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김성완,윤철종,최성우,김성우,우성훈,신남철,박승조 동아대학교 환경문제연구소 1999 硏究報告 Vol.22 No.2
We have investigated a performance of bio-electrode reactor for removal of nutrient like a nitrogen, phosphorus and organic substrate. Lab scale of bio-electrode reactor was operated with synthetic and tannery wastewater. Iron bar and stainless steel used for anode and cathode respectively. In experiment with synthetic wastewater, we were able to obtain the optimal current density range of 2.4-40 mA/dm² after 48 hrs operating time. And in that experiment, about 70~73% of ammonia nitrogen and 54~64% of phosphorus were removed. In experiment with tannery wastewater at 2.4-4.0 mA/dm², the removal rate of ammonia nitrogen, phosphorus and organic substract were about 62-69%, 45~59% and beyond 79% respectively.
리튬이차전지용 부극재료로서 은분말에 대한 전기화학적 특성
박철완,도칠훈,문성인,윤문수 한국공업화학회 2003 응용화학 Vol.7 No.2
Silver powders have been extensively studied as an anode active material for lithium secondary batteries. In the present study, a unique attempt is made to develop silver negative electrode by slurry method, because the silver electrode is a good candidate to replace the commercial graphite electrode for lithium rechargeable batteries. Silver electrode was prepared and its electrochemical properties were characterized gradual increasing test state of charge (GISOC) analysis method. Charge-discharge performance indicates that the initial charge potential range of Li/Ag cells has showed similar behaviors compared with Li/Graphite system and the irreversible capacity facd is also higher than Li/Graphite system.
Bacillus stearothermophilus KJ16이 생산하는 Cyclodextrin Glucanotransferase의 정제와 효소특성
김병우,김광현,남수완,권현주,송승구,윤종원 동의대학교 기초과학연구소 1999 基礎科學硏究論文集 Vol.9 No.1
Cyclodextrin glucanotransferase from B. stearothermophilus KJ16 that can produce both cyclodextrin glucanotransferase and cyclodextrinase was purified by ammonium sulfate precipitation, DEAE-cellulose chromatography, Sephadex G-100 chromatography, and FPLC. The molecular weight of the purified enzyme was about 65,000 dalton by SDS-PAGE. The optimal pH and temperature were 6.0 and 60℃, respectively. The enzyme was stable at 50℃ for 1 hr and in the pH range of 5.5 and 8.5. Mercaptoethanol and dithiothreitol inhibited the enzyme activity strongly. The enzyme produced 60% cyclodextrin(CD) from 5% soluble starch with the ^α-, ^β-, ^γ-CD ratio of 42 : 46 : 12. Amylopectin was the most suitable with 67% conversion to CD.
Utilization of the Bombyx mori Heat Shock Protein 70 Promoter for Screening Transgenic Silkworms
Seong Wan Kim,Seon Young Kim,Eun Young Yun,Kwang-Ho Choi,Seong Ryul Kim,Seok Woo Kang,Seung Won Park,Tae Won Goo 한국응용곤충학회 2014 한국응용곤충학회 학술대회논문집 Vol.2014 No.04
Silkworm transgenesis is now a routine method leading to a satisfactory yield of transformed animals and the reliable expression of transgenes during multiple successive generations. However, the screening of G1 transgenic individuals from numerous progeny has proved to be difficult and time-consuming work. Previously, we characterized the promoter of heat shock protein 70 from Bombyx mori (bHsp70), which is ubiquitously expressed in all tissues and developmental stages. To investigate the utilization of the bHsp70 promoter to screen transgenic individuals, the EGFP marker gene was inserted into the piggyBac vector under the control of the bHsp70 promoter. Mixtures of the donor and helper vectors were micro-injected into 3,060 eggs of bivoltine silkworms (Keomokjam). EGFP fluorescence was observed in 17 broods of transgenic silkworms under a florescence stereomicroscope. Interestingly, this fluorescent marker protein was detected not only in parts of the embryo segments on the seventh day of the G1 embryonic developmental stage but it was also detected in a part of the body of G1 hatched larvae, in the middle silk gland of G1 fifth instar larvae, and in the wings of seven-day-old G1 pupae and G1 moths. Therefore, we suggest that the bHsp70 promoter can be used for the rapid and simple screening of transgenic silkworms.
Expression of BmCecB1 Antimicrobial Peptide in the Body Fluids of Transgenic Silkworm.
Seong Wan Kim,Seon Young Kim,Eun Young Yun,Kwang-Ho Choi,Seong Ryul Kim,Seok Woo Kang,Seung Won Park,Tae Won Goo 한국응용곤충학회 2014 한국응용곤충학회 학술대회논문집 Vol.2014 No.04
This peptide has antibacterial activity against several Gram-positive and Gram-negative bacteria. BmCecB1 is antimicrobial peptides from Bombyx mori and belongs to cecropin family. Antimicrobial peptides are important components of the innate immune systems in all living organism. To produce the BmCecB1 antimicrobial peptide, we constructed transgenic silkworm that expressed BmCecB1 gene under the control BmA3 promoter using piggyBac vector. The use of the 3xP3-driven EGFP cDNA as a marker allowed us to rapidly distinguish transgenic silkworm. Mixtures of the donor vector and helper vector were micro-injected into 600 eggs of bivoltin silkworms, Baegokjam. In total, 49 larvae (G0) were hatched and allowed to develop into moths. The resulting G1 generation consisted of 22 broods, and we selected 2 broods containing at least 1 EGFP-positive embryo. The rate of successful transgenesis for the G1 broods was 11%. We identified 9 EGFP-positive G1 moths and these were backcrossed with wild-type moths. With the aim of identifying a BmCecB1 as antimicrobial peptide, we investigated the Radical diffusion Assay (RDA) and then demonstrated that BmCecB1 possesses high antibacterial activities against Gram-negative bacteria.
Seong Wan Kim,Seon Young Kim,Hye Lim Yeo,Eun Young Yun,Kwang-Ho Choi,Seong Ryul Kim,Seok Woo Kang,Seung Won Park,Tae Won Goo 한국응용곤충학회 2013 한국응용곤충학회 학술대회논문집 Vol.2013 No.10
Immune-inducible antimicrobial peptides were produced using transgenic silkworms that expressed Rel family transcription factor, truncated BmRelish1 (BmRelish1t) genes under the control of the BmA3 promoter using the piggyBac vector. BmRelish1t gene contains all domains of Bmrelish: a Rel homolog domain (RHD), nuclear localization signal (NLS), acidic and hydrophobic amino acids (AHAA) rich region except the Ankyrin repeat domain (ANK) and the death domain (DD). (1:1) Mixtures of the donor vector (pG-3xP3EGFP-BmA3BmRelish1t) and helper vector were micro-injected into 1,800 eggs of bivoltin silkworms, Baegokjam and EGFP-induced fluorescence was observed for 25 broods of transgenic silkworms under a florescence stereomicroscope. Analysis by real-time PCR indicated that transgenic silkworms expressing BmRelish1t recombinant proteins displayed higher mRNA expression levels of the Bombyx mori antimicrobial peptides such as lebocin, moricin, and nuecin than the normal silkworms. Moreover, transgenic silkworms expressing BmRelish1t showed antibacterial activity against Escherichia coli. We suggest that transgenic expression of BmRelish1t may find useful applications for the production of various antimicrobial peptides at the same time in transgenic silkworms.
Utilization of the B. mori Heat Shock Protein 70 Promoter for Screening Transgenic Silkworms
Seong Wan Kim,Hye Lim Yeo,Seon Young Kim,Eun Young Yun,Kwang-Ho Choi,Seong Ryul Kim,Seok Woo Kang,Seung Won Park,Tae Won Goo 한국응용곤충학회 2013 한국응용곤충학회 학술대회논문집 Vol.2013 No.10
Silkworm transgenesis is now a routine method leading to a satisfactory yield of transformed animals and the reliable expression of transgenes during multiple successive generations. However, the screening of G1 transgenic individuals from numerous progeny has proved to be difficult and time-consuming work. Previously, we characterized the promoter of heat shock protein 70 from Bombyx mori (bHsp70), which is ubiquitously expressed in all tissues and developmental stages. To investigate the utilization of the bHsp70 promoter to screen transgenic individuals, the EGFP marker gene was inserted into the piggyBac vector under the control of the bHsp70 promoter. Mixtures of the donor and helper vectors were micro-injected into 3,060 eggs of bivoltine silkworms (Keomokjam). EGFP fluorescence was observed in 17 broods of transgenic silkworms under a florescence stereomicroscope. Interestingly, this fluorescent marker protein was detected not only in parts of the embryo segments on the seventh day of the G1 embryonic developmental stage but it was also detected in a part of the body of G1 hatched larvae, in the middle silk gland of G1 fifth instar larvae, and in the wings of seven-day-old G1 pupae and G1 moths. Therefore, we suggest that the bHsp70 promoter can be used for the rapid and simple screening of transgenic silkworms.
피브로인 H-chain 재조합 단백질 발현시스템을 이용한 녹색형광실크 생산
김성완 ( Seong Wan Kim ),윤은영 ( Eun Young Yun ),최광호 ( Kwang Ho Choi ),김성렬 ( Seong Ryul Kim ),박승원 ( Seung Won Park ),강석우 ( Seok Woo Kang ),구태원 ( Tae Won Goo ) 한국잠사학회 2013 한국잠사곤충학회지 Vol.51 No.2
To express green fluorescent protein in the cocoon of silkworm, we constructed the fibroin H-chain expression system to produce enhanced green fluorescent protein (EGFP) in the cocoon of transgenic silkworms. The EGFP fusion protein, each with N- and C-terminal sequences of the fibroin H-chain, was designed to be secreted into the lumen of the posterior silk glands. The expression of the EGFP/H-chain fusion gene was regulated by the fibroin H-chain promoter. The use of the 3xP3-driven DsRed2 cDNA as a marker allowed us to rapidly distinguish transgenic silkworm. A mixture of the donor and helper vector was micro-injected into 1,200 eggs of bivoltin silkworms, Baegokjam. We obtained 8 broods. The cocoon displayed strong green fluorescence, proving that the fusion protein was present in the cocoon. Also, the presence of fusion proteins in cocoons was demonstrated by SDS-PAGE and immunoblotting. Accordingly, we suggest that the EGFP fluorescence silk will enable the production of the novel biomaterial based on the transgenic silk.
피브로인 H-chain 재조합 단백질 발현시스템을 이용한 황색형광실크의 제작
김성완 ( Seong Wan Kim ),최광호 ( Kwang Ho Choi ),김성렬 ( Seong Ryul Kim ),윤은영 ( Eun Young Yun ),박승원 ( Seung Won Park ),강석우 ( Seok Woo Kang ),구태원 ( Tae Won Goo ) 한국잠사학회 2014 한국잠사곤충학회지 Vol.52 No.2
We constructed the fibroin H-chain expression system to produce enhanced yellow fluorescent proteins (EYFP) in the silk of transgenic silkworm. Fluorescent silk could be made by fusing EYFP cDNA to the heavy chain gene and injecting it into a silkworm. The EYFP fusion protein, each with N- and C-terminal sequences of the fibroin H-chain, was designed to be secreted into the lumen of the posterior silk glands. The expression of the EYFP/H-chain fusion gene was regulated by the fibroin H-chain promoter. The yellow fluorescence proving that the fusion protein was present in the silk. Accordingly, we suggest that the EYFP fluorescence silk will enable the production of novel biomaterial based on the transgenic silk.