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RISS 인기검색어
- 검색키워드
- 저자 : ( Xingyuan Ma ) (검색결과 4 건)
- 무료
- 기관 내 무료
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Preparation and Properties of Graphene Oxide-Modified Anti-UV Waterborne Polyurethane Nanocomposites
Xingyuan Ma,Mingrui Zhang 성균관대학교(자연과학캠퍼스) 성균나노과학기술원 2020 NANO Vol.15 No.02
In this present study, graphene oxide (GO) was used as a secondary chain extender and a functional modification assistant to fabricate a three-dimensional nanocomposite (GO-WPU) with waterborne polyurethane (WPU) through the prepolymer dispersion. The tensile strength and elastic modulus of GO-WPU with 0.2 wt.% GO content, compared with those of pure WPU, increase by 170.38% and 50.9%, respectively. Even with a small amount of GO content added, the ultraviolet absorption rate significantly increased, whereas the ultraviolet transmittance decreased significantly. Other properties such as thermal stability and so on were also much enhanced. These results suggested that the functional nanocomposite GO-WPU prepared through the prepolymer dispersion will be an effective fabrication approach and have a wider scope of applications in functional coating materials and film materials.
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Ma Xingyuan,Zheng Wenyun,Wang Tianwen,Wei Dongzhi,Ma Yushu The Microbiological Society of Korea 2006 The journal of microbiology Vol.44 No.3
The Escherichia coli heat-labile enterotoxin B subunit (HLT-B) is one of the most powerful mucosal immunogens and known mucosal adjuvants. However, the induction of high levels of HLT-B expression in E. coli has proven a difficult proposition. Therefore, in this study, the HLT-B gene was cloned from pathogenic E. coli and expressed as a fusion protein with GST (glutathion S-transferase) in E. coli BL2l (DE3), in an attempt to harvest a large quantity of soluble HLT-B. The culture conditions, including the culture media used, temperature, pH and the presence of lactose as an inducer, were all optimized in order to obtain an increase in the expression of soluble GST-rHLT-B. The biological activity of the purified rHLT-B was assayed in a series of GMI-ELISA experiments. The findings of these trials indicated that the yield of soluble recombinant GST-rHLT-B could be increased by up to 3-fold, as compared with that seen prior to the optimization, and that lactose was a more efficient alternative inducer than IPTG. The production of rHLT-B, at 92 % purity, reached an optimal level of 96 mg/l in a 3.7 L fermentor. The specific GM1 binding ability of the purified rHLT-B was determined to be almost identical to that of standard CTB.
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Xingyuan Ma,Wenyun Zheng,Tianwen Wang,Dongzhi Wei 한국미생물학회 2006 The journal of microbiology Vol.44 No.3
The Escherichia coli heat-labile enterotoxin B subunit (HLT-B) is one of the most powerful mucosal immunogens and known mucosal adjuvants. However, the induction of high levels of HLT-B expression in E. coli has proven a difficult proposition. Therefore, in this study, the HLT-B gene was cloned from pathogenic E. coli and expressed as a fusion protein with GST (glutathion S-transferase) in E. coli BL21 (DE3), in an attempt to harvest a large quantity of soluble HLT-B. The culture conditions, including the culture media used, temperature, pH and the presence of lactose as an inducer, were all optimized in order to obtain an increase in the expression of soluble GST-rHLT-B. The biological activity of the purified rHLT-B was assayed in a series of GM1-ELISA experiments. The findings of these trials indicated that the yield of soluble recombinant GST-rHLT-B could be increased by up to 3-fold, as compared with that seen prior to the optimization, and that lactose was a more efficient alternative inducer than IPTG. The production of rHLT-B, at 92% purity, reached an optimal level of 96 mg/l in a 3.7 L fermentor. The specific GM1 binding ability of the purified rHLT-B was determined to be almost identical to that of standard CTB.
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( Di Liu ),( Fabiao Hu ),( Wenpeng Wang ),( Dong Wu ),( Xiujuan He ),( Wenyun Zheng ),( Haipeng Liu ),( Xingyuan Ma ) 한국미생물생명공학회(구 한국산업미생물학회) 2017 Journal of microbiology and biotechnology Vol.27 No.8
Escherichia coli heat-labile enterotoxin (LT) and its non-toxic mutant (LTm) are well-known powerful mucosal adjuvants and immunogens. However, the yields of these adjuvants from genetically engineered strains remain at extremely low levels, thereby hindering their extensive application in fundamental and clinical research. Therefore, efficient production of these adjuvant proteins from genetically engineered microbes is a huge challenge in the field of molecular biology. In order to explore the expression bottlenecks of LTm in E. coli, we constructed a series of recombinant plasmids based on various considerations and gene expression strategies. After comparing the protein expression among strains containing different recombinant plasmids, the signal sequence was found to be critical for the expression of LTm and its subunits. When the signal sequence was present, the strong hydrophobicity and instability of this amino acid sequence greatly restricted the generation of subunits. However, when the signal sequence was removed, abundantly expressed subunits formed inactive inclusion bodies that could not be assembled into the hexameric native form, although the inclusion body subunits could be refolded and the biological activity recovered in vitro. Therefore, the dilemma choice of signal sequence formed bottlenecks in the expression of LTm. These results reveal the expression bottlenecks of LTm, provide guidance for the preparation of LTm and its subunits, and certainly help to promote efficient preparation of this mucosal adjuvant protein.
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