Specificity of Purified Xylanase from Alkaliphilic Bacillus halodurans Strain C-1 on Hydrolysis of Soluble Xylans
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Abstract
An extracellular xylanase from alkaliphilic Bacillus halodurans strain C-1 was purified to homogeneity, asdemonstrated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and active-PAGE, bymeans of ammonium sulfate precipitation, DEAE-Toyopearl column, and DEAE-HiPrep FF 16/10 and Mono-QHR 5/5 fast performance liquid chromatographies. The molecular weight of the purified xylanase was estimatedto be about 47 kDa. The hydrolysis rate of soluble birchwood xylan by the purified enzyme was higher than thoseof soluble oat spelt and larchwood xylans. The Km value of the enzyme is 1.63, 1.83 and 2.76 mg/ml, againstsoluble birchwood, oat spelt and larchwood xylans, respectively, while the Vmax value of the enzyme is 0.175, 0.150and 0.125 mMmin-1/mg, respectively. The Vmax/Km ratio of xylanase on soluble birchwood xylan was approximately1.3 and 2.4 fold higher than those of soluble oat spelt and larchwood xylans, respectively.
Keywords : Alkaliphilic Bacillus halodurans strain C-1 / Purified xylanase /Specificity of xylanase / Soluble xylan