Characterization of a novel multi-domain xylanase from Clostridium clariflavum with application in hydrolysis of corn cobs

  • Yulu Liu
  • Yawu Sun
  • Huaguang Wang
  • Lei TangEmail author
Original Research Paper



To develop a novel multi-catalytic domain (CD) xylanase Xyn2083 from Clostridium clariflavum by expression of its truncated forms in Escherichia coli and cooperation of xylanase with cellulase in the hydrolysis of waste lignocellulosic resources.


Xyn2083 has two glycoside hydrolase family (GH) domains GH11 and GH10. These two catalytic domains functioned synergistically in xylan hydrolysis. The recombinant protein with GH11 domain, Xyn2083GH11, had the highest xylanase activity among three constructed truncated forms. The deletion of N-terminal extra amino acid residues of Xyn2083GH11 decreased catalytic activity as well as the stability of the enzyme. The hydrolysis rates of cellulose and xylan in the pretreated corn cobs were 90.56% and 72.80% with the addition of Xyn2083GH11 and cellulase, whereas those were 67.95% and 34.45% using sole cellulase respectively. The structural analysis of substrates indicated that the addition of Xyn2083GH11 led to a looser structure and more exposure of crystal cellulose for cellulase to approach.


Since the native multi-CDs’ xylanases are rare, the thermostable Xyn2083 provides a good source for functional studies of two CDs coexisted in one xylanase and for potential applications after modification.


Clostridium clariflavum Corn cobs Xylan Xylanase 



This work was supported by the Program of Introducing Talents of Discipline to Universities (111-2-06), the National First-class Discipline Program of Light Industry Technology and Engineering (LITE2018-27), and Top-notch Academic Programs Project of Jiangsu Higher Education Institutions (PPZY2015A056).

Compliance with ethical standards

Conflict of interest

The authors declare that they have no conflict of interest.

Supplementary material

10529_2019_2721_MOESM1_ESM.docx (40 kb)
Supplementary Table 1—Primers used for amplification of the genes of Xyn2083 derivatives. Supplementary Fig. 1—Xyn2083GH11and its truncated forms. Supplementary material 1 (DOCX 40 kb)


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Copyright information

© Springer Nature B.V. 2019

Authors and Affiliations

  1. 1.Key Laboratory of Industrial Biotechnology, Ministry of EducationJiangnan UniversityWuxiChina
  2. 2.School of BiotechnologyJiangnan UniversityWuxiChina

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