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Efficient Expression and Characterization of an Endo-Type Lyase HCLase_M28 and Its Gradual Scale-Up Fermentation for the Preparation of Chondroitin Sulfate Oligosaccharides

Appl Biochem Biotechnol. 2024-02; 
Ruibao Ju, Baoqin Han, Feng Han, Yanfei Peng
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Codon Optimization … coli, the sequence of HCLase_M28 was codon optimized (HCLase_M28 opt1 ), which was synthesized by GenScript (Nanjing, China) and inserted into plasmid pET-24a ( +) and pET-… Get A Quote

摘要

Glycosaminoglycan (GAG) lyases have been critical in structural and functional studies of GAGs. HCLase_M28, a lyase identified from the genome of Microbacterium sp. M28 was heterologously expressed, enzymatically characterized, and prepared in large-scale fermentation for the production of chondroitin sulfate (CS) oligosaccharides. Results showed that the expression of HCLase_M28 in Escherichia coli BL21 (DE3)-pET24a-HCLase_M28 and Bacillus subtilis W800-pSTOP1622-HCLase_M28 were 108-fold and 25-fold that of wide strain. The optimal lytic reaction of HCLase_M28 happened in 20?mM Tris-HCl (pH 7.2) at 50?°C with a specific activity of 190.9?U/mg toward CS-A. The degrading activity was slightly simulated in pr... More

關(guān)鍵詞

Glycosaminoglycan lyase, Heterologous expression, Large-scale fermentation, Oligosaccharides
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