Purification and some properties of an alkaline xylanase from alkaliphilic Bacillus sp. strain 41M-1.
1993
Nakamura S. | Wakabayashi K. | Nakai R. | Aono R. | Horikoshi K.
An alkaliphilic Bacillus sp. strain, 41M-1, isolated from soil produced multiple xylanases extracellularly. One of these xylanases was purified to homogeneity by ammonium sulfate fractionation and anion-exchange chromatography. The molecular mass of this enzyme (xylanase J) was 36 kDa, and the isoelectric point was pH 5.3. Xylanase J was most active at pH 9.0. The optimum temperature for the activity at pH 9.0 was around 50 degrees C. The enzyme was stable up to 55 degrees C at pH 9.0 for 30 min. Xylanase J was completely inhibited by the Hg2+ ion and N-bromosuccinimide. The predominant products of xylan hydrolysate were xylobiose, xylotriose, and higher oligosaccharides, indicating that the enzyme was an endoxylanase. The apparent Km and Vmax values on xylan were 3.3 mg/ml and 1,100 micromole min-1 mg-1, respectively. Xylanase J showed high sequence homology with the xylanases from Bacillus pumilus and Clostridium acetobutylicum in the N-terminal region. Xylanase J acted on neither crystalline cellulose nor carboxymethyl cellulose, indicating a possible application of the enzyme in biobleaching processes.
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