A New Two-Step Chromatographic Procedure for Fractionation of Potato Proteins with Potato Fruit Juice and Spray-Dried Protein as Source Materials

TY - JOUR

T1 - A New Two-Step Chromatographic Procedure for Fractionation of Potato Proteins with Potato Fruit Juice and Spray-Dried Protein as Source Materials

AU - Schmidt, Jesper Malling

AU - Greve-Poulsen, M.

AU - Damgaard, H.

AU - Sunds, Anne Vuholm

AU - Zdráhal, Z.

AU - Hammershøj, Marianne

AU - Larsen, Lotte Bach

PY - 2017/11/1

Y1 - 2017/11/1

N2 - 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 μg/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 μg/g), while high levels (>1000 μg/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.

AB - 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 μg/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 μg/g), while high levels (>1000 μg/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.

KW - Chlorogenic acid

KW - Glycoalkaloids

KW - Patatin

KW - Polyphenol oxidase

KW - Potatoe protein

KW - Protease inhibitor

KW - Chlorogenic Acid

KW - Glycoalkaloids

KW - Patatin

KW - Polyphenol oxidase

KW - Potato protein

KW - Protease inhibitor

UR - https://www.scopus.com/pages/publications/85026916008

U2 - 10.1007/s11947-017-1966-4

DO - 10.1007/s11947-017-1966-4

M3 - Journal article

SN - 1935-5130

VL - 10

SP - 1946

EP - 1958

JO - Food and Bioprocess Technology

JF - Food and Bioprocess Technology

IS - 11

ER -