Pea protein provides a promising matrix for microencapsulating iron.

Worldwide, the most prevalent nutritional deficiency is iron. The strategies for iron supplementation often fail due to poor adherence to supplementation methods contributed to unpleasant sensory characteristics. An alternative is the use of microencapsulated nutrients for home fortification in order to mask undesirable tastes and to allow its release in strategic sites of the gastrointestinal tract.

Vitamin A modulates the expression of genes involved in iron bioavailability.

Iron bioavailability seems to be regulated by vitamin A (VA) but the molecular events involved in this mechanism are not well understood. It is also known that retinoids mediate most of their function via interaction with retinoid receptors, which act as ligand-activated transcription factors controlling the expression of a number of target genes. Here, we evaluated the VA effects on the modulation of the levels of mRNA encoding proteins involved in the iron bioavailability, whether in the intestinal absorption process or in the liver iron metabolism.

Comparison of alpha-tocopherol microparticles produced with different wall materials: pea protein a new interesting alternative.

Alpha-tocopherol is a radical chain breaking antioxidant that can protect the integrity of tissues and play an important role in life process. Microparticles containing alpha-tocopherol were produced by spray drying technique using pea protein (PP), carboxymethylcellulose(CMC) and mixtures of these materials with maltodextrin (PP-M and CMC-M) as wall materials. The microparticles produced were characterised as regards the core retention (high performance liquid chromatography), the morphology (scanning electron microscopy) and size distribution (laser diffraction).

Functional properties of purified vicilins from cowpea (Vigna unguiculata) and pea (Pisum sativum) and cowpea protein isolate.

The major storage globulins (vicilins) of cowpea (Vigna unguiculata) and pea (Pisum sativum) seeds were purified by ammonium sulfate precipitation, and a semipurified cowpea protein isolate (CPI) was prepared by isoelectric precipitation. Some of the functional properties of these proteins, including solubility, foaming, and emulsifying capacities, were investigated and compared. The solubility of purified cowpea vicilin was reduced at pH 5.