https://scholars.lib.ntu.edu.tw/handle/123456789/597187
標題: | Overproduction of soluble recombinant transglutaminase from Streptomyces netropsis in Escherichia coli | 作者: | Yu, Yu-Jen SHIH-CHENG WU Chan, Hung-Hsiang Chen, Yu-Cheng Chen, Zong-Yu Yang, Ming-Te |
關鍵字: | Cloning; Fusion protein; Microbial transglutaminase; Proregion; Streptomyces netropsis; Thioredoxin; PRO-TRANSGLUTAMINASE; MICROBIAL TRANSGLUTAMINASE; STREPTOVERTICILLIUM-MOBARAENSE; CORYNEBACTERIUM-GLUTAMICUM; PURIFICATION; EXPRESSION; CLONING; GENE; AMINOPEPTIDASE; IDENTIFICATION | 公開日期: | 十二月-2008 | 出版社: | SPRINGER | 卷: | 81 | 期: | 3 | 起(迄)頁: | 523 | 來源出版物: | Applied microbiology and biotechnology | 摘要: | A novel microbial transglutaminase (TGase) from the cultural filtrate of Streptomyces netropsis BCRC 12429 (Sn) was purified. The specific activity of the purified TGase was 18.2 U/mg protein with an estimated molecular mass of 38 kDa by sodium dodecyl sulfate polyacrylamide gel electrophoresis analysis. The TGase gene of S. netropsis was cloned and an open reading frame of 1,242 bp encoding a protein of 413 amino acids was identified. The Sn TGase was synthesized as a precursor protein with a preproregion of 82 amino acid residues. The deduced amino acid sequence of the mature S. netropsis TGase shares 78.9-89.6% identities with TGases from Streptomyces spp. A high level of soluble Sn TGase with its N-terminal propeptide fused with thioredoxin was expressed in E. coli. A simple and efficient process was applied to convert the purified recombinant protein into an active enzyme and showed activity equivalent to the authentic mature TGase. |
URI: | https://scholars.lib.ntu.edu.tw/handle/123456789/597187 | ISSN: | 0175-7598 | DOI: | 10.1007/s00253-008-1688-7 |
顯示於: | 醫學檢驗暨生物技術學系 |
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