Protein Disulfide Isomerase （PDI）， a member of the thioredoxin superfamily， is an oxidoreductase widely exists in animals， plants and microorganisms. In plants， the formation and isomerization of protein disulfide bonds， which are mainly catalyzed by disulfide bond proteins， are crucial in the correct assembly and folding of proteins. In this study， based on the sequence similarity to the PDI gene family in Arabidopsis thaliana， 21 PDI genes were identified and found on nine chromosomes of maize. The phylogenetic tree analysis showed that the maize PDI gene family members were divided into four evolutionary branches and 11 developmental groups， and within each group the gene structure and conserved motifs were similar. The analysis of cis-acting elements in the promoters identified cis-acting elements associating to stress， plant hormones and endosperm specific expression. By quantifying the transcriptional profiles， the high expression was detected in embryo， endosperm and grain. In endosperm， a downward trend followed by upward from 10 to 20 days after pollination was observed. Biodiversity analysis revealed that was diversity of ZmPDIL1-1 gene. The result of subcellular localization showed that ZmPDIL1-1 was located to the endoplasmic reticulum. Collectively， this study provided reference for the functional analysis of PDI gene family in maize.