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Selected Publication:
Kriegshäuser, G; Liebl, W.
Pullulanase from the hyperthermophilic bacterium Thermotoga maritima: purification by beta-cyclodextrin affinity chromatography.
J Chromatogr B Biomed Sci Appl. 2000; 737(1-2):245-251
Doi: 10.1016/S0378-4347(99)00373-4
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- Leading authors Med Uni Graz
- Kriegshäuser Gernot
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- Abstract:
- This is the first report about the isolation of a type I pullulanase from a hyperthermophilic bacterium, Thermotoga maritima strain MSB8. Purification of the enzyme from a cleared cell-free extract was achieved by anion-exchange chromatography and beta-cyclodextrin affinity chromatography. Using this convenient two-step method we have purified the pullulanase 406-fold with a 26% yield. The purified enzyme displayed maximum pullulan hydrolysis at pH 5.9 and 90 degrees C (15-min assay) and was remarkably resistant against thermoinactivation, having a half-life at 90 degrees C of about 3.5 h. To our knowledge, the T. maritima pullulanase is the most thermostable type I pullulanase known to date. The affinity-based purification protocol described here may be useful for the efficient isolation of other pullulanases.
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- Find related publications in this database (Keywords)
- purification
- Thermotoga maritima
- enzymes
- pullulanase