Objectives
In an attempt α-amylase gene from <i>Pyrococcus woesei</i> was amplified and cloned into a pTYB2 vector to generate the recombinant plasmid pTY- α-amylase. Methods
<i>Escherichia coli</i> BL21 used as a host and protein expression was applied using IPTG. SDS-PAGE assay demonstrated the 100 kDa protein. Amylolytic activity of proteins produced by transformed <i>E. coli</i> cells was detected by zymography, and the rate of active α-amylase with and without the intein tag in both soluble conditions and as inclusion bodies solubilized by 4M urea were measured. Results
Amylolytic activity of ∼185,000 U/L of bacterial culture was observed from the soluble form of the protein using this system. Conclusion
These results indicate that this expression system was appropriate for the production of thermostable α-amylase.
Citations
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