Heparinase Ⅲ (HepC) is an important polysaceharide lyase

which plays a vital role in the development of anticancer drugs

production of low molecular weight heparin(LMWH)and quality control of the heparins. The main bottlenecks of HepC application are high production cost

poor level of heterologous recombinant expression as well as lack of efficient expression system. Based on the previous experience

the codon optimization of HepC gene (the optimized gene product named as coHepC) and E.coli expression system by constructing the MBP-coHepC fusion protein were studied. Combining with further optimization of the culture conditions

the soluble expression ratio of the fusion protein was significantly increased and the total enzyme activity in the shake-flask culture reached 7603.46 IU·L-1. At the same time

the possible reasons for the HepC improved expression were analyzed at transcription and translation levels of HepC gene. These studies provided the basis for applications of heparinase Ⅲ.