Abstract
The presence of rennet whey solids in milk powder and buttermilk powder could be detected by analyzing the caseinomacropeptide (6.7 kDa) content by capillary zone electrophoresis. A hydrophilically coated capillary was used in combination with 6 M urea in a citrate buffer at low pH. Under these conditions, genetic A and B variants migrated as a single peak. This afforded a detection limit of 0.4% of rennet whey solids in combination with large volume injections and on-column isotachophoretic concentration of the sample. The detector response (UV at 214 nm) was linear in the range of 1–20% rennet whey solids and the recovery of caseinomacropeptide was 98%. Pseudo-casei-nomacropeptide, lacking the N-terminal Met-residue, could be separated from caseinomacropeptide, thus preventing false positive results for some types of acid buttermilk powder.