Subunit composition affects formation and stabilization of o/w emulsions by 11S seed storage protein cruciferin.

The 11S globulin cruciferin is the major storage protein in Brassicaceae/Cruciferae seeds and exists as a hexamer in its natural configuration. Arabidopsis thaliana cruciferin is composed of CRUA, CRUB and CRUC subunits. Wild type (WT) cruciferin and cruciferins composed only of identical CRUA, CRUB and CRUC subunits were examined for their ability to form and stabilize oil-in-water (o/w) emulsions.

Comparison of five major trichome regulatory genes in Brassica villosa with orthologues within the Brassicaceae.

Coding sequences for major trichome regulatory genes, including the positive regulators GLABRA 1(GL1), GLABRA 2 (GL2), ENHANCER OF GLABRA 3 (EGL3), and TRANSPARENT TESTA GLABRA 1 (TTG1) and the negative regulator TRIPTYCHON (TRY), were cloned from wild Brassica villosa, which is characterized by dense trichome coverage over most of the plant. Transcript (FPKM) levels from RNA sequencing indicated much higher expression of the GL2 and TTG1 regulatory genes in B. villosa leaves compared with expression levels of GL1 and EGL3 genes in either B.

Structural and physicochemical property relationships of cruciferin homohexamers.

Heteromeric cruciferin from wild type (WT) Arabidopsis thaliana and homomeric cruciferin CRUA, CRUB, and CRUC composed of identical subunits obtained from double-knockout mutant lines were investigated for their structural and physicochemical properties. A three-step chromatographic procedure allowed isolation of intact cruciferin hexamers with high purity (>95%). FT-IR and CD analysis of protein secondary structure composition revealed that all cruciferins were folded into higher order structures consisting of 44-50% β-sheets and 7-9% α-helices.

Characterization of Arabidopsis thaliana lines with altered seed storage protein profiles using synchrotron-powered FT-IR spectromicroscopy.

Arabidopsis thaliana lines expressing only one cruciferin subunit type (double-knockout; CRUAbc, CRUaBc, or CRUabC) or devoid of cruciferin (triple-knockout; CRU-) or napin (napin-RNAi) were generated using combined T-DNA insertions or RNA interference approaches. Seeds of double-knockout lines accumulated homohexameric cruciferin and contained similar protein levels as the wild type (WT). Chemical imaging of WT and double-knockout seeds using synchrotron FT-IR spectromicroscopy (amide I band, 1650 cm(-1), νC═O) showed that proteins were concentrated in the cell center and protein storage vacuoles.

In silico homology modeling to predict functional properties of cruciferin.

Cruciferin is the major storage protein in Brassicaceae family oilseeds. The predominant cruciferin isoforms in Arabidopsis thaliana were investigated using homology modeling (HM) for their molecular structures and functional properties. The structure of Brassica napus procruciferin was used as the template for HM to determine the molecular structures and hypervariable regions.

Physicochemical, thermal and functional characterisation of protein isolates from Kabuli and Desi chickpea (Cicer arietinum L.): a comparative study with soy (Glycine max) and pea (Pisum sativum L.).

Background: Chickpea (Cicer arietinum L.) seeds are a good source of protein that has potential applications in new product formulation and fortification. The main objectives of this study were to analyse the physicochemical, thermal and functional properties of chickpea protein isolates (CPIs) and compare them with those of soy (SPI) and pea (PPI) protein isolates.