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Molecular Biotechnology

, Volume 61, Issue 10, pp 791–800 | Cite as

Cloning and Characterization of a Chondroitin AC Exolyase from Arthrobacter sp. SD-04

  • Lu-Zhou Chen
  • Chu-Qi Shi
  • Feng-Xin Yin
  • Feng-Shan Wang
  • Ju-Zheng ShengEmail author
Original paper
  • 34 Downloads

Abstract

Glycosaminoglycans (GAGs) and their low-molecular weight derivates have received considerable interest in terms of their potential clinical applications, and display a wide variety of pharmacological and pharmacokinetic properties. Structurally distinct GAG chains can be prepared by enzymatic depolymerization. A variety of bacterial chondroitin sulfate (CS) lyases have been identified, and have been widely used as catalysts in this process. Here, we identified a putative chondroitin AC exolyase gene, AschnAC, from an Arthrobacter sp. strain found in a CS manufacturing workshop. We expressed the enzyme, AsChnAC, recombinantly in Escherichia coli, then purified and characterized it in vitro. The enzyme indeed displayed exolytic cleavage activity toward HA and various CSs. Removing the putative N-terminal secretion signal peptide of AsChnAC improved its expression level in E. coli while maintaining chondroitin AC exolyase activity. This novel catalyst exhibited its optimal activity in the absence of added metal ions. AsChnAC has potential applications in preparation of low-molecular weight GAGs, making it an attractive catalyst for further investigation.

Keywords

Glycosaminoglycan Chondroitin sulfate Chondroitin AC exolyase Arthrobacter sp. Escherichia coli Substrate specificity Enzymatic characterization 

Notes

Funding

Funding was provided by National Natural Science Foundation of China (Grant No. 31770845)

Compliance with Ethical Standards

Conflict of interest

The authors declare that there are no conflicts of interest.

Supplementary material

12033_2019_208_MOESM1_ESM.docx (45 kb)
Supplementary material 1 (DOCX 44 kb)

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Copyright information

© Springer Science+Business Media, LLC, part of Springer Nature 2019

Authors and Affiliations

  1. 1.Key Laboratory of Chemical Biology of Natural Products (Ministry of Education), Institute of Biochemical and Biotechnological Drug, School of Pharmaceutical SciencesShandong UniversityJinanChina
  2. 2.National Glycoengineering Research CenterShandong UniversityJinanChina

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