Journal of Microbiology and Biotechnology

The Korean Society for Microbiology and Biotechnology (한국미생물·생명공학회)
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Comparison of Alpha-Factor Preprosequence and a Classical Mammalian Signal Peptide for Secretion of Recombinant Xylanase xynB from Yeast Pichia pastoris

  • He, Zuyong (State Key Laboratory of Biocontrol, School of Life Sciences, Sun Yat-Sen University) ;
  • Huang, Yuankai (State Key Laboratory of Biocontrol, School of Life Sciences, Sun Yat-Sen University) ;
  • Qin, Yufeng (State Key Laboratory of Biocontrol, School of Life Sciences, Sun Yat-Sen University) ;
  • Liu, Zhiguo (State Key Laboratory of Biocontrol, School of Life Sciences, Sun Yat-Sen University) ;
  • Mo, Delin (State Key Laboratory of Biocontrol, School of Life Sciences, Sun Yat-Sen University) ;
  • Cong, Peiqing (State Key Laboratory of Biocontrol, School of Life Sciences, Sun Yat-Sen University) ;
  • Chen, Yaosheng (State Key Laboratory of Biocontrol, School of Life Sciences, Sun Yat-Sen University)
  • Received : 2011.09.15
  • Accepted : 2011.12.16
  • Published : 2012.04.28
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Abstract

The secretory efficiency of recombinant xylanase xynB from yeast Pichia pastoris between the ${\alpha}$-factor preprosequence and a classical mammalian signal peptide derived from bovine ${\beta}$-casein was compared. The results showed that although the bovine ${\beta}$-casein signal peptide could direct high-level secretion of recombinant xylanase, it was relatively less efficient than the ${\alpha}$-factor preprosequence. In contrast, the bovine ${\beta}$-casein signal peptide caused remarkably more recombinant xylanase trapped intracellularly. Real-time RT-PCR analysis indicated that the difference in the secretory level between the two signal sequences was not due to the difference in the transcriptional efficiency.

Keywords

References

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