xylA cloning and sequencing and biochemical characterization of xylose isomerase from Thermotoga neapolitana
Article Abstract:
The xylA gene of Thermotoga neapolitana was cloned and expressed in Escherichia coli to study the structure and properties of the enzyme it codes for. Xylose isomerase is most active at 95 degrees centigrade, is stable over a wide range of pH and belongs to the xylose isomerase family II. The thermostability of this enzyme is probably because it has less glutamine and asparagine residues which are denatured at high temperatures. However, the properties of this enzyme are different from those of the enzyme produced by the closely related species Thermotoga maritima.
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1995
User Contributions:
Comment about this article or add new information about this topic:
Thermotoga neapolitana homotetrameric xylose isomerase is expressed as a catalytically active and thermostable dimer in Escherichia coli
Article Abstract:
The cloning, sequencing and expression of Thermotoga neapolitana in Escherichia coli produced a recombinant XI (TNXI) with catalytic properties similar to those of native enzymes. Although tetrameric and dimeric forms were observed from the resulting TNXI, both displayed similar biochemical and physical properties. However, calorimetric results showed that the dimer is more catalytically viable and stable than the tetrameric form.
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1998
User Contributions:
Comment about this article or add new information about this topic:
Cloning, sequencing, and expression of the gene encoding extracellular alpha-amylase from Pyrococcus furiosus and biochemical characterization of the recombinant enzyme
Article Abstract:
Microbiological research shows that the gene encoding the hyperthermophilic extracellular alpha-amylase from the microorganism Pyrococcus furiosus is a single 460-residue polypeptide chain with a 26-residue signal peptide. It has a half-life of 13 hours at 98 degrees centigrade and is more thermostable than the alpha-amylase enzyme from the microorganism Bacillus licheniformis.
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1997
User Contributions:
Comment about this article or add new information about this topic:
- Abstracts: Isolation and characterization of Listeria monocytogenes isolates from ready-to-eat foods in Florida. Functional heterogeneity of RpoS in stress tolerance of enterohemorrhagic Escherichia coli strains
- Abstracts: Purification and characterization of extremely thermostable beta-mannanase, beta-mannosidase, and alpha-galactosidase from the hyperthermophilic eubacterium Thermotoga neapolitana 5068
- Abstracts: Energetic factors and seasonal changes in ovarian function in women from rural Poland. Constraint, pathology and adaptation: how can we tell them apart?
- Abstracts: The genetical and environmental determination of phally polymorphism in the freshwater snail Bulinus truncatus
- Abstracts: Regulatory systems modulating the transcription of the pectinase gens of Erwinia chrysanthemi are conserved in Escherichia coli