Construction of a novel secretion expression system guided by native signal peptide of PhoD in Zymomonas mobilis. Issue 4 (3rd April 2014)

• Record Type: Journal Article
• Authors: Wu, Bo; He, Ming-Xiong; Feng, Hong; Shui, Zong-Xia; Tang, Xiao-Yu; Hu, Qi-Chun; Zhang, Yi-Zheng
• Is Part Of: Bioscience, biotechnology, and biochemistry. Volume 78:Issue 4(2014)
• Page Start: 708
• Page End: 713
• Publication Date: 2014-04-03
• Subjects: Zymomonas mobilis -- secretion expression -- signal peptide -- α-amylase -- consolidated bioprocessing; Biotechnology -- Periodicals; Biochemistry -- Periodicals; 660.6
• DOI: 10.1080/09168451.2014.896736
• Languages: English
• ISSNs: 0916-8451

Abstract

Abstract: In the current study, three native signal peptides (SPs) from PhoC, PhoD, and ZMO0331were investigated and compared to construct novel secretion expression systems in Zymomonas mobilis . The secretion expression of target protein, α-amylase from Bacillus amyloliquefaciens (BAA), guided by PhoD's SP resulted in more hydrolysis of starch than that by the other two SPs. Extracellular and intracellular α-amylase activities of the strain containing PhoD's SP were also higher than the other two strains containing PhoC or ZMO0331's SP. In addition, the evidence by alcohol dehydrogenase activity assay further confirmed that the starch hydrolysis was resulted from the secretion expression of BAA rather than the breakage of cells. Our results indicated that the SP of PhoD is able to serve as a promising candidate to assist secretion expression of heterogeneous genes in Z. mobilis . This will contribute to development of engineered Z. mobili s strains converting starch into ethanol.