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Extremely thermostable amylolytic enzyme from the archaebacterium Pyrococcus furiosus
133
Citations
12
References
1990
Year
Thermoactive EnzymesBiosynthesisEngineeringCellular EnzymologyBiochemistryPeculiar EnzymeBioenergeticsBiocatalysisNatural SciencesEnzyme CatalysisBiotechnologyAerobic BacteriaMicrobial PhysiologyThermostable Amylolytic EnzymeMicrobiologyStructure-function Enzyme KineticsEnzymatic ModificationBiomolecular Engineering
One of the most thermostable and thermoactive enzymes ever described has been characterized from a hyperthermophilic archaebacterium Pyrococcus furiosus. The enzyme system of this bacterium was capable of hydrolyzing starch forming a mixture of various oligosaccharides. Unlike the amylases from aerobic bacteria this enzyme does not require metal ions for activity or stability. The enzyme is catalytically active over a very broad temperature range, namely between 40°C and 140°C. The half life of this peculiar enzyme during autoclaving at 120°C is 2 h.
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