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Background  Cellulose is highly recalcitrant and thus requires a specialized suite of enzymes to solubilize it into fermentable sugars. In  C .  thermocellum , these extracellular enzymes are present as a highly active multi-component system known as the cellulosome. This study explores the expression of a critical  C .  thermocellum  cellulosomal component in  T .  saccharolyticum  as a step toward creating a thermophilic bacterium capable of consolidated bioprocessing by employing heterologously expressed cellulosomes.    Results  We developed an inducible promoter system based on the native  T .  saccharolyticum xynA  promoter, which was shown to be induced by xylan and xylose. The promoter was used to express the cellulosomal component  cipA *, an engineered form of the wild-type  cipA  from  C .  thermocellum . Expression and localization to the supernatant were both verified for CipA*. When a Δ cipA  mutant  C .  thermocellum  strain was cultured with a CipA*-expressing  T .  saccharolyticum  strain, hydrolysis and fermentation of 10 grams per liter SigmaCell 101, a highly crystalline cellulose, were observed. This trans-species complementation of a  cipA  deletion demonstrated the ability for CipA* to assemble a functional cellulosome.    Conclusion  This study is the first example of an engineered thermophile heterologously expressing a structural component of a cellulosome. To achieve this goal we developed and tested an inducible promoter for controlled expression in  T .  saccharolyticum  as well as a synthetic  cipA . In addition, we demonstrate a high degree of hydrolysis (up to 93%) on microcrystalline cellulose.

Functional heterologous expression of an engineered full length CipA from Clostridium thermocellum in Thermoanaerobacterium saccharolyticum