Pullulanase type I from Fervidobacterium pennavorans Ven5: cloning, sequencing, and expression of the gene and biochemical characterization of the recombinant enzyme

Article Abstract:

The pullulanase type I gene from Fervidobacterium pennavorans Ven5 was cloned and sequenced in Escherichia coli. The pulA gene had 50.1% pairwise amino acid identity with pulA from Thermotoga maritima and contained the four regions conserved among all amylolytic enzymes. It encodes a protein of 849 amino acids with a 28-residue signal peptide. Results classify the enzyme as a debranching enzyme, pullulanase type I, and is a good candidate for biotechnological applications in starch processing owing to its unusually high substrate specificity of the recombinant purified pullulanase and its thermal stability.

Research, Enzymes, Recombinant proteins, Enzyme structure-activity relationships

---

Keratin degradation by Fervidobacterium pennavorans, a novel thermophilic anaerobic species of the order Thermotogales

Article Abstract:

The thermophilic bacterium Fervidobacterium pennavorans contains a cell-bound keratinolytic enzyme system which can degrade feathers at high temperatures. The bacterium was collected from a hot spring in the Azores islands. It belongs to the order Thermotogales. The enzyme is a serine protease with a molecular mass of 130 kilo Dalton and an isoelectric point of 3.8. The optimal temperature and pH for its catalytic activity are 80 degrees celsius and 10.0, respectively. This is the only known extremophilic microorganism that can degrade native feather.

Anaerobic bacteria, Keratin

---

Purification and properties of a thermostable pullulanase from a newly isolated thermophilic anaerobic bacterium, Fervidobacterium pennavorans Ven5

Article Abstract:

Thermostable type I pullulanase was purified from Fervidobacterium pennavorans which was isolated from water and mud samples of a thermal spa in Italy. The specific branching enzyme of Fervidobacterium pennavorans produces maltotriose when incubated with pullulan and attacks the alpha-1,6 linkages of branched polysaccharides. Furthermore, the maximum activity of pullunase ranges from pH 5.5 to 6.0 at 85 degrees centigrade.

Analysis, Microbial enzymes, Enzyme kinetics

Similar abstracts:

• Abstracts: xylA cloning and sequencing and biochemical characterization of xylose isomerase from Thermotoga neapolitana. Cloning, sequencing, and expression of the gene encoding extracellular alpha-amylase from Pyrococcus furiosus and biochemical characterization of the recombinant enzyme
• Abstracts: Cloning, sequencing, and expression of genes encoding phosphotransacetylase and Acetate kinase from Clostridium acetobutylicum ATCC 824
• Abstracts: Cross-resistance of the diamondback moth indicates altered interactions with domain II of Bacillus thuringiensis toxins. part 2
• Abstracts: Effect of pasteurization on infectivity of Cryptosporidium parvum oocysts in water and milk. In vitro interactions of Asian freshwater clam (Corbicula fluminea) hemocytes and Cryptosporidium parvum oocysts

This website is not affiliated with document authors or copyright owners. This page is provided for informational purposes only. Unintentional errors are possible.