In an effort to purify potato proteins of superior food grade quality, a new procedure involving anion exchange (ion exchange (IEX)) and hydrophobic interaction chromatography (HIC) was established. Liquid potato fruit juice (PFJ) or re-suspended spray-dried protein was separated by IEX yielding two fractions: a protease inhibitor (PI)-rich fraction and a patatin-rich fraction. Each of these fractions was re-chromatographed on HIC, resulting in two new sub-fractions which were characterised by electrophoresis and mass spectrometry. A high-quality powder should have high lightness, low polyphenol oxidase (PPO) activity and glycoalkaloid content below 150 mu g/g. The PI fraction from spray-dried powder had high lightness (L* = 83) compared to patatin (L* = 50), whereas IEX purification from PFJ resulted in a PI fraction with decreased lightness (L* = 66) and a patatin fraction with increased lightness (L* = 68). HIC fractionation led to increased lightness for patatin fraction, but decreased lightness for the PFJ PI fractions. HIC purification significantly lowered PPO activity in the fractions due to its selective affinity. The lowest total glycoalkaloid content was generally found in HIC fractions from spray-dried powder (150 mu g/g), while high levels (> 1000 mu g/g) were found in PI fractions from PFJ. In conclusion, it was possible to obtain a PI-rich protein isolate from powder with good-quality attributes after both IEX and HIC, while for patatin, the best quality was obtained after the HIC only, and there, the colour or PPO activity may still be a problem depending on source material.