An alkaline and metallo-protein type endo xylanase from Streptomyces sp. CSWu-1

An alkaline xylanase (XynWu-1) from Streptomyces sp. CSWu-1 was isolated from the Korean soil sample, purified and biochemically characterized. The extracellular xylanase was purified 4.8 fold with a 16% yield using Sephadex G-50 followed by DEAE-Sepharose (fast flow) column chromatography. The molecular mass of the enzyme was approximately 37 kDa estimated by SDS-PAGE and xylan zymography. N-terminal amino acid sequence of XynWu-1 was AINVLVAALX. The enzyme was found to be stable in a broad range of pH (7.0 ∼ 13.0) and to 50°C and have an optimal pH and temperature of 11.0 and 60°C, respectively. XynWu-1 activity was found to be affected by Mn²⁺ ion with highest activity at 6 mM and produced xylose, xylobiose, and xylotetraose as major hydrolyzed end products. It was found to degrade agro waste materials like corncob and wheat bran by XynWu-1 (2,000 U/g) as shown by electron microscopy. As being stable in extreme alkaline pH, diverse peculiar biochemical characteristics, and ability to produce oligosaccharide shows that XynWu-1 has potential application in various bioindustries like probiotics, ethanol, etc.