AUTHOREA
Log in
Sign Up
Browse Preprints
LOG IN
SIGN UP
Essential Site Maintenance
: Authorea-powered sites will be updated circa 15:00-17:00 Eastern on Tuesday 5 November.
There should be no interruption to normal services, but please contact us at
[email protected]
in case you face any issues.
Larisa Borshchevskaya
Public Documents
1
Construction of mutant heparinase I with significantly increased specific activity.
Anna Kalinina
and 4 more
April 21, 2020
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%).