1. Kluyveromyces as a host for heterologous gene expression: expression and secretion of prochymosin.
- Author
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van den Berg JA, van der Laken KJ, van Ooyen AJ, Renniers TC, Rietveld K, Schaap A, Brake AJ, Bishop RJ, Schultz K, and Moyer D
- Subjects
- Amino Acid Sequence, Animals, Base Sequence, Cattle, Chymosin genetics, Chymosin metabolism, Cloning, Molecular, Enzyme Precursors genetics, Enzyme Precursors metabolism, Kluyveromyces metabolism, Molecular Sequence Data, Plasmids, Protein Processing, Post-Translational, Protein Sorting Signals genetics, Protein Sorting Signals physiology, Recombinant Fusion Proteins genetics, Recombinant Fusion Proteins metabolism, Saccharomyces cerevisiae genetics, Species Specificity, Chymosin biosynthesis, Enzyme Precursors biosynthesis, Kluyveromyces genetics, Recombinant Fusion Proteins biosynthesis, Saccharomycetales genetics
- Abstract
We have developed the yeast Kluyveromyces lactis as a host organism for the production of the milk-clotting enzyme chymosin. In contrast to Saccharomyces cerevisiae, we found that this yeast is capable of the synthesis and secretion of fully active prochymosin. Various signal sequences could be used to efficiently direct the secretion of prochymosin in Kluyveromyces, but not in S. cerevisiae. We conclude that the efficient synthetic and secretory capacity of this heterologous protein is a property of the yeast Kluyveromyces. These results have led to the development of a large scale production process for chymosin.
- Published
- 1990
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