Rapeseed and milk protein exhibit a similar overall nutritional value but marked difference in postprandial regional nitrogen utilization in rats

Boutry, Claire; Fouillet, Hélène; Mariotti, François; Blachier, François; Tomé, Daniel; Bos, Cécile

doi:10.1186/1743-7075-8-52

Cited by 13 publications

(7 citation statements)

References 43 publications

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“…By contrast, our FSR estimate for kidney was as high as that for liver, while it is, on average, lower in the literature. Nevertheless, the separate studies that have concomitantly examined FSR values in kidney and liver have reported contrasting results, with FSR values lower than (7,10,13,23,34), similar to (7, 10, 14, 15), or even higher than (32) those in kidney than liver.…”

Section: Developed Methods For Fsr Estimation: Theoretical Validation mentioning

confidence: 67%

Isotopic and modeling investigation of long-term protein turnover in rat tissues

Huneau

Mariotti

Tomé

et al. 2013

American Journal of Physiology-Regulatory, Integrative and Comp

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Fractional synthesis rates (FSR) of tissue proteins (P) are usually measured using labeled amino acid (AA) tracer methods over short periods of time under acute, particular conditions. By combining the long-term and non-steady-state (15)N labeling of AA and P tissue fractions with compartmental modeling, we have developed a new isotopic approach to investigate the degree of compartmentation of P turnover in tissues and to estimate long-term FSR values under sustained and averaged nutritional and physiological conditions. We measured the rise-to-plateau kinetics of nitrogen isotopic enrichments (δ(15)N) in the AA and P fractions of various tissues in rats for 2 mo following a slight increase in diet δ(15)N. Using these δ(15)N kinetics and a numerical method based on a two-compartment model, we determined reliable FSR estimates for tissues in which P turnover is adequately represented by such a simple precursor-product model. This was the case for kidney, liver, plasma, and muscle, where FSR estimates were 103, 101, 58, and 11%/day, respectively. Conversely, we identified tissues, namely, skin and small intestine, where P turnover proved to be too complex to be represented by a simple two-compartment model, evidencing the higher level of subcompartmentation of the P and/or AA metabolism in these tissues. The present results support the value of this new approach in gaining cognitive and practical insights into tissue P turnover and propose new and integrated FSR values over all individual precursor AA and all diurnal variations in P kinetics.

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Section: Developed Methods For Fsr Estimation: Theoretical Validation mentioning

confidence: 67%

Isotopic and modeling investigation of long-term protein turnover in rat tissues

Huneau

Mariotti

Tomé

et al. 2013

American Journal of Physiology-Regulatory, Integrative and Comp

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“…Nevertheless, because of technical problems in the Eco-MRI follow-up, we could not evidence a lean mass loss after surgery, although it has been shown in rats (55) and humans (12a). Digestive bioavailability was established using a standardized procedure to determine orofecal digestibility 6 h after the test meal ingestion (10,36,44,45) in the absence of any standardized method to determine ileal digestibility in rats. We measured dietary nitrogen in all the distal segments, including cecum, colon, and feces.…”

Section: Discussionmentioning

confidence: 99%

“…where E free valine and Eprotein-bound valine are the [ 13 C]valine enrichments in the free and protein-bound amino acids, respectively. Ebasal is the value of the nonenriched leucine in the same sample, as a surrogate of basal valine enrichment (10). t inc is the time of incorporation of [ 13 C] valine (in min) between the injection and euthanasia (30 min on average).…”

Section: Calculationsmentioning

confidence: 99%

Effect of different bariatric surgeries on dietary protein bioavailability in rats

Tessier

Ribeiro-Parenti

Bruneau

et al. 2019

American Journal of Physiology-Gastrointestinal and Liver Physi

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Bariatric surgery may induce protein malabsorption, although data are scarce. This study aims at evaluating dietary protein bioavailability after different bariatric surgeries in rats. Diet-induced obese Wistar rats were operated for vertical sleeve gastrectomy (VSG) or Roux-en-Y gastric bypass (RYGB). The control group was composed of pair-fed, sham-operated rats (Sham). Two weeks after surgery, rats were fed a 15N protein meal. Protein bioavailability was assessed by determination of 15N recovery in the gastrointestinal tract and organs 6 h after the meal. Fractional protein synthesis rate (FSR) was assessed using a flooding dose of 13C valine. Weight loss was the highest in RYGB rats and the lowest in Sham rats. Surprisingly, RYGB (95.6 ± 0.7%) improved protein digestibility ( P = 0.045) compared with Sham (93.5 ± 0.5%) and VSG (93.8 ± 0.6%). In contrast, 15N retained in the liver ( P = 0.001) and plasma protein ( P = 0.037) was lower than in Sham, with a similar trend in muscle ( P = 0.052). FSR was little altered by bariatric surgery, except for a decrease in the kidney of RYGB ( P = 0.02). The 15N distribution along the small intestinal tissue suggests that dietary nitrogen was considerably retained in the remodeled mucosa of RYGB compared with Sham. This study revealed that in contrast to VSG, RYGB slightly improved protein digestibility but altered peripheral protein bioavailability. This effect may be ascribed to a higher uptake of dietary amino acids by the remodeled intestine. NEW & NOTEWORTHY Using a sensitive 15N meal test, we found that gastric bypass slightly improved protein digestibility compared with sleeve gastrectomy or control but, in contrast, lowered protein retention in the liver and muscles. This paradox can be due to a higher uptake of dietary nitrogen by the intestinal mucosa that was hypertrophied. This study provides new insight on the digestive and metabolic fate of dietary protein in different models of bariatric surgery in rats.

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“…In a comparative study of different protein sources on postprandial regional N utilization by rats, Boutry et al (2011) showed that canola protein exhibit greater retention of N in visceral organs (small intestinal mucosa, liver and kidneys) than milk proteins which particularly enriched skin tissues. Higher content of threonine, one of the EAA that is required for mucin synthesis, and the high S-AA level of canola protein isolate may be related in promoting the retention of dietary N in visceral tissues.…”

Section: Digestibility and Amino Acid Nutritionmentioning

confidence: 99%

Canola/rapeseed protein-functionality and nutrition

Wanasundara¹,

McIntosh²,

Perera³

et al. 2016

OCL

141

103

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-Protein rich meal is a valuable co-product of canola/rapeseed oil extraction. Seed storage proteins that include cruciferin (11S) and napin (2S) dominate the protein complement of canola while oleosins, lipid transfer proteins and other minor proteins of non-storage nature are also found. Although oil-free canola meal contains 36-40% protein on a dry weight basis, non-protein components including fibre, polymeric phenolics, phytates and sinapine, etc. of the seed coat and cellular components make protein less suitable for food use. Separation of canola protein from non-protein components is a technical challenge but necessary to obtain full nutritional and functional potential of protein. Process conditions of raw material and protein preparation are critical of nutritional and functional value of the final protein product. The storage proteins of canola can satisfy many nutritional and functional requirements for food applications. Protein macromolecules of canola also provide functionalities required in applications beyond edible uses; there exists substantial potential as a source of plant protein and a renewable biopolymer. Available information at present is mostly based on the protein products that can be obtained as mixtures of storage protein types and other chemical constituents of the seed; therefore, full potential of canola storage proteins is yet to be revealed.Keywords: Canola / rapeseed storage proteins / cruciferin / napin / protein digestibility / functional properties Résumé -Protéines de canola et de colza : fonctionnalités et nutrition. Les tourteaux riches en protéines repré-sentent un coproduit de valeur de l'extraction de l'huile de canola/colza. Dans la graine, les protéines de stockage, notamment la cruciférine (11S) et la napine (2S), dominent la fraction protéique du canola, mais des oléosines, des protéines de transfert de lipides et d'autres protéines mineures non dédiées au stockage sont également présentes. Bien que le tourteau de canola déshuilé contienne 36-40 % de protéines sur poids sec, la présence de composants non protéiques, dont les fibres, les polymères phénoliques, les phytates, la sinapine, etc. issus de l'enveloppe de la graine et des composants cellulaires rendent les protéines moins appropriées à une utilisation en alimentation humaine. Cette revue présente les connaissances actuelles en termes de valeur nutritionnelle et fonctionnelle des protéines issues des graines de canola. La séparation des protéines de canola des composants non protéiques représente un défi technique mais nécessaire pour libérer totalement le potentiel nutritionnel et fonctionnel de la protéine. Les protéines de stockage de canola peuvent satisfaire un grand nombre d'exigences nutritionnelles et fonctionnelles pour des applications alimentaires. Les macromolécules protéiques de canola offrent également des fonctionnalités requises dans les applications dépassant les seules utilisations alimentaires ; un potentiel important existe en tant que source de protéines végétales et de biopol...

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Rapeseed and milk protein exhibit a similar overall nutritional value but marked difference in postprandial regional nitrogen utilization in rats

Cited by 13 publications

References 43 publications

Isotopic and modeling investigation of long-term protein turnover in rat tissues

Isotopic and modeling investigation of long-term protein turnover in rat tissues

Effect of different bariatric surgeries on dietary protein bioavailability in rats

Canola/rapeseed protein-functionality and nutrition

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