• 자원리싸이클링
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• 제17권3호
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• pp.35-41
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• 2008

석유를 대체할 수 있는 자원 중의 하나인 오일샌드 역청의 열화학적 전환을 통해 생산된 연료유 특성을 열천칭 분석기와 중질유들의 전환 공정에 사용되는 딜레이드 코킹 반응기(600ml)를 이용하여 분석하였다. 동일한 $50^{\circ}C/min$의 승온 속도로 최종 코킹 온도를 $400{\sim}550^{\circ}C$까지 변화시킨 결과, 최종 코킹 온도가 증가할수록 코킹이 완료되는 시간과 전환률이 증가하였다. 그러나 $450^{\circ}C$이상의 온도에서는 미비하게 증가하여 코킹 운전이 적어도 $450^{\circ}C$ 이상이 되어야 함을 알 수 있었다. 딜레이드 코킹 반응기의 최대 액체 수율은 $475^{\circ}C$의 조건으로 나타났으며 코킹에 의해 생성되는 오일의 API, SIMDAS분석을 통해 경질화가 진행되어 일반적인 디젤과 비슷한 연료 특성을 가짐을 확인하였다.

• KSBB Journal
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• 제25권4호
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• pp.357-362
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• 2010

Green alga, Ulva pertusa kjelmann has been known to be one of the largest pollutants in Korea. Therefore, the efficient pretreatment processes have been required to improve the yields of fermentable sugar. The optimal pretreatment conditions were determined to be $195^{\circ}C$ for 15 min. The sugar yield of glucose and xylose were estimated as 20.5%, and 5.0% respectively, based on theoretical yields. However solid residues were estimated enzymatic digestibility of 90-95% with cellulase loading of 15 FPU/g glucan. This process was proved to generate the low concentration of Hydroxy-Methyl-Furfural (51 ppm), which resulted in ethanol production with 95% of the maximum conversion yield from glucose in the culture of Saccharomyces cerevisiae (ATCC, 24858). This study showed that Ulva pertusa kjellmann can be used as a bioetahnol resource using the high temperature liquefaction process.

• Korean Chemical Engineering Research
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• 제61권4호
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• pp.561-569
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• 2023

푸르푸랄(furfural)은 리그노셀룰로오스 바이오매스(lignocellulose biomass)의 헤미셀룰로오스(hemicellulose) 성분 중 하나인 자일로스(xylose)로부터 생산되는 플랫폼 화학물질이다. 푸르푸랄은 페놀류 화합물이나 바이오 연료 등의 중요한 원료로 사용될 수 있다. 본 연구에서는 푸르푸랄 생산공정에서 일반적으로 사용되는 산 촉매인 황산(sulfuric acid)과 친환경적 촉매인 포름산(formic acid) 두 가지 촉매를 이용하여 회분식 반응 시스템(batch system)에서 자일로스로부터 푸르푸랄을 생산하기 위한 조건을 비교 및 최적화하였다. 자일로스의 초기 농도(10 g/L~100 g/L), 반응 온도(140~200 ℃), 황산 촉매(1~3 wt%), 포름산 촉매(5~10 wt%), 반응 시간에 따라 자일로스로부터 푸르푸랄 수율에 미치는 영향을 조사하였다. 촉매 종류에 따른 최적 조건은 다음과 같았다. 황산 촉매의 경우, 3 wt%의 촉매농도, 50 g/L의 초기 자일로스 농도, 180 ℃의 온도 10분의 반응시간에서 최대 58.97%의 푸르푸랄 수율을 얻었다. 포름산 촉매의 겨우, 5 wt%의 촉매농도, 50 g/L의 초기 자일로스 농도, 180 ℃의 온도, 150분 반응 시간에서 65.32%의 푸르푸랄 수율을 확보하였다.

• 한국작물학회:학술대회논문집
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• 한국작물학회 1999년도 추계 학술대회지
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• pp.145-167
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• 1999

Our self-sufficiency of food has become less than $30{\%}$ and our nation is highly dependant on world's grain market for food. which is unstable in long term due to the world population growth faster than food production. Therefore, it is a great possibility that food might become a political weapon by way of its global shortage. its purchasing difficulty in international free trade market. and the resultant price rising. Our maximal capability of food production has become the most outstanding problem in the dimension of future food security. It would be the utmost scheme for maximal production of food to realize the maximal utilization of arable land through the enlargement of sufficient farming land and the conversion of rotation system for the more grain production. Extensional enlargement of arable land can be positively executed through the development of farming land in domestic and abroad countries. The readjustment of arable land and the installation or irrigation and drainage system can enforce the farming basement for maximal utilization of arable land through the improved rotation between paddy and upland. The prevention policy against farming land encroachment should be strictly executed through grain production encouragement on resting or marginal lands and regulation of utilization conversion for the other than food production on high grade farming lands. It is also required urgently to develope high yielding and high quality varieties through advanced genetic technology for the improvement of unit area yield, especially of wheat, corn. and soybean we import in large quantity The maximal utilization of arable land for the highest production of food can be realized through rational rotation system, the most adaptable crop cultivation on the suitable land, and the most optimal fertilization through the GIS analysis of agricultural environment information on the basis of the computerized soil resource data on super detailed soil maps(1:5000) surveyed plot by plot of whole nation.

• Journal of Microbiology and Biotechnology
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• 제17권1호
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• pp.116-122
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• 2007

An efficient enzyme system for the synthesis of L-tyrosine was developed using a fed-batch reactor with continuous feeding of phenol, pyruvate, and ammonia. A thermo- and chemostable tyrosine phenol-lyase from Symbiobacterium toebii was employed as the biocatalyst in this work. The enzyme was produced using a constitutive expression system in Escherichia coli BL21, and prepared as a soluble extract by rapid clarification, involving treatment with 40% methanol in the presence of excess ammonium chloride. The stability of the enzyme was maintained for at least 18 h under the synthesis conditions, including 75 mM phenol at pH 8.5 and $40^{\circ}C$. The fed-batch system (working volume, 0.51) containing 1.0 kU of the enzyme preparation was continuously fed with two substrate preparations: one containing 2.2 M phenol and 2.4 M sodium pyruvate, and the other containing 0.4 mM pyridoxal-5-phosphate and 4M ammonium chloride (pH 8.5). The system produced 130g/I of L-tyrosine within 30h, mostly as precipitated particles, upon continuous feeding of the substrates for 22 h. The maximum conversion yield of L-tyrosine was 94% on the basis of the supplied phenol.

• 한국미생물·생명공학회지
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• 제19권4호
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• pp.398-404
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• 1991

효모를 Na-alginate에 고정화한 후 연속반응기를 이용한 glucose 발효로 에탄올을 생산하였다. 그 결과 고정화 효모의 활성화 시간은 20~25시간이었다. 연속발효에서 고정화효모의 온도안정성은 30~$37^{\circ}C$였으며 pH 안정성은 pH 4.0~pH 8.0, 최적 희석속도는 $0.2h^[-1}$ 이었고 에탄올생산 최적 당농도는 15%였다. 최적조건에서 에탄올수율은 0.23, 생산된 에탄올 농도는 33.90g/l 그리고 에탄올 생산성은 7.12g/$l\cdot h$로 각각 나타났다.

• KSBB Journal
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• 제27권6호
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• pp.341-346
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• 2012

Indican (indoxyl-${\beta}$-D-glucoside) is a colorless natural compound and can be used as a precursor for the production of indigo. This production step only require an enzyme, ${\beta}$-glucosidase, that readily screened from microbial resource by using selective media supplemented with indican as a sole carbon source. Agrobacterium tumefaciens was well grown in this media and thus presumed to produce a related enzyme. The corresponding gene, encoding a protein with a calculated molecular mass of 51 kDa, was cloned and overexpressed as MBP fusion proteins. The purified enzyme was determined to be a dimer and showed the maximum activity for indican at pH 7.0 and $40^{\circ}C$. The kinetic parameters for indican, Km and Vmax, were determined to be 1.4 mM and 373.8 ${\mu}M/min/mg$, respectively. The conversion yield of indican into indigo using this enzyme was about 1.7-1.8 folds higher than that of previously isolated enzyme from Sinorhizobium meliloti. Additionally, this enzyme was able to hydrolyze various ${\beta}$-1,4 glycoside substrates.

• Journal of Microbiology and Biotechnology
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• 제25권5호
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• pp.696-703
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• 2015

A gamma-aminobutyric acid (GABA)-producing microorganism was isolated from jeot-gal (anchovy), a Korean fermented seafood. The isolate, A156, produced GABA profusely when incubated in MRS broth with monosodium glutamate (3% (w/v)) at 37℃ for 48 h. A156 was identified as Lactobacillus sakei by 16S rRNA gene sequencing. The GABA conversion yield was 86% as determined by GABase enzyme assay. The gadB gene encoding glutamate decarboxylase (GAD) was cloned by PCR. gadC encoding a glutamate/GABA antiporter was located immediately upstream of gadB. The operon structure of gadCB was confirmed by RT-PCR. gadB was overexpressed in Escherichia coli BL21(DE3) and recombinant GAD was purified. The purified GAD was 54.4 kDa in size by SDS-PAGE. Maximum GAD activity was observed at pH 5.0 and 55℃ and the activity was dependent on pyridoxal 5'-phosphate. The K_m and V_max of GAD were 0.045 mM and 0.011 mM/min, respectively, when glutamate was used as the substrate.

• 펄프종이기술
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• 제47권1호
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• pp.17-23
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• 2015

In bioethanol from acid hydrolysis process, neutralization of acid hydrolyzate is essential step, which resulted in dissolved cations in glucose solution. Impact of cations to Saccharomyces cerevisiae in glucose solution was investigated focused on ethanol fermentation. Both potassium and sodium cations decreased the ethanol fermentation and glucose to ethanol conversion as potassium or sodium cations. In sodium cation, more than 1.13 N sodium cation in glucose solution led to ethanol production less than theoretical yield with severe inhibition. In 1.13 N sodium cation concentration, ethanol fermentation was slowed down to reach the maximum ethanol concentration with 48 h fermentation compared with 24 h fermentation in control (no sodium cation in glucose solution). In case of potassium cation, three different levels of potassium led to silimar ethanol concentration even though slight slow down of ethanol fermentation with increasing potassium cation concentration at 12 h fermentation. Sodium cation showed more inhibition than potassium cation as ethanol concentration and glucose consumption by Saccharomyces cerevisiae.

• 한국생물공학회:학술대회논문집
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• 한국생물공학회 2005년도 생물공학의 동향(XVII)
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• pp.243-246
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• 2005

A novel esterase showing high enantioselectivity to (S)-ketoprofen ethyl ester was selected from fosmid environmental DNA library which is provided by Microbial Genomic & Applications Center. As a result of Blast search, the gene wasn't registerated in Gene Bank yet. And as we know, conserved domain region of esterase , G-X-S-X-G, wasn't discovered.$^{4)}$ And it is similar to Beta-lactamase. The DNA sequence of cloned esterase include an open reading frame consisting of 1170 bp, designated as EST-Y29, encoding a protein of 389 amino acids with a molecular mass of about 42.8 kDa. And amino acid sequence analysis revealed only a few identity (28%) to tile known esterases/lipases in the databases containing the conserved sequence motifs of esterases/lipases. when being comparison to other esterase revealed , this enzyme seems to be classified as a new member of esterase family. EST-Y29 was functionally overexpressed in a soluble form in E. coli with maximum conversion yield of (S)-ketoprofen at $65^{\circ}C$. This study demonstrates that functional screening combined with the sequential uses of restriction enzymes to exclude already known enzymes is a useful approach for isolating novel enzyme from a metagenome.