Purification and properties of a hyperthermoactive ?-amylase from the archaeobacterium Pyrococcus woesei
- 1 June 1991
- journal article
- Published by Springer Nature in Archiv für Mikrobiologie
- Vol. 155 (6), 572-578
- https://doi.org/10.1007/bf00245352
Abstract
No abstract availableKeywords
This publication has 16 references indexed in Scilit:
- Extremely thermostable amylolytic enzyme from the archaebacterium Pyrococcus furiosusFEMS Microbiology Letters, 1990
- Purification and characterization of an alpha-glucosidase from a hyperthermophilic archaebacterium, Pyrococcus furiosus, exhibiting a temperature optimum of 105 to 115 degrees CJournal of Bacteriology, 1990
- Physiology and enzymology of thermophilic anaerobic bacteria degrading starchFEMS Microbiology Letters, 1990
- A novel group of abyssal methanogenic archaebacteria (Methanopyrus) growing at 110 °CNature, 1989
- Purification and some properties of the extracellular α-amylase-pullulanase produced by Clostridium thermohydrosulfuricumBiochemical Journal, 1988
- Pyrobaculum gen. nov., a new genus of neutrophilic, rod-shaped archaebacteria from continental solfataras growing optimally at 100 CArchiv für Mikrobiologie, 1987
- Pyrococcus furiosus sp. nov. represents a novel genus of marine heterotrophic archaebacteria growing optimally at 100 CArchiv für Mikrobiologie, 1986
- Complete Nucleotide Sequence of a Thermophilic α-Amylase Gene: Homology between Prokaryotic and Eukaryotic α-Amylases at the Active Sites1The Journal of Biochemistry, 1985
- Simplified method for silver staining of proteins in polyacrylamide gels and the mechanism of silver stainingElectrophoresis, 1985
- Dinitrogen fixation by a thermophilic methanogenic bacteriumNature, 1984