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Background   Zygosaccharomyces bailii  is a diploid budding yeast still poorly characterized, but widely recognised as tolerant to several stresses, most of which related to industrial processes of production. Because of that, it would be very interesting to develop its ability as a cell factory. Gas1p is a β-1,3-glucanosyltransglycosylase which plays an important role in cell wall construction and in determining its permeability. Cell wall defective mutants of  Saccharomyces cerevisiae  and  Pichia pastoris , deleted in the  GAS 1 gene, were reported as super-secretive. The aim of this study was the cloning and deletion of the  GAS 1 homologue of  Z. bailii  and the evaluation of its deletion on recombinant protein secretion.    Results  The  GAS 1 homologue of  Z. bailii  was cloned by PCR, and when expressed in a  S. cerevisiae GAS 1 null mutant was able to restore the parental phenotype. The respective  Z. bailii  Δ gas 1 deleted strain was obtained by targeted deletion of both alleles of the  ZbGAS 1 gene with deletion cassettes having flanking regions of ~400 bp. The morphological and physiological characterization of the  Z. bailii  null mutant resulted very similar to that of the corresponding  S. cerevisiae  mutant. As for  S. cerevisiae , in the  Z. bailii  Δ gas 1 the total amount of protein released in the medium was significantly higher. Moreover, three different heterologous proteins were expressed and secreted in said mutant. The amount of enzymatic activity found in the medium was almost doubled in the case of the  Candida rugosa  lipase CRL1 and of the  Yarrowia lipolytica  protease XPR2, while for human IL-1β secretion disruption had no relevant effect.    Conclusions  The data presented confirm that the engineering of the cell wall is an effective way to improve protein secretion in yeast. They also confirmed that  Z. bailii  is an interesting candidate, despite the knowledge of its genome and the tools for its manipulation still need to be improved. However, as already widely reported in literature, our data confirmed that an "always working" solution to the problems related to recombinant protein production can be hardly, if never, found; instead, manipulations have to be finely tuned for each specific product and/or combination of host cell and product.

Cloning of the Zygosaccharomyces bailii GAS 1 homologue and effect of cell wall engineering on protein secretory phenotype