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The Purification of Cellulase and Hemicellulase Components from an Extreme Thermophile by the Cloning of Enzymes into E. coli
Author(s) -
SCHOFIELD L. R.,
NEAL T. L.,
PATCHETT M. L.,
STRANGE R. C.,
DANIEL R. M.,
MORGAN H. W.
Publication year - 1988
Publication title -
annals of the new york academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.712
H-Index - 248
eISSN - 1749-6632
pISSN - 0077-8923
DOI - 10.1111/j.1749-6632.1988.tb25836.x
Subject(s) - thermophile , unit (ring theory) , cellulase , plant science , biology , botany , mathematics , enzyme , mathematics education , biochemistry
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