TY - JOUR
T1 - Influence of the fractionation method on the protein composition and functional properties
AU - Möller, Anna Cäcilie
AU - van der Padt, Albert
AU - van der Goot, Atze Jan
PY - 2022/10
Y1 - 2022/10
N2 - Mild wet fractionation can separate pea proteins into a soluble and a non-soluble fraction. Soluble proteins and solutes are extracted into the soluble protein fraction, insoluble proteins are collected in the non-soluble protein fraction. The protein composition in the respective fractions was investigated by further fractionating the protein fractions with isoelectric precipitation. The molecular mass of the proteins in the fractions was determined by SDS-PAGE and size exclusion chromatography. The protein fractions' solubility was determined in excess water, and the gelation properties were investigated at the same protein concentration. With mild wet fractionation, compared to conventional wet fractionation, both globulins and albumins are extracted. The protein fractions were mixtures of both proteins, although the non-soluble protein fraction contained mainly globulins. Solubility and gelation properties varied with protein type, composition and protein state; isoelectric precipitation decreased the gelation capacity of the protein fractions.
AB - Mild wet fractionation can separate pea proteins into a soluble and a non-soluble fraction. Soluble proteins and solutes are extracted into the soluble protein fraction, insoluble proteins are collected in the non-soluble protein fraction. The protein composition in the respective fractions was investigated by further fractionating the protein fractions with isoelectric precipitation. The molecular mass of the proteins in the fractions was determined by SDS-PAGE and size exclusion chromatography. The protein fractions' solubility was determined in excess water, and the gelation properties were investigated at the same protein concentration. With mild wet fractionation, compared to conventional wet fractionation, both globulins and albumins are extracted. The protein fractions were mixtures of both proteins, although the non-soluble protein fraction contained mainly globulins. Solubility and gelation properties varied with protein type, composition and protein state; isoelectric precipitation decreased the gelation capacity of the protein fractions.
KW - Mild wet fractionation
KW - Pea albumins
KW - Pea globulins
KW - Pea proteins
KW - Protein functionality
U2 - 10.1016/j.ifset.2022.103144
DO - 10.1016/j.ifset.2022.103144
M3 - Article
AN - SCOPUS:85137655452
SN - 1466-8564
VL - 81
JO - Innovative Food Science and Emerging Technologies
JF - Innovative Food Science and Emerging Technologies
M1 - 103144
ER -