Bioavailability of lysine in rapeseed and soyabean meals determined by digestibility trial in cockerels and chick growth assay

Larbier, Zuprizal M.; Chagneau, Anne-Marie; Lessire, Michel

doi:10.1016/0377-8401(91)90130-k

Cited by 17 publications

(6 citation statements)

References 15 publications

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“…When the total lysine content was compared with the available lysine content, it was found that approximately 75% of the lysine in the extracted protein would be available in feed. These results agree with those of Larbier et al (1991) who found that lysine digestibility of whole rapeseed meal, dehulled rapeseed meal, and soybean meal for cockerels were 80.1, 86.0, and 88.9%, respectively. The available lysine values for chicks were 72.8, 78.3, and 85.5%, respectively.…”

Section: Discussionsupporting

confidence: 92%

Biorefinery process for protein extraction from oriental mustard (Brassica juncea (L.) Czern.) using ethanol stillage

et al. 2012

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Large volumes of treated process water are required for protein extraction. Evaporation of this water contributes greatly to the energy consumed in enriching protein products. Thin stillage remaining from ethanol production is available in large volumes and may be suitable for extracting protein rich materials. In this work protein was extracted from ground defatted oriental mustard (Brassica juncea (L.) Czern.) meal using thin stillage. Protein extraction efficiency was studied at pHs between 7.6 and 10.4 and salt concentrations between 3.4 × 10-2 and 1.2 M. The optimum extraction efficiency was pH 10.0 and 1.0 M NaCl. Napin and cruciferin were the most prevalent proteins in the isolate. The isolate exhibited high in vitro digestibility (74.9 ± 0.80%) and lysine content (5.2 ± 0.2 g/100 g of protein). No differences in the efficiency of extraction, SDS-PAGE profile, digestibility, lysine availability, or amino acid composition were observed between protein extracted with thin stillage and that extracted with NaCl solution. The use of thin stillage, in lieu of water, for protein extraction would decrease the energy requirements and waste disposal costs of the protein isolation and biofuel production processes.

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Section: Discussionsupporting

confidence: 92%

Biorefinery process for protein extraction from oriental mustard (Brassica juncea (L.) Czern.) using ethanol stillage

et al. 2012

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“…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. Canola protein isolate gave true digestibility value of 95% which was similar to milk protein in this study and it was a somewhat different observation than the low digestibility of canola protein reported in human (Bos et al, 2007), pigs (de Lange et al, 1990;Grala et al, 1998) or chicks and cockerels (Larbrier et al, 1991). In this rat model study, canola protein isolates showed fairly close performance as milk protein for the protein nutritional parameters; similar postprandial metabolic losses of dietary N via deamination of dietary amino acids and excretion in urine, similar digestibility values, and postprandial retention of dietary N resulting in similar growth rate and body composition of rats.…”

Section: Digestibility and Amino Acid Nutritionsupporting

confidence: 42%

Canola/rapeseed protein-functionality and nutrition

Wanasundara¹,

McIntosh²,

Perera³

et al. 2016

OCL

142

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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“…The value obtained during the present study is consistent with a published estimate of 95% for rapeseed protein digestibility in rats, within the same range as soy protein and slightly lower than casein [18]. We did not observe in this species the low true protein digestibility of RPI that we [4] and others [8,19,20] had previously evidenced in humans or other monogastric species. Rats may benefit from more efficient enzymatic equipment to digest hydrolysis-resistant rapeseed proteins than humans or pigs, and as such, are probably not a good model to study dietary protein digestibility in humans, unlike the pig [9,21], at least for dietary proteins with relatively slight differences in digestibility.…”

Section: Discussionsupporting

confidence: 93%

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

et al. 2011

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BackgroundRapeseed is an emerging and promising source of dietary protein for human nutrition and health. We previously found that rapeseed protein displayed atypical nutritional properties in humans, characterized by low bioavailability and a high postprandial biological value. The objective of the present study was to investigate the metabolic fate of rapeseed protein isolate (RPI) and its effect on protein fractional synthesis rates (FSR) in various tissues when compared to a milk protein isolate (MPI).MethodsRats (n = 48) were given a RPI or MPI meal, either for the first time or after 2-week adaptation to a MPI or RPI-based diet. They were divided in two groups for measuring the fed-state tissue FSR 2 h after the meal (using a flooding dose of 13C-valine) and the dietary N postprandial distribution at 5 h (using 15N-labeled meals).ResultsRPI and MPI led to similar FSR and dietary nitrogen (N) losses (ileal and deamination losses of 4% and 12% of the meal, respectively). By contrast, the dietary N incorporation was significantly higher in the intestinal mucosa and liver (+36% and +16%, respectively) and lower in skin (-24%) after RPI than MPI.ConclusionsAlthough RPI and MPI led to the same overall level of postprandial dietary N retention in rats (in line with our findings in humans), this global response conceals marked qualitative differences at the tissue level regarding dietary N accretion. The fact that FSR did not however differed between groups suggest a differential modulation of proteolysis after RPI or MPI ingestion, or other mechanisms that warrant further study.

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Bioavailability of lysine in rapeseed and soyabean meals determined by digestibility trial in cockerels and chick growth assay

Cited by 17 publications

References 15 publications

Biorefinery process for protein extraction from oriental mustard (Brassica juncea (L.) Czern.) using ethanol stillage

Biorefinery process for protein extraction from oriental mustard (Brassica juncea (L.) Czern.) using ethanol stillage

Canola/rapeseed protein-functionality and nutrition

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

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