Marine Drugs (Aug 2024)

Identification and Characterization of a Highly Active Hyaluronan Lyase from <em>Enterobacter asburiae</em>

  • Linjing Zhang,
  • Jiayu Jiang,
  • Wei Liu,
  • Lianlong Wang,
  • Zhiyuan Yao,
  • Heng Li,
  • Jinsong Gong,
  • Chuanli Kang,
  • Lei Liu,
  • Zhenghong Xu,
  • Jinsong Shi

DOI
https://doi.org/10.3390/md22090399
Journal volume & issue
Vol. 22, no. 9
p. 399

Abstract

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Hyaluronic acid (HA) is a well-known functional marine polysaccharide. The utilization and derivative development of HA are of great interest. Hyaluronan lyase has wide application prospects in the production of HA oligosaccharides and lower molecular weight HA. In this study, a strain of Enterobacter asburiae CGJ001 with high hyaluronan lyase activity was screened from industrial wastewater. This strain exhibited an impressive enzyme activity of 40,576 U/mL after being incubated for 14 h. Whole genome sequencing analysis revealed that E. asburiae CGJ001 contained a cluster of genes involved in HA degradation, transport, and metabolism. A newly identified enzyme responsible for glycosaminoglycan degradation was designated as HylEP0006. A strain of E. coli BL21(DE3)/pET-22b(+)-hylEP0006 was successfully constructed. HylEP0006 exhibited optimal degradation at 40 °C and pH 7.0, showing a high activity of 950,168.3 U/mg. HylEP0006 showed specific activity against HA. The minimum degradation fragment of HylEP0006 was hyaluronan tetrasaccharides, and HylEP0006 could efficiently degrade HA into unsaturated disaccharides (HA2), with HA2 as the final product. These characteristics indicate that HylEP0006 has a potential application prospect for the extraction and utilization of hyaluronic acid.

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