Peptides derived from plant sources， particularly those rich in cysteine， have demonstrated the capacity to chelate zinc ions effectively. In order to develop peptide-zinc supplement with high zinc chelation rate and high bioavailability， broaden the application field of pea protein， In this study， the disulfide bond of pea protein isolate was reduced bydithiothreitol， then， the reduction products was hydrolysis by flavor protease to prepare pea protein mercapto peptide (FMP) with molecular weight < 6 000 u. The preparation process of pea protein mercaptopeptide-zinc chelate (FMP-Zn) was investigated， the structure was characterized， and the zinc absorption mechanism was studied using IEC-6 cells as the model. The results revealed that the chelating ability of zinc reached (293.98±2.09) mg/g when pH=4.0， 40 ℃， 50 min and the mass ratio of peptide to zinc was 1∶4. Spectroscopic analysis indicated that the main chelating sites of FMP with zinc were carboxyl group， amino group， hydroxyl group and sulfhydryl group. Scanning electron microscopy (SEM) and Energy dispersive spectroscopy(EDS) showed that the FMP-Zn exhibited a loose morphology with zinc ions s uniformly distributed across its surface. In comparison to ZnSO4， FMP-Zn was more stable across various pH conditions and throughout simulated gastrointestinal digestion. After gastrointestinal digestion， the zinc retention rate of FMP-Zn was found to be 9.8 times higher than that of ZnSO4. Furthermore， FMP-Zn significantly enhanced zinc absorption in IEC-6 cells. These findings offer a scientific basis for the development of new zinc supplements and underscore the potential for high-value utilization of pea protein isolate resources.