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Construction of mutant heparinase I with significantly increased specific activity.
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  • Anna Kalinina,
  • Larisa Borshchevskaya,
  • Elena Patrusheva,
  • Tatiana Gordeeva,
  • Sergey Sineoky
Anna Kalinina
NRC "Kurchatov Institute"
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Larisa Borshchevskaya
NRC "Kurchatov Institute"
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Elena Patrusheva
NRC "Kurchatov Institute"
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Tatiana Gordeeva
NRC "Kurchatov Institute" – GosNIIgenetika, Genomic Center
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Sergey Sineoky
NRC "Kurchatov Institute"
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Abstract

The cleavage of heparin by heparin lyases showed great potential as a cost-effective and innoxious method for producing heparin with low molecular weight (LMWH). One of the most studied and sought heparin lyase is heparinase I (HepI). However, the industrial use of HepI was largely hampered by its low specific activity and thermal stability. In this article we describe increasing in specific heparinase I activity by stepwise site-directed mutagenesis. Thus after two cycles of mutagenesis, we obtained mutant heparinase I Flavobacterium heparinum with significantly increased specific activity (25%).

Peer review status:POSTED

06 Apr 2020Submitted to Biotechnology and Bioengineering
21 Apr 2020Assigned to Editor
21 Apr 2020Submission Checks Completed