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The esterase from the thermophilic eubacterium Bacillus acidocaldarius: Structural-functional relationship and comparison with the esterase from the hyperthermophilic archaeon Archaeoglobus fulgidus

โœ Scribed by Sabato D'Auria; Petr Herman; Joseph R. Lakowicz; Fabio Tanfani; Enrico Bertoli; Giuseppe Manco; Mose' Rossi


Publisher
John Wiley and Sons
Year
2000
Tongue
English
Weight
210 KB
Volume
40
Category
Article
ISSN
0887-3585

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The thermophilic esterase from Archaeogl
โœ Sabato D'Auria; Petr Herman; Joseph R. Lakowicz; Enrico Bertoli; Fabio Tanfani; ๐Ÿ“‚ Article ๐Ÿ“… 2000 ๐Ÿ› John Wiley and Sons ๐ŸŒ English โš– 231 KB

The esterase from the hyperthermophilic archaeon Archaeoglobus fulgidus is a monomeric protein with a molecular weight of about 35.5 kDa. The enzyme is barely active at room temperature, displaying the maximal enzyme activity at about 80ยฐC. We have investigated the effect of the temperature on the p