ArticleBrazilian journal of microbiology : [publication of the Brazilian Society for Microbiology]2010
One-step purification and characterization of cellulase-free xylanase produced by alkalophilic Bacillus subtilis ash.
Article in Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology], 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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17 citing papers in PubMed.
- A thermostable GH10 xylanase from Anoxybacteroides tepidamans: structural insights and biochemical characterization.Molecular biology reports · 2026Article
- Exploring black soil microbiota for industrial enzymes: cellulase and xylanase characterization from Bacillus subtilis SSMK413.Microbial cell factories · 2025Article
- Cloning, heterologus expression and characterization of a thermophilic and salt tolerant GH11 xylanase from Allostreptomyces psammosilenae YIM DR4008Antonie van Leeuwenhoek · 2025Article
- Article
- Synthesis, Optimization, and Characterization of Cellulase Enzyme Obtained from ThermotolerantJournal of microbiology and biotechnology · 2024Article
- Shelf-Life Performance of Fish Feed Supplemented with Bioactive Extracts from Fermented Olive Mill and Winery By-Products.Foods (Basel, Switzerland) · 2023Article
- Production and biochemical characterization of partially purified cellulase-free, thermo-acidophilic endoxylanase fromHeliyon · 2022Article
- Cloning, expression, and characterization of a recombinant xylanase from Bacillus sonorensis T6.PloS one · 2022Article
- Characterization of glycoside hydrolase family 11 xylanase from Streptomyces sp. strain J103; its synergetic effect with acetyl xylan esterase and enhancement of enzymatic hydrolysis of lignocellulosic biomass.Microbial cell factories · 2021Article
- Biochemical Characterization of Cellulase FromFrontiers in bioengineering and biotechnology · 2021Article
- Applications of Microbial Enzymes in Food Industry.Food technology and biotechnology · 2018Review
- Article
- Biochemical properties of a new thermo- and solvent-stable xylanase recovered using three phase partitioning from the extract ofBioresources and bioprocessing · 2017Article
- Immobilization of xylanase purified from Bacillus pumilus VLK-1 and its application in enrichment of orange and grape juices.Journal of food science and technology · 2014Article
- Isolation and identification of local Bacillus isolates for xylanase biosynthesis.Iranian journal of microbiology · 2014Article
- Characterization of a new Providencia sp. strain X1 producing multiple xylanases on wheat bran.TheScientificWorldJournal · 2013Article
- Alkaliphilic bacteria: applications in industrial biotechnology.Journal of industrial microbiology & biotechnology · 2011Review
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5 authors.
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Abstract
The present study describes the one-step purification and characterization of an extracellular cellulase-free xylanase from a newly isolated alkalophilic and moderately thermophilic strain of Bacillus subtilis ASH. Xylanase was purified to homogeneity by 10.5-fold with ~43% recovery using ion-exchange chromatography through CM-Sephadex C-50. The purified enzyme revealed a single band on SDS-PAGE gel with a molecular mass of 23 kDa. It showed an optimum pH at 7.0 and was stable over the pH range 6.0-9.0. The optimum temperature for enzyme activity was 55 °C. The purified xylanase did not lose any activity up to 45 ºC, however, it retained 80% and 51% of its activity after pre-incubation at 55 ºC and 60 ºC, respectively. The enzyme obeyed Michaelis-Menton kinetics towards birch wood xylan with apparent Km 3.33 mg/ml and Vmax 100 IU/ml. The enzyme was strongly inhibited by Hg(2+)and Cu(2+)while enhanced by Co(2+) and Mn(2+). The purified enzyme could be stored at 4 ºC for six weeks without any loss of catalytic activity. The faster and economical purification of the cellulase-free xylanase from B. subtilis ASH by one-step procedure together with its appreciable stability at high temperature and alkaline pH makes it potentially effective for industrial applications.
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