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Background    Lipomyces starkeyi  is one of the leading lipid-producing microorganisms reported to date; its genetic transformation was only recently reported. Our aim is to engineer  L. starkeyi  to serve in consolidated bioprocessing (CBP) to produce lipid or fatty acid-related biofuels directly from abundant and low-cost lignocellulosic substrates.    Results  To evaluate  L. starkeyi  in this role, we first conducted a genome analysis, which revealed the absence of key endo- and exocellulases in this yeast, prompting us to select and screen four signal peptides for their suitability for the overexpression and secretion of cellulase genes. To compensate for the cellulase deficiency, we chose two prominent cellulases,  Trichoderma reesei  endoglucanase II (EG II) and a chimeric cellobiohydrolase I (TeTrCBH I) formed by fusion of the catalytic domain from  Talaromyces emersonii  CBH I with the linker peptide and cellulose-binding domain from  T. reesei  CBH I. The systematically tested signal peptides included three peptides from native  L. starkeyi  and one from  Yarrowia lipolytica . We found that all four signal peptides permitted secretion of active EG II. We also determined that three of these signal peptides worked for expression of the chimeric CBH I; suggesting that our design criteria for selecting these signal peptides was effective. Encouragingly, the  Y. lipolytica  signal peptide was able to efficiently guide secretion of the chimeric TeTrCBH I protein from  L. starkeyi . The purified chimeric TeTrCBH I showed high activity against the cellulose in pretreated corn stover and the purified EG II showed high endocellulase activity measured by the CELLG3 (Megazyme) method.    Conclusions  Our results suggest that  L. starkeyi  is capable of expressing and secreting core fungal cellulases. Moreover, the purified EG II and chimeric TeTrCBH I displayed significant and potentially useful enzymatic activities, demonstrating that engineered  L. starkeyi  has the potential to function as an oleaginous CBP strain for biofuel production. The effectiveness of the tested secretion signals will also benefit future secretion of other heterologous proteins in  L. starkeyi  and, given the effectiveness of the cross-genus secretion signal, possibly other oleaginous yeasts as well.    Electronic supplementary material  The online version of this article (doi:10.1186/s12934-017-0742-5) contains supplementary material, which is available to authorized users.

Expression and secretion of fungal endoglucanase II and chimeric cellobiohydrolase I in the oleaginous yeast Lipomyces starkeyi