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• W1575247003 startingPage "2311" @default.
• W1575247003 abstract "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 moleculr 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 micromol-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." @default.
• W1575247003 created "2016-06-24" @default.
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• W1575247003 date "1993-07-01" @default.
• W1575247003 modified "2023-10-16" @default.
• W1575247003 title "Purification and some properties of an alkaline xylanase from alkaliphilic Bacillus sp. strain 41M-1" @default.
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• W1575247003 doi "https://doi.org/10.1128/aem.59.7.2311-2316.1993" @default.
• W1575247003 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/182274" @default.
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