Cloning and expression of a xylanase gene from Clostridium acetobutylicum P262 in Escherichia coli
- Cite this article as:
- Zappe, H., Jones, D.T. & Woods, D.R. Appl Microbiol Biotechnol (1987) 27: 57. doi:10.1007/BF00257254
- 46 Downloads
A xylanase gene from Clostridium acetobutylicum P262 was cloned on a recombinant plasmid pHZ300 which enabled Escherichia coli HB101 cells to produce intracellular xylanase activity. The xylanase gene was located on a 2 kb DNA fragment. The cloned xylanase had an apparent Mr of approximately 28 000 and an isoelectric point of approximately 10. Optimum xylanase activity was obtained at pH 6.0 at 37–43° C. Comparison with a xylanase partially purified from the culture medium of C. acetobutylicum P262 showed that the enzymes had similar characteristics and western blot analysis showed cross-reactivity between antibodies raised against the purified cloned enzyme and a polypeptide of the same Mr from C. acetobutylicum P262.