Ricinus Communis : Nutritional Importance, Health Benefits, and Industrial Applications

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ABSTRACT Medicinal plants have garnered special attention worldwide in food, pharmaceutical, nutraceutical, and cosmetic industries, owing to their diverse nutritional and therapeutic profile. Rural inhabitants have traditionally used these plants as therapeutic agents to manage prevalent disorders. Ricinus communis , known as the castor bean, is native to East Africa, the Mediterranean Basin, and Southeast Asia, including India and Pakistan. It is extensively used in various medicinal systems to treat different disorders. This review summarizes the nutritional composition, phytochemistry, health benefits, safety studies, and applications of castor beans and their oil. Various search engines like Google Scholar, PubMed, and ScienceDirect were used to obtain relevant studies ( n = 159). The findings showed that diverse bioactive compounds, including saponins, emodins, terpenoids, anthraquinones, flavonoids, steroids, and alkaloids, exhibit therapeutic properties such as antioxidant, anticancer, anti‐inflammatory, antimicrobial, antidiabetic, and hepatoprotective properties. Furthermore, its antioxidant potential helps attenuate oxidative stress and its associated disorders, including diabetes, cardiovascular disease, and other metabolic disorders. Additionally, different studies have documented the toxicity of castor beans, especially ricin.

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  • Research Article
  • Cite Count Icon 70
  • 10.1074/jbc.m806102200
Regulatory Monoubiquitination of Phosphoenolpyruvate Carboxylase in Germinating Castor Oil Seeds
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Phosphoenolpyruvate carboxylase (PEPC) is a tightly regulated enzyme situated at the core of plant C-metabolism. Although its anaplerotic role and control by allosteric effectors, reversible phosphorylation, and oligomerization have been well documented in the endosperm of developing castor oil seeds (COS), relatively little is known about PEPC in germinating COS. The initial phase of COS germination was accompanied by elevated PEPC activity and accumulation of comparable amounts of pre-existing 107-kDa and inducible 110-kDa immunoreactive PEPC polypeptides (p107 and p110, respectively). A 440-kDa PEPC heterotetramer composed of an equivalent ratio of non-phosphorylated p110 and p107 subunits was purified from germinated COS. N-terminal microsequencing, mass spectrometry, and immunoblotting revealed that both subunits arose from the same gene (RcPpc3) that encodes the p107 subunit of a phosphorylated 410-kDa PEPC homotetramer in developing COS but that p110 is a monoubiquitinated form of p107. Tandem mass spectrometry sequencing of a diglycinated tryptic peptide identified Lys-628 as p110's monoubiquitination site. This residue is conserved in vascular plant PEPCs and is proximal to a PEP-binding/catalytic domain. Incubation with a human deubiquitinating enzyme (USP-2 core) converted the p110:p107 PEPC heterotetramer into a p107 homotetramer while significantly reducing the enzyme's K(m)(PEP) and sensitivity to allosteric activators (hexose-Ps, glycerol-3-P) and inhibitors (malate, aspartate). Monoubiquitination is a non-destructive and reversible post-translational modification involved in the control of diverse processes such as transcription, endocytosis, and signal transduction. The current study demonstrates that tissue-specific monoubiquitination of a metabolic enzyme can also occur and that this modification influences its kinetic and regulatory properties.

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