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KMID : 0545120120220040479
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Journal of Microbiology and Biotechnology
2012 Volume.22 No. 4 p.479 ~ p.483
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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
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Zuyong He
Yuankai Huang
Yufeng Qin
Zhiguo Liu
Delin Mo
Peiqing Cong
Yaosheng Chen
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Abstract
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The secretory efficiency of recombinant xylanase xynB from yeast Pichia pastoris between the α-factor preprosequence and a classical mammalian signal peptide derived from bovine β-casein was compared. The results showed that although the bovine β-casein signal peptide could direct highlevel secretion of recombinant xylanase, it was relatively less efficient than the α-factor preprosequence. In contrast, the bovine β-casein signal peptide caused remarkably more recombinant xylanase trapped intracellularly. Realtime 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.
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KEYWORD
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alpha-factor preprosequence, mammalian signal peptide, Pichia pastoris, qPCR, copy number
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