title: Topographical and enzymatic characterization of amylases from the extremely thermophilic eubacterium Thermotoga maritima.
abstract: The hyperthermophilic eubacterium Thermotoga maritima uses starch as a substrate, without releasing amylase activity into the culture medium. The enzyme is associated with the 'toga'. Its expression level is too low to allow the isolation of the pure enzyme. Using cycloheptaamylose and acarbose affinity chromatography and common chromatographic procedures, two enzyme fractions are obtained. They differ in specificity, pH-optimum, temperature dependence and stability. Substrate specificity and Ca2+ dependence indicate alpha-, beta- and gluco-amylase activity. Compared with alpha-amylase from Bacillus licheniformis (Tmax = 75 degrees C), the amylases from Thermotoga maritima show exceedingly high thermal stability with an upper temperature limit at 95 degrees C. Significant turnover occurs only between 70 and 100 degrees C, i.e. in the range of viability of the microorganism.
authors.affiliation: Institut für Biophysik und Physikalische Biochemie, Universität Regensburg, Germany.
authors.forename: J
authors.initials: J
authors.lastname: Schumann
authors.forename: A
authors.initials: A
authors.lastname: Wrba
authors.forename: R
authors.initials: R
authors.lastname: Jaenicke
authors.forename: K O
authors.initials: KO
authors.lastname: Stetter
mesh_terms: D000681:Amylases / Q000302:isolation & purification / Q000378:metabolism*; D001407:Bacillus / Q000201:enzymology; D002846:Chromatography, Affinity; D003505:Cyclodextrins / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D006089:Gram-Negative Anaerobic Bacteria / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D013379:Substrate Specificity; D013696:Temperature
chemical_list: D003505:Cyclodextrins; D000681:Amylases