• Title/Summary/Keyword: 써모토가 마리티마

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Characterization of the recombinant cellulase B from Thermotoga maritima (Thermotoga maritima 유래 내열성 cellulase B 융합단백질의 특성 규명)

  • Chung Ho Kim
    • Journal of Applied Biological Chemistry
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    • v.65 no.4
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    • pp.383-386
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    • 2022
  • A gene encoding thermostable cellulase B (TmCelB) was isolated from Thermotoga maritima. The open reading frame (ORF) of TmCelB gene was 825bp long which predicted to encode 274 amino acid residues with a molecular weight of 31,732 Da. The 17 amino acid residues from N-terminal of the TmCelB was known as signal peptides. To analyze the enzymatic activity and biochemical properties, the ORF of TmCelB gene excluding a putative signal sequence encoding 17 amino acids were introduced into the E. coli expression vector, pRSET-B, and overexpressed in E. coli BL21. The optimum temperature of recombinant TmCelB was around 95 ℃, and the optimum pH of recombinant TmCelB was around pH 4.5. The recombinant TmCelB was stable at temperature below 100 ℃.