Schofield, L.R., Neal, T.L., Patchett, M.L., Strange, R.C., Daniel, R.M. & Morgan, H.W. (1988). The Purification of Cellulase and Hemicellulase Components from an Extreme Thermophile by the Cloning of Enzymes into E. coli. Annuals of the New York Academy of Sciences, 542, 240-243.
Permanent Research Commons link: http://hdl.handle.net/10289/4543
The use of heat treatment to purify enzymes by selective denaturation and then by the subsequent precipitation of denatured protein is a simple, rapid, and well established procedure. Successful applications are limited to those few enzymes that possess a thermostability considerably higher than the majority of cell proteins. The introduction of thermostable enzymes into the protein population of a mesophile by cloning offers a clear opportunity to employ a heat-treatment method of purification to its full advantage (e.g., see references 1 and 2). In light of the difficulties involved in purifying bacterial cellulases, the cloning of some of the cellulase and hemicellulase genes of Caldocellum saccharolyticum into Escherichia coli has provided a welcome alternative procedure for obtaining pure enzymes.