Two extremely thermostable xylanases of the hyperthermophilic bacterium Thermotoga maritima MSB8

Article Abstract:

XynA and XynB endoxylanases, which are not affected by high temperature or salt concentrations, are formed when the carbon source of Thermotoga martimia MSB8 is xylose or xylan. Though the enzymes are produced by different genes, their structure is similar because antibodies formed against XynA cross-react with XynB. XynB is activated by the addition of NaCl while XynA is most active if NaCl is not present. Both these enzymes hydrolyze polysaccharides but XynB is more active towards low mass substrates.

Microbial enzymes

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dentification and characterization of a novel intracellular alkaline alpha-amylase from the hyperthermophilic bacterium Thermotoga maritima MSB8

Article Abstract:

A study was conducted about the putative intracellular alpha-amylase AmyC from the hyper-thermophilic bacterium Thermotoga maritima that was heterologously over expressed in Escherichia coli and biochemically characterized. The AmyC amino acid sequence shows no similarity to sequences of members of the classical alpha-amylase family GHF 13, instead the five characteristic conserved regions invariably present in GHF 57 proteins are found in AmyC.

Science & research, Escherichia coli, Microbiological chemistry

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Characterization of a tetrameric inositol monophosphatase from the hyperthermophilic bacterium Thermotoga maritima

Article Abstract:

Research was conducted to characterize inositol monophosphatase (I-1-Pase) enzyme of a heat stable bacterium. Analyses of recombinant I-1-Pase show a quaternary structure, a 20-fold higher substrate hydrolysis rate, higher catalytic efficiency, and heat stability.

Enzymes, Phosphatases, Enzyme kinetics, Enzyme structure-activity relationships

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