• 한국가스학회지
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• 제23권2호
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• pp.61-67
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• 2019

우리나라는 천연가스 수입국으로 2018년 미국이 수출한 물량의 20%를 수입할 정도로 많은 양을 수입하고 있다. 이에 가스 수요를 만족시키며, 기후변화 대응에 효과적으로 대응할 수 있는 바이오가스는 대체제가 될 수 있을 것으로 생각된다. 그러나 바이오가스의 생산량의 20%만이 판매되고 있고, 이 역시 효율이 좋지 못해 활용하기 어려운 실정이다. 본 연구에서는 바이오가스를 도시가스로 공급 할 수 있는 최적의 정제 시스템을 개발을 목적으로 하였다. 시스템 선정을 위한 바이오가스에 대한 분석, 시스템 설계를 위한 사례 발굴, 시나리오 구성, 비용편익 툴을 개발하고 사례 적용하여 최적의 시스템을 개발하고자 하였다.

• 생물환경조절학회지
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• 제3권2호
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• pp.136-144
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• 1994

A long- time aeration method was developed for purification of animal wastewater. Under repeated aereations of 4 hours on and 4 hours off, the higher removal rates were obtained which were in average of 99%, 96%, 92% and 50% for BOD, SS, total nitrogen and phosporous, respectively. In detail, the measured BOD concentrations of the influent and effluent were 2,700ppm and 40ppm while the SS concentrations in the primary chamber and of the effluent were about 3,000 and 110 ppm, respectively. Zeolite and activated carbon, applied for removing the nitrogen and phosphorous, showed a good absorption, especially zeolite for NH$_4$-N and activated carbon for NO$_3$-N and PO$_4$-P. The treatment cost per head by this method amounts to 1,923 won and it comes to 1.6% in the whole production cost. Therefore, this method is economically available with the half cost of the conventional activated sludge process.

• 한국생물공학회:학술대회논문집
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• 한국생물공학회 2003년도 생물공학의 동향(XII)
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• pp.501-504
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• 2003

A novel prepurification method was developed aiming at increasing yield and purity, also reducing solvent usage for purification of paclitaxel. This method was a simple and efficient procedure, for the isolation and prepurification of paclitaxel from the biomass of Taxus chinensis, consisting of micelle formation, followed by two steps of precipitation. The use of a micelle and precipitation in the prepurification process allows for rapid separation of paclitaxel from interfering compounds and dramatically reduces solvent usage compared to alternative methodologies. This prepurification process serves to minimize the size and complexity of the HPLC operations for paclitaxel purification. This process is readily scalable to a pilot plant and eventually to a production environment where multikilogram quantities of material are expected to be produced. As much as possible, the process has been optimized to minimize solvent usage, complexity, and operating costs.

• 한국양식학회지
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• 제19권1호
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• pp.40-46
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• 2006

Bacillus subtilis strain with highly active chitosanase was isolated from the intestine of Sebastiscus marmoratus (scorpion fish). It was named as Bacillus subtilis CH1 by morphological, biochemical and 165 rRNA gene analysis. The optimal conditions for chitosanase production were investigated. The optimum carbon and nitrogen sources for Bacillus stibtilis CH1 were 2% starch and 1% yeast extract respectively. Unlike other chitosanases, the expression of this chitosanase was not induced or slightly induced with chitosan. The chitosanase secreted into the medium were concentrated with ammonium sulfate precipitation and purified by gel permeation chromatography. The molecular weight of purified chitosanase was 30 kDa. The optimum pH and temperature of purified chitosanase were 5.5 and $60^{\circ}C$ respectively. The purified chitosanase was continuously thermostable at $40^{\circ}C$ and showed stable activity between pH 6.0 and 8.0. Chitosanase activity of Bacillus subtilis CH1 under optimum condition was 4.1 units/ml.

• 한국미생물·생명공학회지
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• 제31권2호
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• pp.201-204
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• 2003

Glycopeptide antibiotics, teicoplanin was purified from a mutant strain of Actinoplanes teichomyceticus ATCC31121, A. teichomyceticus MSL2211. We developed a simple procedure to separate and purify the teicoplanin from the fermentation broth. Teicoplanin was purified by two-step purification system, hydrophobic adsorption and sugar affinity chromatography in combination with HPLC analysis based on the properties of hydrophobic acyl chain and sugar moiety in teicoplanin. Teicoplanin was separated from the culture broth by Diaion HP-20 and further purified by concanavalin A affinity column chromatography. As an adsorbent resin, Diaion HP-20 in broth eliminated toxic effects on growth, reduced feedback repression of teicoplanin production, and assisted In rapid recovery of teicoplanin. The teicoplanin displayed the final yield of 80% and 95% of purity.

• 한국생물공학회:학술대회논문집
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• 한국생물공학회 2000년도 추계학술발표대회 및 bio-venture fair
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• pp.619-622
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• 2000

For the production of $B^{30}-homoserine$ human insulin precursor, four types of fusion peptides LacZ, MBP, GST, and His-tagged sequence were studied in this work. Recombinant E. coli JM 103 and E. coli JM 109 containing fusion peptides were cultivated at $37^{\circ}C$ for 1hr, and gene expression was occurred when 0.5mM of isopropyl-D-thiogalactoside(IPTG) was added to the culture broth, and followed by longer than 4hr fermentation respectively. DEAE-Sphacel and gel filtration chromatography, amylose and glutathione-Sepharose 4B affinity chromatography, and nickel-affinity chromatography system were employed as purification of $B^{30}-homoserine$ human insulin precursor. Recovery yields of His-tagged, LacZ, GST, and MBP fused $B^{30}-homoserine$ human insulin precursor resulted in 47%, 20%, 20%, and 18%, respectively.

• Journal of Microbiology and Biotechnology
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• 제9권2호
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• pp.219-222
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• 1999

A simple sequence of membrane concentration and DEAE-Cellulose chromatography has been optimized to give a purified dextransucrase from Leuconostoc mesenteroides B-512FMCM with the highest specific activity (248.8 IU/mg protein) ever reported in high yield (overall 88.7%) for dextransucrase. When there was no sucrose in the dextransucrase and the dextran reaction digest, the dextransucrase hydrolyzed glucose from dextran. The glucose was transferred to the other glucoses from dextran and formed isomaltose and isomaltodextrin. The transglycosylation efficiency of glucose from dextran was much higher with acceptors. The dextransucrase can be used for the production of various kinds (or structures) of oligosaccharides using dextran and various acceptors with almost 100% theoretical yield.

• Journal of Microbiology and Biotechnology
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• 제13권4호
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• pp.620-623
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• 2003

The delta sleep-inducing peptides (DSIP, Trp-Ala-Gly-Gly-Asp-Ala-Ser-Gly-Glu) is an important regulatory hormone, controlling hypothalamus and pituitary functions. In the current study, an expression system was designed for the rapid and economic expression oi recombinant DSIP for biophysical studies. Artificially synthesized oligonucleotides encoding DSIP were cloned into a pGEX-KG vector and expressed in E. coli (BL21). The recombinant GST-DSIP was then readily purified using a GST affinity column. To obtain intact DSIP from the GST-DSIP, thrombin cleavage and a CNBr reaction were successively carried out. The DSIP in the CNBr reaction mixture was subjected to RP-HPLC purification to yield 1.2 mg DSIP from a 1 liter culture of E. coli. Identification of the DSIP was peformed using MALDI-MS and an amino acid composition analysis.

• Food Science and Biotechnology
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• 제14권5호
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• pp.581-585
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• 2005

The antimicrobial activity of partially purified enterocin K25, produced by Enterococcus sp. K25, was abolished by proteases such as pepsin and proteinase K. The bacteriocin was resistant to heat treatment at $75^{\circ}C$ for 15 min and lost 75% of its activity at $100^{\circ}C$ for 30 min. Enterocin K25 showed bactericidal mode of action against an indicator strain, Lactobacillus plantarum NCDO 955. Enterocin K25 was purified to 112.6-fold purity via conventional steps of ammonium sulfate precipitation, ion exchange chromatography, and reversed phase high performance liquid chromatography (RP-HPLC). The molecular mass of the purified enterocin K25 was estimated as 4.3 kDa on an electrophoresis gel. Plasmid (${\sim}6.5\;kb$) linkage of production of enterocin K25 was confirmed by plasmid curing.

• Journal of Pharmaceutical Investigation
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• 제8권2호
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• pp.1-10
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• 1978

During the course of studies on the production of glutathione from yeast, process development and optimization was carried out. The optimal pH for the extraction of glutathione was found to be 2.5 to 4.0 and the maximum yield for glutathione was obtained when the extraction temperature was 25 to $45^{\circ}C$. The cuprous salt of glutathione was recovered maximally at the range of 2 to 4g of cuprous oxide per 10 Kg of compressed yeast. Further purification was needed for the removal of impurities from glutathione. Cation exchange resin, anion exchange resin and Sephadex G-25 were employed for this purpose. 13 to 15 g of glutathione was obtained from 10 Kg of compressed yeast and the purity was above 99.3%.