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Biochemical characterization of a novel thermostable ulvan lyase from Tamlana fucoidanivorans CW2-9

J Agric Food Chem. 2024-05; 
Yan Xu, Jin Li, Lu An, Yuankai Qiu, Aihua Mao, Zhixiao He, Jialing Guo, Hanbing Yan, Han Li, Zhong Hu
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Proteins, Expression, Isolation and Analysis The His-tagged recombinant proteins were purified on a Ni column (GenScript) and then analyzed by sodium dodecyl sulfate−polyacrylamide gel electrophoresis (SDSPAGE). Get A Quote

摘要

Ulvan is a complex sulfated polysaccharide extracted from Ulva, and ulvan lyases can degrade ulvan through a β-elimination mechanism to obtain oligosaccharides. In this study, a new ulvan lyase, EPL15085, which belongs to the polysaccharide lyase (PL) 28 family from Tamlana fucoidanivorans CW2-9, was characterized in detail. The optimal pH and salinity are 9.0 and 0.4 M NaCl, respectively. The Km and Vmax of recombinant EPL15085 toward ulvan are 0.80 mg·mL-1 and 11.22 μmol·min -1 mg-1·mL-1, respectively. Unexpectedly, it is very resistant to high temperatures. After treatment at 100 °C, EPL15085 maintained its ability to degrade ulvan. Molecular dynamics simulation analysis and site-directed mutagenesis a... More

关键词

lyase; mutation; thermostability; ulvan.