Changes in the Physicochemical Properties of Rapeseed-derived Protein
Complexes During Enzyme-Assisted Wet Milling
Abstract
Oilseeds need to be exploited not only for the oil but also as a source
of functional protein-rich ingredients for food. This work evaluated the
physicochemical properties of the colloidal fraction resulting from wet
milling of rapeseed, used as model oilseed. The extraction was conducted
either at natural pH (5.7) or at alkaline pH (8.5), with or without
addition of a commercial pectinase. The slurry was mixed for 4 h at room
temperature, and then pressed at the same pH or after shifting to
alkaline/acidic pH. The resulting extract, rich in oil and protein
particles, showed differences in particle size, microstructure and
composition. The oil and protein yields in the extract (in relation to
the amount originally in the oilseed) ranged between 60 and 70 %, with
a significant increase in protein recoveries with addition of pectinase,
regardless of the pH. A protein concentrate, containing between 25 and
42 % protein on dry matter, depending on the treatment was obtained
after centrifugation, together with a fiber precipitate and an oil
fraction. The composition of the concentrates varied, with the highest
purity found for extracts at pH 5.7, showing a nearly complete physical
separation of the oleosomes by low speed centrifugation. All
concentrates showed similar protein composition, as analyzed by gel
electrophoresis. The amino acid composition was also similar amongst the
treatments. This work evidences the critical role played by biopolymers’
interactions in forming different colloidal structures, with clear
consequences on the functionality of the final ingredient.