Sang-Woo BAE, Hye-Jin KANG, Sung-Mi HWANG, Woo-Jin CHANG, Sung Ho HA, Yoon-Mo KOO
언어
영어(ENG)
URL
https://www.earticle.net/Article/A105439
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원문정보
초록
영어
Recombinant protein is often produce by E.coli in the form of inclusion bodies (IBs). IBs are densed particle of proteins and do not have activity as protein. To convert IBs into water-soluble active protein, the refolding process is required. Ionic liquids (ILs) are organic salts composed of anion and cation, and the salts that do not crystallize at room temperature are called room temperature ionic liquids (RTILs) in particular. Tunable hydrophobicity and polarity of RTILs leads the expansion of its application in chemical and biological processes. In this study, we investigated how the hydrophobicity of RTILs affects protein refolding efficiency. Especially the effect of N-alkyl-N’-methylimidazolium methylsulfate having sulfur in anion part of ILs on target protein having the disulfide bond during refolding process. As the alkyl chain length increased the refolding efficiency generally decreased. In addition, we found that N-alkyl-N’- methylimidazolium methylsulfate is only effective as refolding additive when the target protein contain disulfide bond.
키워드
Protein refoldingIonic liqudisLysozyme
저자
Sang-Woo BAE [ Dept. of Biological Engineering, Inha University ]
Hye-Jin KANG [ Dept. of Biological Engineering, Inha University ]
Sung-Mi HWANG [ Dept. of Biological Engineering, Inha University ]
Woo-Jin CHANG [ Dept. of Biological Engineering, Inha University ]
Sung Ho HA [ Dept. of Biological Engineering, Inha University ]
Yoon-Mo KOO [ Dept. of Biological Engineering, Inha University ]
한국생물공학회 [The Korean Society for Biotechnology and Bioengineering]
설립연도
1984
분야
공학>생물공학
소개
이 법인은 생물 공학의 발전과 보급에 이바지하고, 회원 상호 간의 연구 협력과 친목을 도모함을 목적으로 한다
1. 생물공학 분야의 발전을 위한 연구 협력
2. 생물공학의 실용화를 촉진시키기 위한 산학 협동
3. 학술연구 발표회, 강연회, 연수회 등 학술활동의 개최
4. 국,영문 학술지,소식지,학술회의 Proceedings 및 학술도서의 발간
5. 생물공학 발전을 위한 정책 건의
6. 기타 국제 교류 등 본 학회의 목적 달성을 위한 제반 활동