Abstract: Endoglucanases are the main cellulolytic enzymes in the gut of Anoplophora glabripennis.In this study,random peptide phage display technology was employed to screen peptides that bound the AgEG2,a member of endoglucanase isozymes.Phage clones displaying peptide TPHRSPL accounted for 33.7% of the selected phage population after three rounds of screening,and showed higher phage recovery than the other clones in the binding assay.Peptide TPHRSPL was chemically synthesized and tested for its binding activity to AgEG2.The synthetic peptide exhibited high binding specificity for AgEG1 and AgEG2.This indicated that peptide TPHRSPL had the affinity to the endoglucanase of A.glabripenni,which could be used to study the biological role of the enzyme in the gut,and had the potential to be developed into biological control agents of A.glabripenni.