Abstract:Pullulanase is able to exclusively cleave the α-1，6-glycosidic bond in the branch point of branched starch.This characteristic makes pullulanase a crucial enzyme preparation in the starch sugar industry to play a vital role in enhancing quality and efficiency of the starch deep-processing sector.Carbohydrate-binding modules （CBM） are non-catalytic domains widely present in glycoside hydrolases.This domain plays a crucial role in the substrate specificity of glycoside hydrolases，stability of the enzyme structure，and substrate-binding capacity.Therefore，studying the CBM of pullulanase is crucial for its performance modification and optimization.The research progress in the CBM of pullulanase was reviewed，and the effects of different CBM on the physicochemical properties of pullulanase were summarized.In addition，the research progress in key amino acid mutation and modification of the CBM of pullulanase was reviewed.Finally，the future research trends were prospected.The aim was to provide reference for the study and application of pullulanase.