• Korean Journal of Fisheries and Aquatic Sciences
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• v.30 no.3
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• pp.423-427
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• 1997

The effect of different treatments on the quality and yield of purified agar produced from Gelidium amansii has been studied, and the extraction condition ol agar produced from G. amansii has been examined. The contents of ash, sulfate in agar produced from g. amansii collected from different places were $2.63\~2.92\%\;and\;1.38\~1.78\%$, respectively. Yields and gel strength of agar produced from G. amansii collected from different places were $31.6\~46.8\%\;and\;496\~887g/cm^2$, respectively. It was effective to extract agar at $120^{\circ}C\;for\;2\~3hrs$. Agar was purified by D.W. washing, EDTA washing, chitosan treatment, CPC treatment, PEG treatment, ethanol precipitation, acetone precipitation and propanol precipitation. The mineral contents of agar produced from Gelidium amansii were Na (2934ppm), Ca (2472ppm), Mg (2259ppm), K (2527ppm), P1(81.1ppm), Fe (66.4ppm), Al (71.7ppm), Zn (29.7ppm) and Pb (ND: not detected), respectively.

• Journal of Energy Engineering
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• v.20 no.1
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• pp.13-20
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• 2011

The high fuel flexibility of Micro Gas Turbine(MGT) has boosted their use in a wide variety of applications. Recently, the demand for biogas generated from the digestion of organic wastes and landfill as a fuel for gas turbines has increased. We researched the influence of firing landfill gas(LFG) on the performance and operating characteristics of a micro gas turbine combined heat and power system. $CH_4$ and $CO_2$ simultaneous recovery process has been developed for field plant scale to provide an isothermal, low operating cost method for carrying out the contaminants removal in Land Fill Gas(LFG) by liquid phase catalyst for introduce into the green house for the purpose of $CO_2$ rich cultivation of the plants. Methane purification and carbon dioxide stripping by muti panel autocirculation bubble lift column reactor utilizing Fe-EDTA was conducted for evaluate optimum conditions for land fill gas. Based on inflow rate of LFG as 0.207 $m^3$/min, 5.5 kg/$cm^2$, we designed reactor system for 70% $CH_4$ and 27% $CO_2$ gas introduce into MGT system with $H_2S$ 99% removal efficiency. A green house designed for four different carbon dioxide concentration from ambient air to 1500 ppm by utilizing the exhaust gas and hot water from MGT system.

• Korean Journal of Plant Resources
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• v.21 no.1
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• pp.52-59
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• 2008

This study was conducted to evaluate the antioxidative potentials of 4 Aster species. Flowers and aerial parts were extracted with 80% ethanol, and antioxidative activities and bioactive substance contents were investigated. Flowers showed higher extraction yield than aerial parts of all 4 species used. Among the samples tested, Flowers of A. scaber were found to be the most effective in both DPPH and ABTS radical scavenging assay. However, $Fe^{2+}$ chelate effect of all samples were lower than EDTA. Four samples(A. scaber flowers, A. sphathulifolius aerial parts, A. koraiensis flowers, A. scaber aerial parts) out of eight showed stronger inhibitory activities against linoleic acid oxidation than BHT at 8 days. Total polyphenol and flavonoid contents of A. scaber flowers(90.46 and $75.36mg{\cdot}g^{-1}$) were the highest, and followed by A. sphathulifolius flowers.

• Microbiology and Biotechnology Letters
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• v.26 no.6
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• pp.515-522
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• 1998

Plant root rotting fungi, Fusarium solani are suppressed their growth by the chitinase which is produced from the antagonistic soil bacteria. The chitinase producable antagonistic bacterium Pseudomonas sp. 3098 was selected as a powerful biocontrol agent of F. solani from ginseng rhizosphere. The antagonistic Pseudomonas sp. 3098 was able to produce a large amount of extracellular chitinase which is key enzyme in the decomposition of fusarial hypal walls. The chitinase was purified from cultural filtrate of Pseudomonas sp. 3098 by the procedure of ammonium sulfate precipitation, anion exchange chromatography, gel filtration on Bio-Gel P-100, and 1st and 2nd hydroxyapatite chromatography. The molecular mass of the purified enzyme was ca. 45 kDa on SDS-FAGE. The optimal pH and temperature for the activity of purified chitinase were 5.0 and 45$^{\circ}C$, respectively. The enzyme was stable in pH range of 5.0 to 9.0 up to 5$0^{\circ}C$ The enzyme was significantly inhibited by metal compounds such as FeCl$_2$, AgNO$_3$ and HgCl$_2$, and was slightly inhibited by p-CMB, iodoacetic acid, urea, 2,4-DNP and EDTA. The enzyme had ability of digestion on colloidal chitin and chitin from shrimp shell, but could not digest chitosan and chitin from crab shell. Km value of the enzyme was 0.11% on colloidal chitin, and the maximum hydrolysis rate of the enzyme was 34% on colloidal chitin.

• Journal of Life Science
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• v.16 no.2 s.75
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• pp.245-252
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• 2006

A bacterial strain, identified as Staphylococcus aureus JJ-11, producing collagenase was isolated out of 40 persons having skin troubles. S. aureus JJ-11 produced collagenase optimally in the media containing 1.5%(w/v) gelatin, 1%(w/v) yeast extract, 0.4%(w/v) $K_2HPO_4$, 0.005%(w/v) $NiSO_4{\cdot}6H_2O$ at $37^{\circ}C$ for 18 hrs. The collagenase produced by Staphylococcus aureus JJ-11 was purified at 6.66-folds purity through application of chromatography with Amberlite IRA-900 and Sephacryl S-300 HR columns. The molecular weight of the partially purified enzyme was estimated to be 62 kDa by SDS-PAGE. The protein exhibited optimum enzymatic activity at pH 7.0, and showed a stable activity at pH 4-8. The optimum temperature for collagenase was at $37^{\circ}C$, and activity was maintained upto $40^{\circ}C$. The enzyme activity was slightly elevated in the presence of divalents such as, $Fe^{2+},\;Co^{2+}\;and\;Ba^{2+}$ However, the activity was inhibited in the presence of $Sr^{2+}\;or\;Hg^{2+}$. The inhibition of activity by O-phenanthroline and EDTA suggested that the enzyme may contain metal which is required for activity. The enzyme showed the highest activity when insoluble collagen (type I) was, used as a substrate.

• Applied Chemistry for Engineering
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• v.24 no.2
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• pp.177-183
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• 2013

In this study, the antioxidative activities and component analysis of Broussonetia kazinoki SIEB (B. kazinoki). extracts were investigated. B. kazinoki extract showed the effective free radical (1,1-diphenyl-2-picrylhydrazyl, DPPH) scavenging activity ($FSC_{50}=8.53{\mu}g/mL$). Reactive oxygen species (ROS) scavenging activity ($OSC_{50}$) of the ethyl acetate fraction of B. kazinoki. extracts in the luminol-dependent $Fe^{3+}-EDTA/H_2O_2$ system was $1.69{\mu}g/mL$. The ethyl acetate fraction of B. kazinoki. extracts also exhibited more prominent cellular protective effects (${\tau}_{50}$, 183.3 min at $10{\mu}g/mL$) than that of typical antioxidant $\alpha$-tocopherol (${\tau}_{50}$ = 38.00 min) in the $^1O_2$-induced photohemolysis of human erythrocytes. Components of the ethyl acetate fraction obtained from B. kazinoki extracts were analyzed by TLC, HPLC chromatogram, LC/ESI-MS/MS and $^1H$-NMR. Consequently, Components, components were identified as the kazinol J of kazinol series and luteolin (2-(3,4-dihydroxyphenyl)-5,7-dihydroxy-4-chromenone) of flavonoid series having antioxidant activities. These results indicate that extract/ fraction of B. kazinoki can be used as antioxidants in biological systems, particularly skins exposed to UV radiation by quenching and/or scavenging $^1O_2$ and other ROS, and protecting cellular membranes against ROS. Thus, the extract/fraction of B. kazinoki could be applicable to new cosmeceuticals.

• Korean Journal of Microbiology
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• v.35 no.4
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• pp.315-321
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• 1999

This study has been performed to deveope a yeast strain having high ${\alpha}$-amylase production ability using nuclear transfer method. Hybrids formed between the strains of Saccharomyces fiburigera KCTC 7393 and Saccharomyces cerevisiae KCTC 7049 (tyr-, ura-)were obtained by nuclear transfer technique. Nuclei isolated from the wild type S. fiburigera strain were transfered into auxotrophic mutants S. cerevisiae and selected the hybrids showing an increased starch degrading capability were selected (MN-16). This transformant grew best and produced maximal ${\alpha}$-amylase activity on the medium containing 2% (V/V) soluble starch. ${\alpha}$-Amylase from MN-16 was purified electrophoretically homogenety and its properties were investigated. The enzyme was purified about 10.6 fold with an overall yield 9.7% from the culture medium by ammonium sulfate fractionation. DEAE-Sephacel column chromatography, and Sephacryl S-200 column chromatography. The purified enzyme showed a single band on SDS-polyacrylamide gel electrophoresis. The molecular weight of the ${\alpha}$-amylase was estimated to be 53,000 daltons by SDS-PAGE and by gel permeation chromatography on Sephacryl S-200. The purified enzyme showed the maximum activity at pH 5.5 and 40${\circ}C$. The km value for soluble starch was 2.5㎎/㎖. The enzyme activity increased in the presence of $Ca^{2+}, Co^{2+}, EDTA, Mg^{2+}, Mn^{2+}, Zn^{2+}$, but inhibited by $Cu^{2+}, Fe^{2+}$, and $Ni^{2+}$

• Korean Journal of Microbiology
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• v.47 no.1
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• pp.81-86
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• 2011

Xylanase is a class of enzymes that hydrolyze the linear polysaccharide ${\beta}$-1,4-xylan into xylose. This enzyme is applied in the process of paper making and may be used for the process of biofuel production in the future. The Paenibacillus donghaensis JH8, isolated from Donghae deepsea sediment and reported as a novel bacterium, was known to degrade xylan and its xylanase was characterized in this study. The enzyme was maximally induced in the presence of 0.1% xylan. The production of xylanase was started at early logarithmic phase and reached about 55 miliunit at stationary phase of growth. The optimal temperature and pH of extracellular xylanase were found to be $40^{\circ}C$ and pH 6.0, respectively. The activity of xylanase was inhibited by the presence of $Ca^{2+}$, $Mn^{2+}$, $Fe^{2+}$, $Cu^{2+}$, $Al^{3+}$ or EDTA, and activated by $K^+$, $Ag^+$ or DTT. This xylanase was stable at $40^{\circ}C$ for 120 min, but lost almost their activity in 30 min at $60^{\circ}C$. Zymography analysis of concentrated culture supernatant revealed one major band at 42 kDa and two faint bands at 68 and 120 kDa.

• Korean Journal of Microbiology
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• v.49 no.1
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• pp.78-82
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• 2013

A novel Chryseobacterium sp. JK1 strain isolated from soil had been reported that this isolate produced large amount of extracellular protease at mesophilic temperature in previous study. The optimal temperature and pH of extracellular protease were $40^{\circ}C$ and 7.0, respectively, showing narrow range of optimal temperature and relatively broad activity from pH 6.0 to 9.0. In addition, the protease showed greatest activity against skim milk and lowest against bovine serum albumin (BSA). The protease strongly inhibited by ethylenediaminetetraacetic acid (EDTA), ethylene glycol tetraacetic acid (EGTA) or phenylmethylsulfonyl fluoride (PMSF), and addition of cation $Ag^+$ or $Cu^{2+}$, and slightly inhibited by $Al^{3+}$. No significant inhibition was found with pepstatin, and addition of cation, $K^+$, $Ca^{2+}$, $Na^+$, $Fe^{2+}$ or $Mg^{2+}$. On the contrary, protease was enhanced by addition of divalent cation $Mn^{2+}$ (5 mM). Zymography analysis of concentrated culture supernatant revealed two major bands at 67 and 145 kDa. These results suggest that Chryseobacterium sp. JK1 strain produced extracellular neutral serine proteases which could apply in food industry.

• Microbiology and Biotechnology Letters
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• v.32 no.3
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• pp.230-237
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• 2004

In this study nitroreductase from Pseudomonas sp. HK-6 capable of degrading 2,4,6-trinitrotoluene (TNT) was characterized. Through a series of purification process including ammonium sulfate precipitation, DEAE-sepharose, and Q-sepharose, three different fractions I, II, and III having the enzyme activity of NTRs whose molecular weights were approximately 27 kDa were detected in fractions from HK-6 cells. Specific activity of the three fractions were approximately 4.85 unit/mg, 5.47 unit/mg, and 5.01 unit/mg, and concentrated to 9.0-, 10.1-, and 9.3-fold compared to crude extract, respectively. The optimal pH and temperature for the three NTR fractions were approximately 7.5 and $30^{\circ}C$, respectively. Metal ions, $Ag^{＋}$ , $Cu^{ 2+}$, $Hg^{2＋}$ inhibited approximately 70% of enzymes activities of all NTR, while $Fe^{2＋}$ did not stimulate or inhibit the activities. Monitoring the effect of chemicals on the enzyme activity revealed that those NTR fractions lost enzyme activity in presence of $\beta$-mercaptoethanol, but were a little influenced by dithiothreitol, EDTA and NaCl. The three NTR fractions demonstrated enzyme activities for nitrobenzene and RDX as well as TNT.