Title
Comparative study of the structural and functional properties of protein isolates prepared from edible vegetable leaves
Author
Akinsola A. Famuwagun, Adeola M. Alashi, Saka O. Gbadamosi, Kehinde A. Taiwo, Durodoluwa J. Oyedele, Odunayo C. Adebooye & Rotimi E. Aluko
Year
2020
Journal
International Journal of Food Properties, 23:1, 955-970
Abstract
Isoelectric precipitation was used to produce protein isolates (>90% protein
contents) from three edible vegetable leaves. Amaranth (ALI), eggplant (ELI)
and fluted pumpkin (FLI) leaf protein were isolated to study their conformational structures. Intrinsic fluorescence indicated a loose structural conformation for ELI at all the pH values, whereas FLI and ALI had more compact
structures at pH 3.0 and pH 9.0. The surface hydrophobicity showed a greater
distribution of hydrophobic amino acid groups of the protein isolates at the
basic than the acidic regions. The SDS-PAGE results showed that the leaf
isolates had similar polypeptide bonds characterized by 20, 25, 40 and 200
kDa and some distinct bands above 200 kDa. The ELI formed emulsions with
significantly (p < .05) smallest oil droplet sizes (<3.3 µm) when compared to
FLI and ALI. However, foaming capacity was mostly pH-dependent with
significantly (p < .05) higher values at pH 7.0 and 9.0. The leaf protein isolates
may be considered as potential functional food ingredients.
Full Article
Instrument
FP-6300, J-810
Keywords
Leaf, protein isolate, Intrinsic fluorescence, gel electrophoresis, functional properties