Heparin depolymerization by immobilized heparinase: A review

Int J Biol Macromol. 2017 Jun:99:721-730. doi: 10.1016/j.ijbiomac.2017.03.036. Epub 2017 Mar 11.


Heparin is a member of the glycosaminoglycan (GAG) family composed of glucosamine and uronic acid units containing O-sulfo, N-acetyl and N-sulfo groups, which are alternating in the chain and linked by 1→4 manner. It is a naturally occurring anticoagulant that prevents the formation of clots and their growth within blood. Certain low molecular weight heparins (LMWHs) are considered as better therapeutic agents than natural heparin because of the reduced side effects and smaller risk of bleeding. LMWHs can be produced from heparin by chemical or enzymatic depolymerizations. Heparinases catalyze the cleavage of glycosidic linkage between amino sugars and uronic acids in heparin. There are three kinds of heparinases which are frequently used for depolymerization of heparin. Despite wide range of applications of heparinases in health care, their use still has been hampered due to poor stability and high cost. To overcome this problem heparinases are recommended for immobilization to reduce the cost of product and enhance stability. Heparinases have been successfully immobilized using various methods and supports, mostly for deheparinization of blood through extracorporeal devices. The focus of this review is to present the current status of heparinase immobilization including various supports and methods used, stability and applications.

Keywords: Enzymes; Heparin; Heparinase and glycosaminoglycans; Immobilization; Low molecular weight heparins.

Publication types

  • Review

MeSH terms

  • Animals
  • Delivery of Health Care
  • Enzymes, Immobilized / chemistry*
  • Enzymes, Immobilized / metabolism*
  • Heparin / chemistry*
  • Heparin Lyase / chemistry*
  • Heparin Lyase / metabolism*
  • Humans
  • Molecular Weight
  • Polymerization*


  • Enzymes, Immobilized
  • Heparin
  • Heparin Lyase