Objectives:The use of endo-arabinanase from Bacillus licheniformis (ABNase) for sugarcane saccharification has been evaluated by enzyme immobilization and commercial cocktail supplement with the immobilized heterologous protein.Results:Biochemical characterization of the purified ABNase showed that the catalytic activity was strongly inhibited by 5 mM Cu2+, Zn2+ or Fe3+. The optimum pH and temperature for activity were 5.5–6.5 and 35–40 °C, respectively. The enzyme stability increased 128-fold when immobilized with glyoxyl agarose, and the hydrolysis of pretreated sugar cane biomass increased by 15 % when a commercial enzyme cocktail was supplemented with immobilized ABNase.Conclusion:Pectin hydrolysis by recombinant ABNase plays a role in the effective application of enzymatic cocktails for biomass saccharification.