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8173132 
Journal Article 
Purification and characterization of a new thermoalkali-stable xylanase produced from Bacillus amyloliquifaciens NRRL B-14393 by solid-state fermentation of water hyacinth 
Rashad, MM; Mahmoud, AE; Nooman, MU; El-Torky, AEDMM; Keshta, AT; Mahmoud, HA 
2015 
0 
Research Journal of Pharmaceutical, Biological and Chemical Sciences
ISSN: 0975-8585 
6 
6 
467-478 
English 
Purification and characterization of crude xylanase produced by Bacillus amyloliquifaciens NRRL B-14393 grown on water hyacinth under solid-state fermentation were investigated. Xylanase was purified using DEAE-Sepharose and Sephadex G-100 columns which affected specific activity (1009.14 U/mg) and 18.67 purification fold. The pure xylanase has molecular weights of 34.679 and 29 KDa by gel filtration and SDS-polyacrylamide electrophoresis, respectively. The pure xylanase showed a maximal activity at pH 9.5 and 50°C. The enzyme showed a broad range of pH stability (pH 5.5-12). Xylanase retained its full activity up to 40°C for 15 min. It was stable up to 60°C with a thermal denaturing half- life of 90 min. The enzyme exhibited a high specificity for the birch wood xylan substrate. Xylanase had a Km value of 2.94mg ml-1 and Vmax of 10.92 μmole min-1 ml-1.The enzyme was nearly completely inhibited by MnSO4 and HgCl2 at 1 and 10mM concentration. It consisted of 17 amino acids and rich in aspartic acid and tyrosine. These properties make this enzyme a potential candidate for future use in biotechnological applications particularly in the pulp and paper industry as well as large scale production of xylooligosaccharides. 
Bacillus amyloliquifaciens; Characterization; Purification; Solid state fermentation; Water hyacinth; Xylanase