• Journal of Sericultural and Entomological Science
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• v.38 no.1
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• pp.42-47
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• 1996

To investigate the host range determining factors of nuclear polyhedrois virus (NPV), Autographa california NPV and Bombyx mori NPV were coinfected into the two different cell lines, BmN-4 and Sf-9. The recombinant baculoviruses, RecS-A6 and RecB-727 which have an expanded host range, were isolated from Sf-9 and BmN-4 cell lines, respectively. The molecular biological characteristics of the recombinant baculoviruses were investigated. The pathogenicity of RecB-727 was similar to that of wild type BmNPV, while the pathogenicity of RecS-A6 was relatively lower than that of wild type BmNPV. The restriction enzyme digestion patterns of parental viruses and recombinant viruses showed that the recombinant virus has an expanded host range by genetic recombination. Southern blot analysis revealed that the p10 gene of RecB-727 was derived from AcNPV genomic DNA, while RecS-A6 has p10 gene of BmNPV in a viral genome. To investigate the host range expansion mechanism of recombinant baculovirus, HindIII-SacI 0.6 kb DNA fragments of RecS-A6 and RecB-727 were cloned and sequenced. The results showed that of wild type BmNPV helicase gene, suggesting that the expanded host range of recombinant baculoviruses was due to the insertion of BmNPV helicase gene into AcNPV viral genome.

• The monthly packaging world
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• s.280
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• pp.44-57
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• 2016

(사)한국포장재재활용사업공제조합은 자원의 재활용 촉진 및 환경친화적이며 효율적인 재활용 촉진을 위하여 그와 관련한 연구 및 기술개발을 수행 또는 지원을 바탕으로, 재활용 산업을 육성 발전시킴으로써 환경보전과 국민의 삶의 질 향상에 기여하며 "자원의 절약과 재활용 촉진에 관한 법률 제16조 제1항"의 규정에 의한 제품 포장재의 제조 수입 판매업자의 재활용 의무를 대행함을 목적으로 설립된 단체이다. 조합 연구소는 지난 4월 2015 포장재 자원순환 연차보고서를 발표했다. 본 고에서는 EPR대상 포장재 재활용 의무량 및 실력과 함께 연도별 포장재 재질 구조 등급별 시장조사, 재활용 현황에 대해 살펴본다.

• 환경사랑
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• s.35
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• pp.12-13
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• 2003

한국스티로폴공업협동조합 소속 단열재 생산업체에서는 기존의 KS규격(국가표준)에서 정하는 단열기준보다 더 높은 단열기준의 단체표준 규격을 제정하고, 조합의 단체표준규격을 통과한 제품에만 공동으로 정한 상표를 부착토록 하는 공동상표제도 시행을 위해 금년 11월말까지 설비보완 및 인증심사등을 완료하여 늦어도 2004년 1월부터 한단계 높은 단열재를 생산 보급할 예정이다

• Proceedings of the Korean Society of Applied Pharmacology
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• 1993.04a
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• pp.57-57
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• 1993

단백질 분해효소는 염증주변에 축적된 파괴조직이나 변성단백질등을 분해하여 염증, 특히 만성염증의 순환을 정상화함으로써 소염제로서 사용되어 왔으며 현재, Chymotrypsin, Trypsin, Promelain, Papain, Serrathiopeptidase, Pronase 등이 소염효소제로써 사용되고 있다. 이들은 주로 미생물 배양액에서 통상적인 방법으로 정제하여 사용하며, 유전자 재조합기술을 사용하여 재조합 균주에서 생산할 경우 그 생산성을 증대시킬수 있을 것이라 기대된다.

• 한국생물공학회:학술대회논문집
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• 2001.11a
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• pp.711-714
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• 2001

The production of the recombinant Plasmodium vivax merozoite surface protein (PvMSP) has been investigated in the recombinant E.coli system. Experimental optimization of the culture conditions, such as the effect of initial pH, and operating temperature has been tried on the growth of recombinant E.coli and on the overproduction of the target foreign protein.

• KSBB Journal
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• v.11 no.3
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• pp.311-316
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• 1996

The effects of polyethylene glycol (PEG) on glucoamylase production in recombinant Saccharomyces cerevisiae were studied. By PEG addition, the cell growth was not affected. However, the glucoamylase production was increased in all range of PEG molecular weights and concentrations. The optimal molecular weight of PEG was 6000 and the optimal concentration was 1g/L. Using these optimals, the extracellular glucoamylase activity was 23% higher in PEG-containing medium than that in medium without PEG.

• Environmental Analysis Health and Toxicology
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• v.19 no.3
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• pp.295-305
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• 2004

본 연구에서는 유전자 재조합 발광 박테리아를 이용하여 농약에 대한 박테리아의 스트레스 반응과 세포 독성을 분석하였다. 15종류의 농약에 대하여 유전자 손상, 생물막 손상, 산화적 손상 및 단백질 손상을 측정할 수 있는 발광 박테리아와 독성 유무로 인한 세포 독성을 측정할 수 있는 발광 박테리아, 5종을 이용하여 스트레스 반응을 분류하고 세포 독성 정토를 분석하였다. 그 결과, 농약의 화학적 구조가 박테리아의 스트레스 반응에 영향을 미치며, 산화과정이 진행 됨에 따라 독성의 작용 기작이 변하는 것을 확인 할 수 있었다. 이와 같은, 유전자 재조합 발광 박테리아를 이용한 생물체내의 독성 메커니즘에 대한 분석은 생태계 유해물질들에 의한 독성을 분석하고 예상하기 위해 적용될 수 있을 것이다.

• Microbiology and Biotechnology Letters
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• v.34 no.3
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• pp.273-277
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• 2006

To investigate the antigenicity and protective immunity of outer membrane protein H (OmpH) in Pasteurella multocida D:4, the recombinant OmpH protein was produced in Escherichia coli. The truncated and Trx-fused form of recombinant OmpH (53 kDa) was purified, and used as an antigen in the immunization and challenge experiment. The immunized mice with the recombinant OmpH produced a high-titer antibody, and had protective immunity against P. multocida as same level as the mice immunized with formalin-killed whole cell.

• KSBB Journal
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• v.28 no.5
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• pp.332-337
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• 2013

The gene encoding for xylose isomerase from the thermophilic bacterium Thermotoga maritima was cloned and recombinantly expressed in E. coli cells. Optimal activity was shown at $90^{\circ}C$ and pH 8.0. Treatment of saponin by recombinant xylose isomerase increased the growth inhibitory effect against human gastric cancer (AGS) cells and human colon cancer (HT-29) cells. On the other hand, treatment of fucoidan by the enzyme could not change the growth inhibitory effect against the same cancer cells. One ${\mu}g/ml$ of enzyme-treated saponin exhibited the same or higher growth inhibitory effect against both cancer cells compared with 100 ${\mu}g/ml$ of enzymeuntreated saponin. These results would be useful in the development of functional food or drug.

• Journal of Life Science
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• v.30 no.3
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• pp.304-312
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• 2020

Agarase can be used in the field of basic science, as well as for production of agar-derived high-functional oligosaccharides and bioenergy production using algae. In 2012, we summarized the classification, origin, production, and applications of agar. In this paper, we briefly review the literature on the recombinant expression of agarases from 2012 to the present. Agarase genes originated from 19 genera, including Agarivorans, Flammeovirga, Pseudoalteromonas, Gayadomonas, Catenovulum, Microbulbifer, Cellulophaga, Saccharophagus, Simiduia, and Vibrio. Of the 47 recombinant agarases, there were only two α-agarases, while the rest were β-agarases. All α-agarases produced agarotetraose, while β-agarases yielded many neoagarooligosaccharides ranging from neoagarobiose to neoagarododecaose. The optimum temperature ranged between 25 and 60℃, and the optimum pH ranged from 3.0 to 8.5. There were 14 agarases with an optimum temperature of 50℃ or higher, where agar is in sol state after melting. Artificial mutations, including manipulation of carbohydrate-binding modules (CBM), increased thermostability and simultaneously raised the optimum temperature and activity. Many hosts and secretion signals or riboswitches have been used for recombinant expression. In addition to gene recombination based on the amino acid sequence after agarase purification, recombinant expression of the putative agarase genes after genome sequencing and metagenome-derived agarases have been studied. This study is expected to be actively used in the application fields of agarase and agarase itself.