Secretion of mouse alpha-amylase from Kluyveromyces lactis.
We constructed two mouse alpha-amylase secretion vectors for Kluyveromyces lactis using the well-characterized signal sequence of the pGKL 128 kDa killer precursor protein. Both PHO5 and PGK expression cassettes from Saccharomyces cerevisiae directed the expression of mouse alpha-amylase in YPD medium at a similar level of efficiency. K. lactis transformants secreted glycosylated and non-glycosylated alpha-amylase into the culture medium and both species were enzymatically active. The K. lactis/S. cerevisiae shuttle secretion vector pMI6 was constructed, and K. lactis MD2/1(pMI6) secreted about four-fold more alpha-amylase than S. cerevisiae YNN27 harboring the same plasmid, indicating that K. lactis is an efficient host cell for the secretion and production of recombinant proteins.[1]References
- Secretion of mouse alpha-amylase from Kluyveromyces lactis. Tokunaga, M., Ishibashi, M., Tatsuda, D., Tokunaga, H. Yeast (1997) [Pubmed]
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