Sequential release of amino acids and peptides during in vitro digestion of casein and rapeseed proteins

Savoie, L.; Galibois, Isabelle; Parent, Gérard; Charbonneau, Ruth

doi:10.1016/s0271-5317(05)80094-6

Cited by 38 publications

(24 citation statements)

References 12 publications

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“…The higher in vitro digestibility of RPI recorded in this study may be due to the significant reduction in the soluble and indigestible carbohydrates, antinutritional factors, and more accessibility of amino acid peptide bonds by the digestive enzymes as reported by Devappa and Swamylingappa (2008). Protein isolate (RPI) obtained in this study exhibited lower in vitro digestibility values than casein (97%), but more than rapeseed (83%) and jatropha protein isolates (88.5-90.6%) (Savoie et al, 1988;Devappa and Swamylingappa, 2008).…”

Section: Discussionmentioning

confidence: 60%

Nutritional evaluation of protein isolate from rubber seed in the diet of Labeo rohita : Effects on growth performance, nutrient utilization, whole body composition and metabolic enzymes activity

Fawole

Sahu

Jain

et al. 2016

Animal Feed Science and Technology

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a b s t r a c tThe nutritional potential of protein isolate from rubber seed (RPI) in the diets of Labeo rohita (initial average weight 4.45 ± 0.01 g) was assessed in a 60 days feeding trial. Five isonitrogenous (32.62 ± 0.13 CP Kg −1 ) and isocaloric (18.47 ± 0.08 MJ kg −1 ) experimental diets were formulated with graded level of RPI like 0%, 25%, 50%, 75%, or 100% in replacement for soybean protein isolate (SPI), and designated as Control, RPI25, RPI50, RPI75, RPI100, respectively. The RPI contributed 0%, 13%, 26%, 39% or 52% of the total dietary protein in the diets. Each diets were randomly assigned to 15 experimental tanks containing 12 fish in triplicates and fed to satiation twice daily at 10:00 h and 18:00 h. At the end of the feeding trial, the growth performance and nutrient utilization indices such as percent weight gain (WG%), specific growth rate (SGR), daily growth coefficient (DGC), feed intake (FI), protein efficiency ratio (PER), feed conversion ratio (FCR) and protein retention (PR) values were not significantly (p > 0.05) affected by the dietary treatments irrespective of inclusion levels of RPI. A significantly higher (p < 0.05) hepatosomatic index (HSI) was recorded in the control and RPI 50 group compared to other treatment groups (p < 0.05). The intestinal somatic index (ISI) and Survival rate were similar (p > 0.05) in all the groups. The apparent digestibility coefficients (ADCs) of dry matter and protein for fish fed the control and RPI 100 diets were found to be similar, while RPI 50 and RPI 75 groups exhibited a significantly lower value corresponding to the protease enzyme activity. The whole body compositions and digestive/metabolic enzymes activities among the various groups did not differ significantly (p > 0.05). The serum cholesterol and triglyceride levels were found to be significantly higher (p < 0.05) in the control compared to the RPI fed groups. Significantly higher serum glucose level was recorded in RPI 50, while a reverse was seen in the liver glycogen contents. Overall, this study clearly showed that RPI from rubber seed can serve as alternative protein source in the diets of L. rohita fingerlings without any adverse effects on growth, nutrient utilization and physio-metabolic responses.

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Section: Discussionmentioning

confidence: 60%

Nutritional evaluation of protein isolate from rubber seed in the diet of Labeo rohita : Effects on growth performance, nutrient utilization, whole body composition and metabolic enzymes activity

Fawole

Sahu

Jain

et al. 2016

Animal Feed Science and Technology

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“…Early studies of Savoie et al (1988) suggested that canola protein concentrate (52%, %N × 6.25) exhibits lower in vitro digestibility values (83%) than casein (97%) which may be attributed to the structural rigidity of canola proteins that resists acid-induced (optimum activity of pepsin is pH 1.3-2.0) denaturation and unfolding. Evaluation of rapeseed protein products in rats (Delisle et al, 1983), pigs (Grala et al, 1998) and humans (Bos et al, 2007) indicated that the canola proteins exhibit relatively poor digestibility in vivo and hydrolysis resistant protein fragments exist in the digested products.…”

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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“…The in vitro experimental procedure reproducing in vivo luminal proteolysis conditions has already been described in detail (Savoie et al, 1988 In a previous study (Galibois and Savoie, 1987), good correlations were already found when comparing EAA patterns of digestion products released after a 6-h in vitro proteolysis with qualitative plasma essential amino acid profiles, measured by porto-arterial differences at given intervals in the rat.…”

Section: In Vitro Datamentioning

confidence: 95%

“…Concerning individual kinetics, the highest correspondences were found with rapeseed proteins, with 5 out of 9 EAA (methionine, isoleucine, leucine, phenylalanine and arginine) having their in vitro sequence of release significantly correlated with their in vivo sequence of absorption. With (Geiger, 1947 (Savoie et al, 1988) were compared to the pattern of appearance of dietary amino acids in portal vein of pigs fed the same proteins (Galibois et al, in press). Special attention was paid to peptide-bound amino acids found in the in vitro digesta, as it was shown that peptide absorption is an important mechanism for assimilation of dietary protein (Adibi and Kim, 1981).…”

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confidence: 99%