Purification and characterization of extremely thermostable beta-mannanase, beta-mannosidase, and alpha-galactosidase from the hyperthermophilic eubacterium Thermotoga neapolitana 5068

Article Abstract:

The hyperthermophilic eubacterium Thermotoga neapolitana 5068 produces the extremely thermostable and thermoactive beta-mannanase, beta-mannosidase and alpha-galactosidase. Beta-mannanase is a 65 kDa extracellular monomeric enzyme, with an optimum temperature of 90-92 degree celsius (C). Beta-mannosidase is a 100 kDa homodimer, with 87 degree C optimal temperature for activity. Alpha-galactosidase is a 61 kDa monomeric enzyme, with an optimum temperature of 100-103 degree C. The enzymes hydrolyze galactomannans to form monosaccharides that provide nutrition to T. neapolitana.

Physiological aspects, Bacteria, Thermophilic, Microbial enzymes, Thermophiles

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Functional-genomics-based identification and characterization of open reading frames encoding [alpha]-glucoside-processing enzymes in the hyperthermophilic archaeon Pyrococcus furiosus

Article Abstract:

Bioinformatics analysis and transcriptional response information for Pyrococcus furiosus grown on [alpha]-glucans have identified a novel isomaltase (PF0132). This has represented a new glycoside hydrolase (GH) family, a novel GH57 [beta]-amylase (PF0870), and an extracellular starch-binding protein (1,141 amino acids), in addition to many other putative [alpha]-glucan-processing enzymes.

Science & research, Enzymes, Genetic transcription, Transcription (Genetics), Glycogen, Protein binding, Nutritional aspects, Computational biology, Hydrolases, Chemical properties

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Responses of wild-type and resistant strains of the hyperthermophilic bacterium Thermotoga maritima to chloramphenicol challenge

Article Abstract:

The responses of wild type and resistant strains of hyperthermophilic bacterium Thermotoga maritima to chloramphenicol were investigated. The response of the wild-type was similar to that of mesophilic bacteria, the mutant showed reduced susceptibility attributed to five mutations in 23S rRNA and phenotypic preconditioning to chloramphenicol.

Analysis, Gene mutations, Gene mutation, Ribosomal RNA, Chloramphenicol

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