ArticleWorld journal of microbiology & biotechnology2012
Cloning, purification and characterization of an alkali-stable endoxylanase from thermophilic Geobacillus sp. 71.
Article in World journal of microbiology & biotechnology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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9 citing papers in PubMed, 28 citations in OpenAlex.
- Expression, Characterization and Its Deinking Potential of a Thermostable Xylanase FromFrontiers in bioengineering and biotechnology · 2021Article
- Article
- Biochemical characterization of the xylan hydrolysis profile of the extracellular endo-xylanase from Geobacillus thermodenitrificans T12.BMC biotechnology · 2017Article
- Hyperthermostable Thermotoga maritima xylanase XYN10B shows high activity at high temperatures in the presence of biomass-dissolving hydrophilic ionic liquids.Extremophiles : life under extreme conditions · 2016Article
- Complete genome sequence, metabolic model construction and phenotypic characterization of Geobacillus LC300, an extremely thermophilic, fast growing, xylose-utilizing bacterium.Metabolic engineering · 2015Article
- Properties of an alkali-thermo stable xylanase from Geobacillus thermodenitrificans A333 and applicability in xylooligosaccharides generation.World journal of microbiology & biotechnology · 2015Article
- Comparative analysis of the Geobacillus hemicellulose utilization locus reveals a highly variable target for improved hemicellulolysis.BMC genomics · 2014Article
- Characterization and constitutive expression of an acidic mesophilic endo-1,4-β-D-xylanohydrolase with high thermotolerance and catalytic efficiency in Pichia pastoris.World journal of microbiology & biotechnology · 2013Article
- Characteristics of thermostable endoxylanase and β-xylosidase of the extremely thermophilic bacterium Geobacillus thermodenitrificans TSAA1 and its applicability in generating xylooligosaccharides and xylose from agro-residues.Extremophiles : life under extreme conditions · 2013Article
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8 authors at 1 institution in 1 country.
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Abstract
The gene encoding a xylanase from Geobacillus sp. 71 was isolated, cloned, and sequenced. Purification of the Geobacillus sp 7.1 xylanase, XyzGeo71, following overexpression in E. coli produced an enzyme of 47 kDa with an optimum temperature of 75°C. The optimum pH of the enzyme is 8.0, but it is active over a broad pH range. This protein showed the highest sequence identity (93%) with the xylanase from Geobacillus thermodenitrificans NG80-2. XyzGeo71 contains a catalytic domain that belongs to the glycoside hydrolase family 10 (GH10). XyzGeo71 exhibited good pH stability, remaining stable after treatment with buffers ranging from pH 7.0 to 11.0 for 6 h. Its activity was partially inhibited by Al(3+) and Cu(2+) but strongly inhibited by Hg(2+). The enzyme follows Michaelis-Menten kinetics, with K(m) and V(max) values of 0.425 mg xylan/ml and 500 μmol/min.mg, respectively. The enzyme was free from cellulase activity and degraded xylan in an endo fashion. The action of the enzyme on oat spelt xylan produced xylobiose and xylotetrose.
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