ArticleWorld journal of microbiology & biotechnology2012
Production of alkaliphilic, halotolerent, thermostable cellulase free xylanase by Bacillus halodurans PPKS-2 using agro waste: single step purification and characterization.
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 6 papers.
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6 citing papers in PubMed.
- An environment-benign approach of bamboo pulp bleaching using extracellular xylanase of strain Bacillus stratosphericus EB-11 isolated from elephant dung.Folia microbiologica · 2023Article
- Role of extremophiles and their extremozymes in biorefinery process of lignocellulose degradation.Extremophiles : life under extreme conditions · 2021Review
- Valorization of untreated rice bran towards bioflocculant using a lignocellulose-degrading strain and its use in microalgal biomass harvest.Biotechnology for biofuels · 2017Article
- Biochemical properties of a new thermo- and solvent-stable xylanase recovered using three phase partitioning from the extract ofBioresources and bioprocessing · 2017Article
- 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
- Function and biotechnology of extremophilic enzymes in low water activity.Aquatic biosystems · 2012Article
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Authors and funding
5 authors.
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Abstract
The alkaliphilic Bacillus halodurans strain PPKS-2 was shown to produce extracellular alkaliphilic, thermostable and halotolerent xylanase. The culture conditions for xylanase production were optimized with respect to pH, temperature, NaCl and inexpensive agro waste as substrates. Xylanase yield was enhanced more than four fold in the presence of 1% corn husk and 0.5% peptone or feather hydrolysate at pH 11 and 37°C. Xylanase was purified to 11.8-fold with 8.7% yield by using traditional chromatographic methods whereas the same enzyme purified to 20-fold with 72% yield by using corn husk as ligand. Its molecular mass was estimated to be 24 kDa by SDS-PAGE. The xylanase had maximal activity at pH 11 and 70°C. The enzyme was active over broad range, 0-20% sodium chloride. The enzyme was thermostable retaining 100% of the original activity at 70°C for 3 h. The apparent K (m) values for oat spelt xylan and brichwood xylan were 4.1 and 4.4 mg/ml respectively. The deduced internal amino acid sequence of PPKS-2 xylanase resembled the sequence of β-1,4-endoxylanase, which is member of glycoside hydrolase family 11.
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