A chitosanase from Paecilomyces lilacinus with binding affinity for specific chito-oligosaccharides

Yi Yun Chen, Chih Yu Cheng, Te Lin Haung, Yaw-Kuen Li*

*Corresponding author for this work

Research output: Contribution to journalArticle

6 Scopus citations


A purple-spore, rhizosphere-inhabiting nematophagous fungus, further identified as Paecilomyces lilacinus, was found to grow on chitosanase-detecting plate. An induced endochitosanase having a molecular mass of 23 kDa was purified from the culture medium by a single cation-exchange column-chromatography step. Its optimum pH, optimum temperature and pI were found to be 6.0, 50 °C and 8.3 respectively. The N-terminal amino acid sequence of the purified enzyme was partially determined. On the basis of the partial sequence XQLPANLXXIYD and the BLAST results, the purified chitosanase was classified as a new member of the family 75 glycohydrolases. Complete hydrolysis of 95% deacetylated chitosan by the isolated chitosanase released chitotriose, chitotetraose and chitopentaose as the major hydrolytic products. Two oligosaccharides, which were further determined to be GlcN-GlcN-GlcNAc and GlcNAc-GlcN-GlcN-GlcNAc by chemical methylation followed by liquid chromatography-tandem MS analysis, were obtained after the denaturation of the purified chito-sanase. This is the first documented finding that chitosanase can be produced in a Paecilomyces strain and that it has binding affinity for specific N-acetylated oligosaccharides.

Original languageEnglish
Pages (from-to)145-150
Number of pages6
JournalBiotechnology and Applied Biochemistry
Issue number2
StatePublished - 1 Apr 2005


  • Chitooligosaccharide
  • Chitosanase
  • Family 75 glycohydrolase
  • Paecilomyces lilacinus
  • Tandem MS analysis

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