Biotechnology Letters

, Volume 34, Issue 1, pp 91–96

Trichoderma reesei cellobiohydrolase II is associated with the outer membrane when overexpressed in Escherichia coli

Authors

  • Diya M. Abdeljabbar
    • Department of Chemical & Biological EngineeringPrinceton University
  • Hank J. Song
    • Department of Chemical & Biological EngineeringPrinceton University
    • Department of Chemical & Biological EngineeringPrinceton University
    • Department of Molecular BiologyPrinceton University
    • A207 Engineering QuadranglePrinceton University
Original Research Paper

DOI: 10.1007/s10529-011-0743-0

Cite this article as:
Abdeljabbar, D.M., Song, H.J. & Link, A.J. Biotechnol Lett (2012) 34: 91. doi:10.1007/s10529-011-0743-0

Abstract

Cellulose degradation is essential for the future production of many advanced biofuels. Cellulases from the filamentous fungus Trichoderma reesei are among the most efficient enzymes for the hydrolysis of cellulosic materials. One of the cellulases from T. reesei, cellobiohydrolase II (CBH2), was studied because of its industrial relevance and proven enzymatic activity. Using both crude and rigorous membrane fractionation methods we show that full length T. reesei CBH2 is exclusively localized to the outer membrane when expressed recombinantly in Escherichia coli. Even fusing signal sequence-free maltose-binding protein to the N-terminus of CBH2, which has been shown to increase solubility of other proteins, did not prevent the outer membrane localization of CBH2. These results highlight the difficulties in producing fungal cellulases in bacterial hosts and provide a stepping stone for future cellulase engineering efforts.

Keywords

Fungal cellulaseFusion proteinHeterologous protein expressionMembrane localization

Copyright information

© Springer Science+Business Media B.V. 2011