Production of repetitive amino acid sequenced protein in Escherichia coli. = 대장균 내에서 반복적인 아미노산 서열을 가진 단백질 생산을 위한 연구

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Repetitive sequenced proteins and polypeptides are being highlighted as being the next new biomaterial for the future. Not only do they display outstanding mechanical properties, the proteins also exhibit biocompatibility. Spider silk has attracted much attention in the biotechnology field due to its great physical properties: strength, toughness, elasticity, as well as biocompatibility and biodegradability. However, mass production of spider silk has been imposed by the aggressive territorialism and cannibalism of spiders. Alternative ways to produce the silk has been studied including production of recombinant spider silk protein through Escherichia coli. This study shows the increased production of native- sized recombinant spider silk protein through engineering of promoters and introducing synthetic biology approach to increase the production of the silk protein. In addition, production of artificially made recombinant protein was shown as well. Tyrosine and phenylalanine were repeated within the recombinant gene and was expressed successfully in the E.coli system for the first time to our knowledge. In addition, to increase the production of the recombinant protein, charged tRNAs of both tyrosine and phenylalanine were expressed within the cell. These results show the possibility of mass production of spider silk protein as well as genetic strategies for expressing high molecular weight and repetitive sequenced proteins.
Advisors
Lee, Sang Yupresearcher이상엽researcher
Description
한국과학기술원 :생명화학공학과,
Publisher
한국과학기술원
Issue Date
2013
Identifier
325007
Language
eng
Description

학위논문(석사) - 한국과학기술원 : 생명화학공학과, 2013.8,[v, 42 p. :]

Keywords

Spider silk protein▼aorthogonal ribosomes▼apromoter exchange▼arecombinnt protein production; 거미실크단백질▼a오소거날 리보솜▼a방향족 아미노산▼a프로모터 치환▼a인위적 단백질 발현

URI
http://hdl.handle.net/10203/266350
Link
http://library.kaist.ac.kr/search/detail/view.do?bibCtrlNo=848989&flag=dissertation
Appears in Collection
CBE-Theses_Master(석사논문)
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