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Updated: Feb 15, 2026

Chromatographic Purification of Highly Active Yeast Ribosomes
Published on: October 24, 2011
[A highly active GH11 xylanase from Penicillium sp. L1 with potential applications in xylo-oligosaccharide
Xiaoyu Wang1, Weina Liu2, Xiangming Xie1
1College of Biological Sciences and Biotechnology, Beijing Forestry University, Beijing 100083, China.
Abstract:
Xylanase is a high-profile glycoside hydrolase with applications in brewing, feed, pharmacy and bioenergy industries, but most of xylanases are in active below 30 ℃. In order to obtain low temperature active xylanase, a xylanase gene, XYN11A, was cloned from Penicillium sp. L1 and expressed in Pichia pastoris GS115. After purification and enzyme assay, optimal pH and temperature were determined to be 3.5 to 4.0 and 55 ℃. This enzyme was stable at acid and neutral condition (pH 1.0 to 7.0) or under the treatment of 40 ℃ for 1 hour. This xylanase displayed strong resistance to all tested ions and chemicals. Noteworthily, XYN11A maintained a higher activity of 6 700 U/mg than a lot of GH11 xylanase, and demonstrated higher activity (24% to 58%) at lower temperature from 20 to 40 ℃. After beechwood xylan hydrolysis for 16 h, the hydrolysates consisted mainly of xylobiose, xylotriose and xylotetraose and barely of xylose, thus XYN11A could be used for the production of prebiotic xylooligosaccharide. Possessing the features of acidophilic, highly active at lower temperature and oligosaccharide production, XYN11A demonstrated great potential in food and feed industrials.
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