| Title: | Comparison of alpha-factor preprosequence and a classical mammalian signal peptide for secretion of recombinant xylanase xynB from yeast Pichia pastoris |
| Author(s): | He Z; Huang Y; Qin Y; Liu Z; Mo D; Cong P; Chen Y; |
| Address: | "State Key Laboratory of Biocontrol, School of Life Sciences, Sun Yat-Sen University, Guangzhou 510006, People's Republic of China" |
| ISSN/ISBN: | 1738-8872 (Electronic) 1017-7825 (Linking) |
| 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 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" |
| Keywords: | "Amino Acid Sequence Animals Bacterial Proteins/chemistry/genetics/*metabolism Caseins/chemistry/*genetics Cattle Endo-1, 4-beta Xylanases/chemistry/genetics/*metabolism Gene Expression Mating Factor Molecular Sequence Data Peptides/chemistry/*genetics Pich;" |
| Notes: | "MedlineHe, Zuyong Huang, Yuankai Qin, Yufeng Liu, Zhiguo Mo, Delin Cong, Peiqing Chen, Yaosheng eng Comparative Study Research Support, Non-U.S. Gov't Korea (South) 2012/04/27 J Microbiol Biotechnol. 2012 Apr; 22(4):479-83. doi: 10.4014/jmb.1109.09031" |
