Secretive expression of heterologous β-glucosidase in Zymomonas mobilis

Zichen Luo,Jie Bao

Published 2015 in Bioresources and Bioprocessing

ABSTRACT

BackgroundZymomonas mobilis is an efficient ethanol fermentation strain, but its narrow substrate range limits its fermentation in lignocellulose hydrolysate. As a potential consolidated bioprocessing (CBP) stain for bioethanol production, the ability of cellulose utilization was necessary. In this study, extracellular expression of β-glucosidase on Z. mobilis was studied as the first step for construction of a practical CBP strain to reduce the use of β-glucosidase in the cellulase components.ResultsThe heterologous β-glucosidase from Bacillus polymyxa was expressed in the ethanologenic strain Z. mobilis (ZM4) and secreted extracellularly by an endogenous signal peptide and a fusion protein. The signal peptide SP1086 of the endoglucanase gene ZMO1086 from Z. mobilis was identified and facilitated 12 % of the endoglucanase encoded by ZMO1086 from Z. mobilis ZM4 and 16 % of the β-glucosidase encoded by bglB gene secreted out of the membrane of Z. mobilis ZM4. Another method for enhancement of the β-glucosidase secretion is to fuse the β-glucosidase encoded by bglB with the levansucrase encoded by sacB from Z. mobilis ZM4 to achieve the secretive expression. Its expression level was enhanced two times but only showed a 2 % secretion ratio in this situation.ConclusionsThe SP1086 signal peptide showed an obviously secreting capacity of the β-glucosidase protein. The fusion protein with SacB also showed the secretion effect, but it was less efficient.

PUBLICATION RECORD

  • Publication year

    2015

  • Venue

    Bioresources and Bioprocessing

  • Publication date

    2015-06-30

  • Fields of study

    Biology, Chemistry, Engineering, Environmental Science

  • Identifiers
  • External record

    Open on Semantic Scholar

  • Source metadata

    Semantic Scholar

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