Comparative study of the structural and functional properties of protein isolates prepared from edible vegetable leaves

International Journal of Food Properties

Durodoluwa J. Oyedele¹  Kehinde A. Taiwo¹  Saka O. Gbadamosi¹  Odunayo C. Adebooye¹  Rotimi E. Aluko²  Akinsola A. Famuwagun²  Adeola M. Alashi² 

[1] Obafemi Awolowo University;University of Manitoba;

关键词: leaf;    protein isolate;    intrinsic fluorescence;    gel electrophoresis;    functional properties;   

DOI  :  10.1080/10942912.2020.1772285

来源: DOAJ

【 摘 要 】

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.

【 授权许可】

Unknown