (w/v) or n-butanol at the concentrations of 20-30% (v/v). These results suggested that the ${\beta}$-mannanase expressed in P. pastoris could potentially be used as an additive in the feed for monogastric animals.

• Microbiology and Biotechnology Letters
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• v.47 no.2
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• pp.259-268
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• 2019

In this study, the extracellular metalloprotease from Serratia marcescens PPB-26 was purified to homogeneity via ethanol fractionation and DEAE-cellulose column chromatography. Thus, a 3.8-fold purification was achieved with a 20% yield and specific activity of 76.2 U/mg. The purified protease was a 50-kDa monomer whose optimum pH and temperature for activity were 7.5 and $30^{\circ}C$ respectively; however, it was found to remain active in the 5-9 pH range and up to $40^{\circ}C$ for 6 h. The protease had a half-life of 15 days at $4^{\circ}C$, an optimum reaction time of 10 min, and an optimum substrate (casein) concentration of 0.25%. Furthermore, the Michaelis constant ($K_m$) and reaction velocity ($V_{max}$) of the protease were calculated to be 0.28% and $111.11{\mu}moles/(min{\cdot}mg)^{-1}$, respectively. The protease was stable when subjected to metal ions (2 mM), showing increased activity with most (especially $CoCl_2$ and $MgSO_4$ (30.54% increase)). It was also stable when exposed to oxidizing agents, bleaching agents, and detergents (5% v/v for 60 min). It retained 93% of its activity in non-ionic detergents (Tween-20, Tween-80, and Triton X-100). Moreover, wash performance analysis in commercial detergents (Ariel and Tide) showed that not only was the protease capable of protein stain removal, but also reduced cleaning time by 80% when added to detergents. Thus, the Serratia marcescens PPB-26 metalloprotease appears to be a promising new candidate as a laundry additive in the detergent industry.

• Journal of Microbiology and Biotechnology
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• v.27 no.7
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• pp.1216-1222
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• 2017

To develop starters for the production of functional foods or materials, lactic acid bacteria producing ${\gamma}-aminobutyric$ acid (GABA) were screened from jeotgals, Korean fermented seafoods. One isolate producing a high amount of GABA from monosodium $\text\tiny{L}$-glutamate (MSG) was identified as Enterococcus avium by 16S rRNA gene sequencing. E. avium M5 produced $18.47{\pm}1.26mg/ml$ GABA when incubated for 48 h at $37^{\circ}C$ in MRS broth with MSG (3% (w/v)). A gadB gene encoding glutamate decarboxylase (GAD) was cloned and overexpressed in E. coli BL21 (DE3) using the pET26b (+) expression vector. Recombinant GAD was purified through a Ni-NTA column and the size was estimated to be 53 kDa by SDS-PAGE. Maximum GAD activity was observed at pH 4.5 and $55^{\circ}C$and the activity was dependent on pyridoxal 5'-phosphate. The $K_m$ and $V_{max}$ values of GAD were $3.26{\pm}0.21mM$ and $0.0120{\pm}0.0001mM/min$, respectively, when MSG was used as a substrate. Enterococcus avium M5 secretes a lot of GABA when grown on MRS with MSG, and the strain is useful for the production of fermented foods containing a high amount of GABA.

• Journal of Microbiology and Biotechnology
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• v.32 no.4
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• pp.437-446
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• 2022

In this study, to obtain icaritin with high pharmacological activities from icariin, which has a content ratio of over 58% in the total flavonoids of Epimedium herb, a special Epimedium flavonoid-glycosidase was produced, purified and characterized from Aspergillus sp.y848 strain. The optimal enzyme production was gained in a medium containing 5% (w/v) wheat bran extract and 0.7% (w/v) Epimedium leaf powder as the enzyme inducer, and strain culture at 30℃ for 6-7 days. The molecular weight of the enzyme was approximately 73.2 kDa; the optimal pH and temperature were 5.0 and 40℃. The enzyme Km and Vmax values for icariin were 15.63 mM and 55.56 mM/h. Moreover, the enzyme hydrolyzed the 7-O-glucosides of icariin into icariside II, and finally hydrolyzed 3-Orhamnoside of icariside II into icaritin. The enzyme also hydrolyzed 7-O-glucosides of epimedin B to sagittatoside B, and then further hydrolyzed terminal 3-O-xyloside of sagittatoside B to icarisiede II, before finally hydrolyzing 3-O-rhamnoside of icarisiede II into icaritin. The enzyme only hydrolyzed 7-O-glucoside of epimedin A or epimedin C into sagittatoside A or sagittatoside C. It is possible to prepare icaritin from the high-content icariin in Epimedium herb using this enzyme. When 2.5% icariin was reacted at 40℃ for 18-20 h by the low-cost crude enzyme, 5.04 g icaritin with 98% purity was obtained from 10 g icariin. Also, the icaritin molar yield was 92.5%. Our results showed icaritin was successfully produced via cost-effective and relatively simple methods from icariin by crude enzyme. Our results should be very useful for the development of medicines from Epimedium herb.

• Microbiology and Biotechnology Letters
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• v.41 no.1
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• pp.33-43
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• 2013

A bacterium producing a fibrinolytic enzyme was isolated from Cheonggukjang. The bacterium was identified as a strain of Bacillus amyloliquefaciens by 16S rDNA analysis and designated as B. amyloliquefaciens HC188. The optimum culture medium appeared to be one containing 0.5% (w/v) maltose and 0.5% (w/v) soytone. Bacterial growth in the optimal medium at $37^{\circ}C$ reached the stationary phase after 27 h of incubation and the fibrinolytic enzyme showed optimum activity at 24 h. The enzyme was purified by 20-80% ammonium sulfate precipitation, CM Sepharose fast flow ion exchange chromatography, and Sephacryl S-200HR column chromatography. Its specific activity was 38359.3 units/mg protein and the yield was 5.5% of the total activity of the crude extracts. The molecular weight was 24.7 kDa and the amino acids of the N-terminal sequence were AQSVPYGVSQIKAPA. The fibrinolytic enzyme activity had an optimum temperature of $40^{\circ}C$ and an optimum pH of 8.0, and the enzyme was stable in the ranges $20-40^{\circ}C$ and pH 6.0-8.0. Enzyme activity was increased by $Ca^{2+}$ and $Co^{2+}$ but inhibited by $Cu^{2+}$, EDTA, and PMSF. It is suggested that the purified enzyme is a metallo-serine protease.

• Korean Journal of Microbiology
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• v.40 no.4
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• pp.320-327
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• 2004

Three hundreds thirty two bacterial colonies which were able to degrade crude oil were isolated from soil sam­ples that were contaminated with oil in Daejeon area. Among them, one bacterial strain was selected for this study based on its higher oil degrading ability, and this selected bacterial strain was identified as Acinetobactor sp. B2 through physiological-biochemical tests and analysis of its 16S rRNA sequence. Acinetobactor sp. B2 was able to utilize various carbohydrates but did not utilize trehalose and mannitol as a sole carbon source. Acinetobactor sp. B2 showed a weak resistance to antibiotics such as kanamycin, streptomycin, tetracycline and spectinomycin, but showed a high resistance up to mg/ml unit to heavy metals such as Ba, Li, Mn, AI, Cr and Pb. The optimal growth temperature of Acinetobactor sp. B2 was $30^{\circ}C.$ The lipase produced by Acinetobactor sp. B2 was purified by ammonium sulfate precipitation, DEAE-Toyopearl 650M ion exchange chromatography and Sephadex gel filtration chromatography. Its molecular mass was about 60 kDa and condition for the optimal activity was observed at $40^{\circ}C$ and pH 10, respectively. The activation energy of lipase for the hydrolysis of p­nitrophenyl palmitate was 2.7 kcal/mol in the temperature range of 4 to $37^{\circ}C,$ and the enzyme was unstable at the temperature higher than $60^{\circ}C.$ The Michaelis constant $(K_m)\;and\;V_{max}$ for p-nitrophenyl palmitate were 21.8 uM and $270.3\;{\mu}M\;min^{-1}mg^{-1},$ respectively. This enzyme was strongly inhibited by 10 mM $Cd^{2+},\;Co^{2+},\;Fe^{2+},\;Hg^{2+},$ EDTA and 2-Mercaptoethalol.

• Resources Recycling
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• v.30 no.3
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• pp.30-40
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• 2021

The present study investigates the bioleaching efficiencies of arsenic via contact and non-contact mechanisms. The attachment of Acidithiobacillus ferrooxidans was restricted by a partition system comprising a semi-permeable membrane with a molecular weight cutoff of 12-14 kDa. The results were compared for two arsenic concentrations in the system (1.0% and 0.5% w/v) to maintain a homogeneous system. The overall bacterial performance was monitored by comparing total arsenic and iron concentrations, Fe ion speciation, pH, and solution redox potentials in flask bioleaching experiments over a period of 10 d. Our results indicated that bacterial attachment could increase arsenic extraction efficiency from 20.0% to 44.9% at 1.0 % solid concentrations. These findings suggest that the bacterial contact mechanism greatly influences arsenic bioleaching from mine tailings. Therefore, systems involving two-step or non-contact bioleaching are less effective than those involving one-step or contact bioleaching for the efficient extraction of arsenic from mine tailings.