Chemical and Nutritional Evaluation of Protein-Rich Ingredients Obtained through a Technological Process from Yellow Lupin Seeds (Lupinus luteus).

In recent years, interest in plant-based proteins has been rising due to ethical and sustainability issues. In this context, the production of protein concentrates and isolates from new plant sources have increased enormously because of their nutritional and techno-functional properties. Therefore, this work describes a pilot process for obtaining protein-rich ingredients from a yellow lupin variety (Lupinus luteus) developed by the Agriaquaculture Nutritional Genomic Center (CGNA).

Molecular and functional characterization of ferredoxin NADP(H) oxidoreductase from Gracilaria chilensis and its complex with ferredoxin.

Backgroud: Ferredoxin NADP(H) oxidoreductases (EC 1.18.1.

Emulsifying and Foaming Properties of Different Protein Fractions Obtained from a Novel Lupin Variety AluProt-CGNA(®) (Lupinus luteus).

The use of vegetable proteins as food ingredient is becoming increasingly important due to their high versatility and environmental acceptability. This work describes a chemical characterization and techno-functional properties (emulsifying and foaming properties) of 3 protein fractions obtained from a protein-rich novel lupin variety, AluProt-CGNA(®) . This nongenetically modified variety have a great protein content in dehulled seeds (60.

Novel regulatory principles of the spliceosomal Brr2 RNA helicase and links to retinal disease in humans.

For each round of pre-mRNA splicing, a spliceosome is assembled anew on its substrate. RNA-protein remodeling events required for spliceosome assembly, splicing catalysis, and spliceosome disassembly are driven and controlled by a conserved group of ATPases/RNA helicases. The activities of most of these enzymes are timed by their recruitment to the spliceosome.

Inhibition of RNA helicase Brr2 by the C-terminal tail of the spliceosomal protein Prp8.

The Ski2-like RNA helicase Brr2 is a core component of the spliceosome that must be tightly regulated to ensure correct timing of spliceosome activation. Little is known about mechanisms of regulation of Ski2-like helicases by protein cofactors. Here we show by crystal structure and biochemical analyses that the Prp8 protein, a major regulator of the spliceosome, can insert its C-terminal tail into Brr2's RNA-binding tunnel, thereby intermittently blocking Brr2's RNA-binding, adenosine triphosphatase, and U4/U6 unwinding activities.