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Literature summary for 4.2.2.7 extracted from

  • Yang, B.; Zhang, C.; Wang, C.; Zhou, H.; Li, Z.; Song, Y.; Zhang, T.; Luo, X.
    Soluble expression and purification of heparinase I in Escherichia coli using a hexahistidine-tagged small ubiquitin-like modifier as a fusion partner (2017), Biotechnol. Biotechnol. Equip., 31, 1040-1045 .
No PubMed abstract available

Application

Application Comment Organism
synthesis expression in Escherichia coli using a hexahistidine-tagged small ubiquitin-like modifier. The fusion protein exhibits high enzyme activity without requirements of in vitro refolding and SUMO-tag releasing process, and the optimum enzyme activity is obtained at 30°C, pH 7.0 and 10 mmol/l Ca2+ in the reaction buffer Pedobacter heparinus

Organism

Organism UniProt Comment Textmining
Pedobacter heparinus
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