Ricin (from Ricinus communis) as undesirable substances in animal feed - Scientific Opinion of the Panel on Contaminants in the Food Chain

,

doi:10.2903/j.efsa.2008.726

Cited by 13 publications

(7 citation statements)

References 88 publications

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“…The oil makes up about 50% of the weight of the seeds and is mostly constituted of ricinoleic acid (90%), with minor amounts of dihydroxystearic, linoleic, oleic, and stearic acids. Ricin isoforms and the alkaloid ricinine, are not transferred to the oil fraction during extraction, which can be performed by cold or warm pressing, but remain in the seed cake [93,94].…”

Section: Bioterrorism and Environmental Toxicitymentioning

confidence: 99%

“…Ricinus derived material should be appropriately inactivated through physical and/or chemical methods to guarantee animal and human health [95]. Nevertheless, many accidental poisonings are still reported for animals eating improperly detoxified fertilizer or other agricultural products containing castor derived material [76,94].…”

Section: Bioterrorism and Environmental Toxicitymentioning

confidence: 99%

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Ricin: An Ancient Story for a Timeless Plant Toxin

Polito

Bortolotti

Battelli

et al. 2019

Toxins

112

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The castor plant (Ricinus communis L.) has been known since time immemorial in traditional medicine in the pharmacopeia of Mediterranean and eastern ancient cultures. Moreover, it is still used in folk medicine worldwide. Castor bean has been mainly recommended as anti-inflammatory, anthelmintic, anti-bacterial, laxative, abortifacient, for wounds, ulcers, and many other indications. Many cases of human intoxication occurred accidentally or voluntarily with the ingestion of castor seeds or derivatives. Ricinus toxicity depends on several molecules, among them the most important is ricin, a protein belonging to the family of ribosome-inactivating proteins. Ricin is the most studied of this category of proteins and it is also known to the general public, having been used for several biocrimes. This manuscript intends to give the reader an overview of ricin, focusing on the historical path to the current knowledge on this protein. The main steps of ricin research are here reported, with particular regard to its enzymatic activity, structure, and cytotoxicity. Moreover, we discuss ricin toxicity for animals and humans, as well as the relation between bioterrorism and ricin and its impact on environmental toxicity. Ricin has also been used to develop immunotoxins for the elimination of unwanted cells, mainly cancer cells; some of these immunoconjugates gave promising results in clinical trials but also showed critical limitation.

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Section: Bioterrorism and Environmental Toxicitymentioning

confidence: 99%

Section: Bioterrorism and Environmental Toxicitymentioning

confidence: 99%

Ricin: An Ancient Story for a Timeless Plant Toxin

Polito

Bortolotti

Battelli

et al. 2019

Toxins

112

View full text Add to dashboard Cite

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“…Thus, a higher lactose content leads to a larger responsivity of the 2-D PC PAAm-AAc-Lactose sensor. We determined a limit of detection (LoD) of the 2-D PC PAAm-AAc-Lactose-120 hydrogel sensor of 9 μg/mL (7.5 × 10 –8 M) ricin, which is far below the adult human lethal oral dose of 20–30 mg/kg . This LoD value is comparable to a mouse bioassay method (∼7.5 μg/mL) but our ricin sensor responds faster (100 min) compared to the mouse bioassay method (24 h). , We also determined that the dynamic range of the 2-D PC PAAm-AAc-Lactose-120 hydrogel sensor is between 2.5 × 10 –7 M and 24.3 × 10 –7 M, while its linear range is from 7.5 × 10 –8 M to 27.5 × 10 –8 M (see SI and Figure S9 for calculation details).…”

Section: Resultsmentioning

confidence: 94%

Responsive Photonic Crystal Carbohydrate Hydrogel Sensor Materials for Selective and Sensitive Lectin Protein Detection

et al. 2017

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Lectin proteins, such as the highly toxic lectin protein, ricin, and the immunochemically important lectin, jacalin, play significant roles in many biological functions. It is highly desirable to develop a simple but efficient method to selectively detect lectin proteins. Here we report the development of carbohydrate containing responsive hydrogel sensing materials for the selective detection of lectin proteins. The copolymerization of a vinyl linked carbohydrate monomer with acrylamide and acrylic acid forms a carbohydrate hydrogel that shows specific "multivalent" binding to lectin proteins. The resulting carbohydrate hydrogels are attached to 2-D photonic crystals (PCs) that brightly diffract visible light. This diffraction provides an optical readout that sensitively monitors the hydrogel volume. We utilize lactose, galactose, and mannose containing hydrogels to fabricate a series of 2-D PC sensors that show strong selective binding to the lectin proteins ricin, jacalin, and concanavalin A (Con A). This binding causes a carbohydrate hydrogel shrinkage which significantly shifts the diffraction wavelength. The resulting 2-D PC sensors can selectively detect the lectin proteins ricin, jacalin, and Con A. These unoptimized 2-D PC hydrogel sensors show a limit of detection (LoD) of 7.5 × 10 M for ricin, a LoD of 2.3 × 10 M for jacalin, and a LoD of 3.8 × 10 M for Con A, respectively. This sensor fabrication approach may enable numerous sensors for the selective detection of numerous lectin proteins.

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“…Type 1 RIP is characterised by low toxicity, especially when compared to type 2 RIPs (e.g. ricin) (EFSA CONTAM Panel, 2008;Devappa et al, 2010b;Wu and Sun, 2012). Curcin concentrations are assessed by the applicant according to a specific qualitative method based on SDS-gel electrophoresis followed by mass spectrometry (SDS-gel electrophoresis and nano-LC-ESI-MS/MS).…”

Section: Anti-nutritional Factorsmentioning

confidence: 99%

Safety of hydrothermally treated kernels from edible Jatropha curcas L. (Chuta) as a novel food pursuant to Regulation (EU) 2015/2283

Turck¹,

Bohn²,

Castenmiller³

et al. 2022

EFS2

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Following a request from the European Commission, the EFSA Panel on Nutrition, Novel Foods and Food Allergens (NDA) was asked to deliver an opinion on hydrothermally treated kernels from edible Jatropha curcas (Chuta) as a novel food (NF) pursuant to Regulation (EU) 2015/2283. Although Jatropha curcas is generally considered a toxic plant due to the presence of phorbol esters (PEs), edible varieties exist in Central America. The applicant has developed a breeding programme for an edible cultivar and proposes the kernels from this cultivar as an NF as whole kernels or fragments thereof to be used as a snack or as a food ingredient. Procedures are in place to avoid commingling with non‐edible kernels, with the last steps being the analytical control of PEs concentrations in all produced batches. The Panel considers that the production process of the NF is sufficiently described and that the information provided on the composition of the NF is sufficient for its characterisation. Components of the NF were tested for genotoxicity applying the standard in vitro test battery and no genotoxic concerns have been identified. In a conservative scenario for exposure to PEs from the NF, it was assumed that all kernels contain PEs at the level of detection of the analytical method. When comparing the estimated maximum exposure to PEs with a reference point from a subchronic study in pigs, a margin of exposure ≥ 900 is obtained, which is considered sufficiently large. The presence of anti‐nutritional factors does not pose safety concerns as they are within the ranges found in vegetables. The Panel concludes that the NF is safe under the proposed conditions of use.

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Ricin (from Ricinus communis) as undesirable substances in animal feed - Scientific Opinion of the Panel on Contaminants in the Food Chain

Cited by 13 publications

References 88 publications

Ricin: An Ancient Story for a Timeless Plant Toxin

Ricin: An Ancient Story for a Timeless Plant Toxin

Responsive Photonic Crystal Carbohydrate Hydrogel Sensor Materials for Selective and Sensitive Lectin Protein Detection

Safety of hydrothermally treated kernels from edible Jatropha curcas L. (Chuta) as a novel food pursuant to Regulation (EU) 2015/2283

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