Earticle

초록

영어

GST fusion proteins not only act as solubility enhancing partners but also offer an important biological assay for direct protein-to-protein interactions. A protein of sponge, called silicatein, can catalyze silica deposition in vitro at an environment friendly condition. The soluble expression of silicatein was enhanced when expressed as a GST fusion protein in E.coli. Furthermore, this fusion protein was immobilized on GSH -coated plate via GST-tag and remained active to form silica layer on surface by means of biosilification in the presence of TEOS at an ambient condition, room temperature and neutral pH. Simultaneously, GFP or HRP protein was immobilized on silica surface by simple adding it during biosilification. Immobilized proteins retained their activity and were released gradually. This technique can be applied to form biocompatible silica coating for catalytic, diagnostic and sensing surface, and matrix for tissue cultures.

키워드

저자

• Mi-Ran KI [ Department of Biotechnology and Bioinformatics, Korea University. ]
• Ki Baek YEO [ Department of Biotechnology and Bioinformatics, Korea University. ]
• Ki Ha MIN [ Department of Biotechnology and Bioinformatics, Korea University. ]
• Eui Kyoung JANG [ Department of Biotechnology and Bioinformatics, Korea University. ]
• Seung Pil PACK [ Department of Biotechnology and Bioinformatics, Korea University. ]

참고문헌

발행기관

간행물

표지보기 관심저널 등록

• 간행물명

  한국생물공학회 학술대회

• 간기

  반년간

• 수록기간

  1985~2013

• 십진분류

  KDC 476 DDC 576