Comparison of alpha-factor preprosequence and a classical mammalian signal peptide for secretion of recombinant xylanase xynB from yeast Pichia pastoris.

Zuyong He, Yuankai Huang, Yufeng Qin, Zhiguo Liu, Delin Mo, Peiqing Cong, Yaosheng Chen

State Key Laboratory of Biocontrol, School of Life Sciences, Sun Yat-Sen University, Guangzhou 510006, People's Republic of China.

Journal of microbiology and biotechnology 2012 Apr

filter terms:

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 highlevel 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. 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.

Citation

Zuyong He, Yuankai Huang, Yufeng Qin, Zhiguo Liu, Delin Mo, Peiqing Cong, Yaosheng Chen. Comparison of alpha-factor preprosequence and a classical mammalian signal peptide for secretion of recombinant xylanase xynB from yeast Pichia pastoris. Journal of microbiology and biotechnology. 2012 Apr;22(4):479-83