Expression of the Bacillus subtilis levanase gene in Escherichia coli and Saccharomyces cerevisiae.
Wanker E 1 , Schörgendorfer K , Schwab H .
Author information
- 1 Institut für Biotechnologie, Technische Universität Graz, Austria.
Abstract
The gene coding for the inulin hydrolyzing enzyme levanase which was
previously cloned from Bacillus subtilis was fused to the tac-promoter. Overexpression in Escherichia coli resulted in high amounts of intracellularly produced levanase (up to 20 U mg-1).
After removal of the bacterial 5' sequences, the levanase gene was also
cloned into a yeast expression vector based on the PGK-promoter.
Clones containing the intact levanase gene including the bacterial
signal sequence gave rise to synthesis of active levanase by
Saccharomyces cerevisiae transformants.
A considerable amount of levanase protein was found in the culture
medium (around 0.5 U ml-1) indicating efficient secretion of B. subtilis
levanase from yeast.
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