• Journal of Industrial Technology
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• v.18
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• pp.417-423
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• 1998

Experiments were performed to evaluate UV/VIS absorbance and TOC of humic acid solutions which were ozonated at different pH values. The optimum conditions for ozonation of humic acid from this study are pH 9 (buffered) and 0.84 ($H_2O_2/HA$, w/w) for $H_2O_2$ dosage.

• Transactions of the Korean hydrogen and new energy society
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• v.19 no.1
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• pp.41-48
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• 2008

Fermentative $H_2$ production was studied using microbial consortia isolated from heat-treated ($90{\circ}C$, 20 min) sewage sludge. Important parameters investigated were carbon(C) and nitrogen(N)-sources, C/N ratio, phosphate concentration, pH and temperature during anaerobic cultivation in serum bottles. Starch, ribose, sucrose and glucose were good C-sources for the culture growth and $H_2$ production. Yeast extract was better N-source than $(NH_4)_2SO_4$ or peptone when individually added to the synthetic media, however the combination of above three N-sources exhibited the additional effect for cell growth and $H_2$ evolution. Addition of 100 mM phosphate as a buffering agent prevented the rapid pH drop during the cultivation. The optimum initial pH for the cell growth was at 7.0, whereas $H_2$ production was observed at pH 5.5. Optimum temperature for the cell growth and $H_2$ production was $37{\circ}C$. Initial C/N ratio of 1.22 in the media using glucose and yeast extract as the C- and N-sources, respectively, showed the $H_2$ yield 1.0 mol $H_2$/mol glucose.

• KSBB Journal
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• v.17 no.3
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• pp.307-310
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• 2002

In order to obtain high density seed cells for biofiltration, we studied batch and fed-batch culture of P. putida. Studies were carried out to find optimum fermentation conditions such as pH, concentration of glucose and agitation speed. Specific growth rate of P. putida was dependent on agitation speed and a high rpm of 300 was necessary to carry out the efficient aerobic growth of P. putida. Specific growth rate was highest at pH 7. Feeding glucose and yeast extract continuously at the initial growth phase was the most effective way to get high cell density of P. putida.

• KSBB Journal
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• v.14 no.4
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• pp.511-516
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• 1999

The effects of environmental and compositon factors, such as reaction time, metal ions, pH, agitation speed, the weight ratio of water to oil, and the weight of enzyme, on the hydrolysis of oils by Lipase-OF were investigated. In case of oils with low melting point, the optimum temperature of hydrolysis were the enzyme activity was maximum was 37$^{\circ}C$. However, when the melting temperature was higher than 4$0^{\circ}C$, the optimum temperature was around the fusion temperature. The activity of Lipase-OF decreased very rapidly with increase of temperature in the range of higher than 45$^{\circ}C$ and the activity perished above $65^{\circ}C$. The effect of agitation speed was investigated from 150 to 650 rpm. The hydrolysis of oils increased as the agitation speed increased up to 350 rpm, but it did not increase any more above 350 rpm. The weight ratio of water to oil was changed from 1 : 9 to 9 : 1 for the investigation of the effect on the hydrolusis. The weight ratio for maximum hydrolysis was 1 : 1. $Ca^{2+}\;and\;Mg^{2+}$ among various metal ions had some effect on the stimulation of hydrolysis. The optimum concentration of the ions was about 100ppm at which the hydrolysis increased, compared with that of distilled water, by 2 to 3%. The Optimum pH of Lipase-OF was 7. The hydrolysis decreased as the pH decreased as the pH decreased and also decreased as the pH increased. The content of enzyme affected the hydrolysis of oil. The hydrolysis increased with the content of Lipase-OF in the range of less than 0.013 wt% of substrate. However, the increase of hydrolysis with the content of Lipase-OF ceased above 0.013 wt%. The experiments investigating the effect of environmental and composition factors on the hydrolysis of oils showed that the optimum temperature was 37$^{\circ}C$, the pH 7, the concentration of $Ca^{2+}\;or\;Mg^{2+}$ 100 ppm, the agitation speed 350 rpm, the weight ratio of water to oil 1 : 1, and the content of Lipase-OF 0.013 wt% of substrate.

• Journal of Mushroom
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• v.14 no.4
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• pp.191-196
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• 2016

This study was conducted to investigate optimum conditions for mass production of ntagonistic microbes Alcaligenes sp. HC12. Alcaligenes sp. HC12 had a potent biological control agent to control browning disease caused by Pseudomonas agarici. Alcaligenes sp. HC12 markedly showed the antagonistic activity against Pseudomonas agarici, the most destructive pathogen of cultivated mushrooms. To define the optimum conditions for the mass production of the Alcaligenes sp. HC12, we have investigated optimum culture conditions and effects of various nutrient source on the bacterial growth. The optimum initial pH and temperature were determined as pH 9.0 and $30^{\circ}$, respectively. The optimal concentration of medium elements for the growth of pathogen inhibitor bacterium(Alcaligenes sp. HC12) was determined as follows: 0.5% dextrine, 1.5% yest extract, 1.0% $NaNO_3$, 0.5% $KH_2PO_4$, and 1.5% asparagine.

• Microbiology and Biotechnology Letters
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• v.32 no.2
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• pp.184-189
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• 2004

Rice wine cake (RWC) is the solid waste obtained after rice wine fermentation. For the mass production of the spores of yeast Saccharomyces from RWC, the optimum pretreatment condition of RWC, the optimum composition of culture medium, and the optimum culture condition were examined. For sporulation, yeast cells were grown in the pre sporulation medium (PSM), transferred into sporulation medium (SM) containing 1 % potassium acetate, and incubated in a rotary shaking incubator at $25^{\circ}C$ for 4 days. The supernatant of the mixture of RWC and water was used as the presporulation medium (PSM). The optimum temperature and time for the pre-incubation of the mixture of RWC and water (1:2) to obtain maximum sporulation yield were $V^{\circ}C$ and 24 hr, respectively, and optimum culture time in PSM was 48 hr. Using these optimum conditions, the asci number obtained was 0.72$ 1.06${\times}$10^{8}$$m\ell$. The addition of wheat coat koji into SM increased the final number of asci to beTEX>$10^{8}$ $m\ell$. Spores were formed in the SM with the initial pH of 7-11, but no spores were formed in the SM with the initial pH of 5. To save the time and effort to pretreat the RWC, 2% and 0.5% RWC without any pretreatment were directly added into PSM containing 1 % brown sugar and SM, respectively, and the maximum asci number of $1.27${\times}$10^{8}$ /$m\ell$ was obtained.

• International Journal of Industrial Entomology and Biomaterials
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• v.22 no.2
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• pp.83-93
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• 2011

Biochemical and enzymatic characterization for extracellular protease isolated from Cordyceps militaris cultivated on rice bran medium was investigated. C militaris produced proteolytic enzymes from 10 days after inoculation, maximum enzyme production was found at 25 days. The optimum temperature and pH of proteases production was at $25^{\circ}C$ and pH 7.0, respectively. The protease activity was observed in the four peaks (Pro-I, Pro-II, Pro-III, and Pro-IV) separated through Sephadex G-100 column chromatography. The separated protease was optimally active at $25^{\circ}C$. Optimum pH of the protease was between 7 and 8. Enzyme was also stable over at $30-80^{\circ}C$. The enzyme was highly stable in a pH range of 4-9. Protease activity was found to be slightly decreased by the addition of $Mg^{2+}$, $Mn^{2+}$, $Zn^{2+}$, $Fe^{2+}$ and $Cu^{2+}$, whereas inhibited by the addition of $Ca^{2+}$ and $Co^{2+}$ Protease activity was inhibited by protease inhibitor PMSF. On the other hand, the partially purified protease was investigated on proteolytic protease activity by zymogram gel electrophoresis using three substances (casein, gelatin and fibrin). Four active bands (F-I, FII, F-III, and F-IV) of fibrin degradation were revealed on fibrin zymogram gels. Both of F-II and FIII showed caseinolytic, fibrinolytic and gelatinolytic activities in three gels. Thermostability, pH stability, and pH-thermostability of the enzyme determined the residual fibrinolytic activity also displayed on fibrin zymogram gel. The only one enzyme (F-II) displayed over a broad range of temperature at $30-90^{\circ}C$. The FII displayed fibrinolytic activity in the pH range 3-5, but was inactivated in the range of pH 6-11. The F-I and F-III showed enzyme activity in the pH range of 6-11. In the pH-thermostability, the F-II only kept fibrinolytic activity after heating at $100^{\circ}C$ for 10, 20 and 30 min at pH 3 and pH 7, respectively. On the other hand, the F-II was retained activity until heating for 10 min under pH 11 condition. By using fibrin zymogram gel electrophoresis, extracellular fibrinolytic enzyme F-II from C. militaris showed unusual thermostable under acid and neutral conditions.

• Journal of Microbiology and Biotechnology
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• v.8 no.5
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• pp.501-508
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• 1998

An alkalophilic mi.croorganism (strain YB380), which produces yeast cell wall hydrolase extracellulary, was isolated from Korean soil. The rod-shaped cells were 0.3~0.4 by 2~4${\mu}{\textrm}{m}$ long, motile, aerobic, gram-positive, and spore-forming. The color of the colony was light yellow. The temperature range for growth at pH 9.0 was 25 to $45{\circ}C, with optimum growth at $35{\circ}C. The pH range for growth at $35{\circ}C was 8 to 11 with an optimum pH of 9.0. Therefore, the strain YB380 is an obligate alkalophile. The 16S rRNA of strain YB380 has a 99% sequence similarity with that of Bacillus alcalophilus. On the basis of physiological properties, cell wall fatty acid composition, and phylogenetic analysis, we propose that the isolated strain is Bacillus alcalophilus. The yeast cell wall hydrolase from Bacillus alcalophilus subsp. YB380 has been purified and partially characterized. The molecular weight was estimated to be 27,000 daltons with an optimum temperature and pH of $60{\circ}C and 9.0, respectively. The N-terminal amino acid sequence of the enzyme was analyzed as Gln- Thr- Val- Pro- Trp- Gly- Ile- Asn- Arg- Val.

• Journal of Soil and Groundwater Environment
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• v.6 no.2
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• pp.23-30
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• 2001

Column tests were carried out to examine the effect of surfactant solution conditions on the surfactant-enhanced remediation of soil columns contaminated by toluene. The conditioned parameters of the surfactant solution for the column tests were concentration, pH, temperature and flow rate. The test results revealed that an optimum condition was achieved for 4% (v/v) of concentration, 10 of pH, $20^{\circ}C$ of temperature and 4 mL/min of flow rate respectively. The removal of 95% of toluene was obtained when optimal conditions of each surfactant solution parameter were simultaneously met. This was a marked improvement and removal efficiency increased by 6-19% compared to that with unadjusted conditions. The optimum range of these parameters may be useful for a surfactant-based remediation in the aquifer contaminated by toluene.

• The Korean Journal of Mycology
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• v.21 no.4
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• pp.285-292
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• 1993

For the enzymatic conversion of 5'-XMP to 5'-GMP, partially purified XMP aminase from Escherichia coli was coupled with the yeast, Saccharomycrs cerevisiae, capable of ATP regeneration through glycolytic pathway. In order to elevate the level of XMP aminase in E. coli, $guaB^{-}(IMP\;dehydrogenase-less)$ mutant were introduced, and the yeast used as ATP supplier was treated by some method to increase its membrane permeability. The optimum conditions for efficient conversion reaction by energy-coupled system were investigated. As the results, a CH 41, $guaB^-$ mutant of E. coli K-12, showed 2.75 fold increase in the level of XMP aminase, compared with its parent cell. And the lyophylized yeast was the most effective at the ATP supplier. The optimum temperature and pH of conversion reaction were $40{\circ]C$ and pH 7.4, and the highest conversion ratio was shown under the reaction condition of 100 mM glucose, 100 mM inorganic phosphate and 6 mM AMP. When 36 units/ml XMP aminase used under the above conditions, the amount of 60 mg/ml yeast was sufficient to be used. Under the optimum condition, 71% of 1.8 mM(65.6 mg/100 ml) 5'-XMP was converted to 5'-GMP within 8 hr.