Biochemical confirmation and characterization of the family-57-like alpha-amylase of Methanococcus jannaschii.
The gene encoding a family-57-like alpha-amylase in the hyperthermophilic archaeon Methanococcus jannaschii, has been cloned into Escherichia coli. Extremely thermoactive alpha-amylase was confirmed in partially purified enzyme solution of the recombinant culture. This enzyme activity had a temperature optimum of 120 degrees C and a pH optimum 5.0-8.0. The amylase activity is extremely stable against denaturants. Hydrolysis of large sugar polymers with alpha-1-6 and alpha-1-4 linkages yields products including glucose polymers of 1-7 units. Highest activity is exhibited on amylose. The catalyst exhibited a half-life of 50 h at 100 degrees C, among the highest reported thermostabilities of natural amylases.
Kim
J W
JW
Department of Chemical and Biochemical Engineering, University of Iowa, Iowa City, Iowa 52242, USA.
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Whiteley
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D000595:Amino Acid Sequence; D000688:Amylose / Q000378:metabolism; D050260:Carbohydrate Metabolism; D003001:Cloning, Molecular; D004926:Escherichia coli / Q000378:metabolism; D005936:Glucans / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D017017:Methanococcus / Q000201:enzymology* / Q000235:genetics*; D008969:Molecular Sequence Data; D011994:Recombinant Proteins / Q000378:metabolism; D016415:Sequence Alignment; D013696:Temperature; D000516:alpha-Amylases / Q000096:biosynthesis / Q000235:genetics* / Q000378:metabolism
D005936:Glucans; D011994:Recombinant Proteins; D000688:Amylose; D000516:alpha-Amylases