Biochemical characterization of a noble xylanase from Paenibacillus sp. EC116

Min Soo Kim, Mi Hee Woo, Young Hyo Chang, Namhyun Chung, Joong Su Kim

Research output: Contribution to journalArticlepeer-review

5 Citations (Scopus)


In our present study, a new Endo-1,4-β-xylanase (EC was isolated, which belongs to glycosyl hydrolase family 10 member. The new enzyme designated as xynA was expressed for biochemical characterization. The xynA xylanase was identified in Paenibacillus sp. EC116. The novel gene had the size of 2673 base pairs, which correspond to 891 amino acid residues. The expressed enzyme has a size of ~100 kDa. The amino acid sequence was similar to that of endo-1,4-beta-xylanase from Paenibacillus sp. FSL R5-192 (ETT36211.1) (96 % identical). The xylanase has an optimal temperature of 40 °C and the pH optimum of 6.0. The specific activity of the xylanase toward birchwood xylan was about 0.69 μmol min−1 mg−1, the Vmax value of 1.639 μmol mg−1 min−1, and the Km value of 35.1 mg ml−1. The EC116 xylanase was relatively stable up to 60 °C. Xylanase enzymes have numerous industrial applications, which need to meet the specific requirements for each application. We hope that our EC116 xylanase is one of the candidates for commercial applications.

Original languageEnglish
Pages (from-to)313-320
Number of pages8
JournalApplied Biological Chemistry
Issue number2
Publication statusPublished - 2016 Apr 1

Bibliographical note

Funding Information:
This work was supported by grants from the KRIBB Initiative Program and the Korean Ministry of Education, Science, and Technology (grant number NRF-2011-0023196).

Publisher Copyright:
© 2016, The Korean Society for Applied Biological Chemistry.


  • Glycosyl hydrolase family 10
  • Paenibacillus sp
  • Saccharification
  • Xylanase
  • Β-glucosidase

ASJC Scopus subject areas

  • General Biochemistry,Genetics and Molecular Biology
  • Organic Chemistry


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