Short communication: Stabilization of milk proteins at pH 5.5 using pectic polysaccharides derived from potato tubers

Potato pectin has unique molecular characteristics that differentiate it from commercially available pectins sourced from citrus peels or apple pomace, including a higher degree of branching and a higher acetyl content. The objective of this study was to evaluate the ability of potato pectin to stabilize milk proteins at an acidic pH above their isoelectric point, pH 5.5, at which no citrus- or apple-derived pectins are functional. Potato pectin was extracted from raw potato tubers by heating at pH 4.5 and 120°C for 30 min after removing starch solubilized using a dilute HCl solution adjusted to pH 2. The potato pectin was found to have a galacturonic acid content of 17.31 ± 3.29% (wt/wt) and a degree of acetylation of 20.20 ± 0.12%. A portion of the potato pectin was deacetylated by heating it in an alkaline condition. The deacetylation resulted in a galacturonic acid content of 19.12 ± 4.64% (wt/wt) and a degree of acetylation of 3.03 ± 0.03%. Particle size distributions in acidified milk drink (AMD) samples adjusted to pH 5.5 demonstrated that the acetylated and deacetylated potato pectins were capable of inhibiting the aggregation of milk proteins to the largest degree at a pectin concentration of 1.0 and 0.25% (wt/wt), respectively. Pectin molecules that were not bound to milk proteins in these AMD samples were quantified after centrifugally separating milk proteins and pectin bound to them from the serum. We found that, for the acetylated and deacetylated potato pectins, all or approximately half of the pectin molecules were bound to milk proteins at a pectin concentration of 0.25 or 1.0% (wt/wt), respectively. These results suggest that the presence of acetyl groups is a critical factor that determines how potato pectin molecules bind electrostatically to milk protein surfaces, form 3-dimensional structures there, and function as a stabilizer. The present results demonstrate that potato pectin can stabilize milk proteins at pH 5.5 and potentially enable the development of novel AMD products with improved functionality for casein-containing products with moderately acidic pH profiles.