Recent years have witnessed growing interest in research on the structure and propertiesof proteins and peptides as physiologically active dietary components. The above has spurred a new interest in the isolation of animal, plant and microbiological peptides and investigation of their biological activity. The isolation and separation of protein and peptide mixture is not an easy procedure. Immobilised Metal Ion Affinity Chromatography (IMAC) is increasingly often used in this process. Affinity chromatography relies on the specific interactions between amino acids, their reactive groups in peptides and metal ions. The objective of this study was to determine whether copper and nickel ions can be used for the separation of peptides isolated from string beans than had been blanched and heated in a microwave oven. In this study, peptides extracted with 1% trichloroacetic acid (TCA) from string beans that had been blanched and heated in a microwave oven, were separated by chromatography on columns with copper and nickel ions immobilised through iminodiacetic acid (IDA). Peptide concentrations of the separated fractions were determined. Peptides found in string beans had similar affinity for metal ions in the Cu > Ni sequence, with selectivity in the Ni > Cu sequence. Microwave heating of string beans decreases the peptide content of extracts isolated with 1% TCA. The resulting changes are dependent on the duration of the process and the type of heating medium. Affinity chromatography with the use of metal ions immobilized to iminodiacetic acid (IDA)-Sephadex G-25 may be successfully used for the separation of peptides isolated from string beans.