Work

Assembly of oleosin during efficient extraction: Altering the sequence of defatting solvents

Year: 2024

Type: article

Abstract: During the extraction of membrane proteins from oil bodies (OBs), organic solvents dissolve the lipid core and precipitate proteins through solvent stress. Here the effects of solvent type and defatting sequence on the composition and structure of membrane proteins were investigated via SDS-PAGE, FTIR, and SEM-EDS. High purity oleosin (86 %) was obtained by treatment first with a Floch solution and then with cold acetone and petroleum ether after twice washing OBs with urea. The 3D spatial structure of oleosin was predicted using AlphaFold 2, revealing that the secondary structure of oleosin was dominated by α-helices (>60 %). Oleosin consisted of two district types, with oleosin-H (16–17 kDa) being the part of the molecule with limited water solubility, while oleosin-L (13–14 kDa) constituted the non-soluble part. The results provided a technical means of efficient extraction of Camellia oleosins and selective separation of oleosin-L and oleosin-H. • Oleosin was easily prepared by urea washing and defatting with organic solvent. • The main driving force behind oleosin assembly was hydrophobic interactions. • Increasing the polarity of organic solvent reduced the extraction of oleosin-H. • Oleosin-H was more hydrophilic because of its looser structure in N-terminal.

Source: Food Chemistry X

DOI: 10.1016/j.fochx.2024.102022