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Background  The oleaginous yeast  Yarrowia lipolytica  is increasingly used as an alternative cell factory for the production of recombinant proteins. Recently, regulated promoters from genes  EYK1  and  EYD1 , encoding an erythrulose kinase and an erythritol dehydrogenase, respectively, have been identified and characterized in this yeast. Hybrid promoters up-regulated by polyols such as erythritol and erythrulose have been developed based on tandem copies of upstream activating sequences from  EYK1  (UAS1 EYK1 ) and  XPR2  (encoding extracellular protease, UAS1 XPR2 ) promoters.    Results  The strength of native (p EYD1 ) and engineered promoters ( pEYK1 - 3AB  and  pHU8EYK ) was compared using the extracellular lipase CalB from  Candida antarctica  as a model protein and a novel dedicated host strain. This latter is engineered in polyol metabolism and allows targeted chromosomal integration. In process conditions, engineered promoters  pEYK1 - 3AB  and  pHU8EYK  yielded 2.8 and 2.5-fold higher protein productivity, respectively, as compared to the reference  pTEF  promoter. We also demonstrated the possibility of multicopy integration in the newly developed host strain. In batch bioreactor, the CalB multi-copy strain RIY406 led to a 1.6 fold increased lipase productivity (45,125 U mL −1 ) within 24 h as compared to the mono-copy strain.    Conclusions  The expression system described herein appears promising for recombinant extracellular protein production in  Y. lipolytica .

Efficient expression vectors and host strain for the production of recombinant proteins by Yarrowia lipolytica in process conditions