Journal
CARBOHYDRATE POLYMERS
Volume 295, Issue -, Pages -Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.carbpol.2022.119825
Keywords
Heparanase Bp; Heparinase III; Low molecular weight heparin; Enzymatic synthesis; Anticoagulant activity
Categories
Funding
- GlycoMIP a National Science Founda- tion Materials Innovation Platform [DMR-1933525]
- Key Research and Development Program of Zhejiang [2021C03084]
- High -Level Talent Special Support Plan of Zhejiang Province [2019R52009]
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In this study, two LMWHs were enzymatically synthesized, and it was found that HepBp can be used to prepare a new type of LMWH with high anticoagulant activity.
Low-molecular-weight heparin (LMWH) is prepared from the controlled chemical or enzymatic depolymerization of animal sourced heparins. It has been widely used as an anticoagulant. Concerns about the shortcomings of animal-derived heparin and the contamination of supply chain demand biochemical approaches for synthesizing LMWH. In the present study, two LMWHs were enzymatically synthesized from low molecular weight N-sulfated heparosan (LMW-NSH) cleaved by recombinant hydrolase, endo-beta-glucuronidase, (HepBp) or heparin lyase III (HepIII), followed by subsequent sulfotransferase modifications. Structural characterization shows that LMWH chains prepared using HepBp had a saturated uronic acid residue at their reducing ends, while chains of LMWH prepared using HepIII had an unsaturated uronic acid residue at their non-reducing end. Both LMWHs had antifactor Xa and anti-factor IIa activities comparable to enoxaparin. This approach demonstrates that the hydrolase, HepBp, can be used to prepare a new type of LMWH that has no unsaturated uronic acid at its non-reducing end.
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