The Purification and Characterization of an Extremely Thermostable alpha-Amylase from the Hyperthermophilic Archaebacterium Pyrococcus furiosus
Contributor(s):
Davis, Bradley R.
Lewis, Marc S.
Anfinsen, Christian B. (Christian Boehmer), 1916-1995
Krutzsch, Henry C.
Privalov, Peter L.
Griko, Y. V.
Laderman, Kenneth A.
Journal of Biological Chemistry
Publication:
American Society for Biochemistry and Molecular Biology, 15 November 1993
Anfinsen believed that the discovery of hyperthermophilic bacteria in the early 1980s provided a valuable tool for the analysis of protein stability, because these bacteria made it possible to study the molecular mechanisms that governed structure and function in a system adapted for elevated temperatures. In this article, Anfinsen, et al, reported that they had purified to homogeneity the alpha-amylase, an enzyme that degrades starch, from the hyperthermophilic archaebacterium Pyrococcus furiosus. Due to the large amount of data available on alpha-amylase, Anfinsen believed that the enzyme was a "favorable" choice for the comparison of mesophilic, or optimal temperature-loving, and Thermophilic enzymes.
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