The isolation of a, a', and ß-strands of b-conglycinin from soy protein concentrate (SPC) needed to be performed. Reagents for extraction and purification were sourced from Sigma-Aldrich and Bio-Rad (Hercules, CA, USA). SPC was subjected to pH adjustment to the isoelectric point of each strand, following a standard titration curve (Figure ). The precipitated proteins underwent centrifugation at 10,000 × g for 20 minutes at 4°C, resulting in the isolation of a clear supernatant rich in the desired proteins. Chromatographic separation was achieved through ion-exchange chromatography on a Biorad EconoPac Gravity Column with DEAE resin, equilibrated with Tris-HCl buffer. A stepwise elution gradient of NaCl in the range of 0 to 1 M was applied to elute distinct protein fractions. B-conglycinin containing fractions were identified via absorbance monitoring at 280 nm. Eluted fractions were concentrated using an ultrafiltration device (10 kDa molecular weight cutoff). The resulting strands were used for our further analysis.