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

摘要

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.