ArticleJournal of industrial microbiology & biotechnology2007
Purification and characterization of two sugarcane bagasse-absorbable thermophilic xylanases from the mesophilic Cellulomonas flavigena.
Article in Journal of industrial microbiology & biotechnology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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8 citing papers in PubMed, 26 citations in OpenAlex.
- Isolation and Characterization of Thermophilic Bacteria from a Hot Spring in the State of Hidalgo, Mexico, and Geochemical Analysis of the Thermal Water.Microorganisms · 2024Article
- pCold-assisted expression of a thermostable xylanase from3 Biotech · 2022Article
- Optimization of bioprocesses with Brewers' spent grain andEngineering in life sciences · 2022Article
- Complete Genome Sequence of Cellulomonas sp. JZ18, a Root Endophytic Bacterium Isolated from the Perennial Desert Tussock-Grass Panicum turgidum.Current microbiology · 2021Article
- Xylanases of Cellulomonas flavigena: expression, biochemical characterization, and biotechnological potential.AMB Express · 2017Article
- Microbial xylanases and their industrial application in pulp and paper biobleaching: a review.3 Biotech · 2017Article
- Draft genome sequence of Cellulomonas carbonis T26(T) and comparative analysis of six Cellulomonas genomes.Standards in genomic sciences · 2015Article
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4 authors at 1 institution in 1 country.
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Abstract
We report the purification and characterization of two thermophilic xylanases from the mesophilic bacteria Cellulomonas flavigena grown on sugarcane bagasse (SCB) as the only carbon source. Extracellular xylanase activity produced by C. flavigena was found both free in the culture supernatant and associated with residual SCB. To identify some of the molecules responsible for the xylanase activity in the substrate-bound fraction, residual SCB was treated with 3 M guanidine hydrochloride and then with 6 M urea. Further analysis of the eluted material led to the identification of two xylanases Xyl36 (36 kDa) and Xyl53 (53 kDa). The pI for Xyl36 was 5.0, while the pI for Xyl53 was 4.5. Xyl36 had a Km value of 1.95 mg/ml, while Xyl53 had a Km value of 0.78 mg/ml. In addition to SCB, Xyl36 and Xyl53 were also able to bind to insoluble oat spelt xylan and Avicel, as shown by substrate-binding assays. Xyl36 and Xyl53 showed optimal activity at pH 6.5, and at optimal temperature 65 and 55 degrees C, respectively. Xyl36 and Xyl53 retained 24 and 35%, respectively, of their original activity after 8 h of incubation at their optimal temperature. As far as we know, this is the first study on the thermostability properties of purified xylanases from microorganisms belonging to the genus Cellulomonas.
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