Variation in seed protein digestion of different pea (Pisum sativum L.) genotypes by cecectomized broiler chickens: 1. Endogenous amino acid losses, true digestibility and in vitro hydrolysis of proteins

Gabriel, Irène; Lessire, Michel; Juin, Hervé; Burstin, Judith; Duc, Gérard; Quillien, Laurence; Thibault, J. N.; Leconte, Maryse; Hallouis, Jean-Marc; Ganier, Patrice; Mézière, Nadine; Sève, Bernard

doi:10.1016/j.livsci.2007.04.002

Cited by 26 publications

(15 citation statements)

References 30 publications

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“…We recently developed a proteome reference map of pea mature seeds 19, showing the extreme diversity of pea seed storage proteins. Because these different proteins do not have equivalent nutritional properties in animal diets, both because of their differential digestibility and their contrasted amino‐acid composition 20, 21, it is paramount to study the genetic control of storage protein deposition in seeds as a component of seed quality for animal feed. Applying the PQL approach to seed protein composition should allow us to decipher the genetic control of this economically significant trait and contribute to improving the nutritive value of legume seeds.…”

Section: Introductionmentioning

confidence: 99%

A PQL (protein quantity loci) analysis of mature pea seed proteins identifies loci determining seed protein composition

Bourgeois¹,

Jacquin²,

Cassecuelle³

et al. 2011

Proteomics

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Legume seeds are a major source of dietary proteins for humans and animals. Deciphering the genetic control of their accumulation is thus of primary significance towards their improvement. At first, we analysed the genetic variability of the pea seed proteome of three genotypes over 3 years of cultivation. This revealed that seed protein composition variability was under predominant genetic control, with as much as 60% of the spots varying quantitatively among the three genotypes. Then, by combining proteomic and quantitative trait loci (QTL) mapping approaches, we uncovered the genetic architecture of seed proteome variability. Protein quantity loci (PQL) were searched for 525 spots detected on 2-D gels obtained for 157 recombinant inbred lines. Most protein quantity loci mapped in clusters, suggesting that the accumulation of the major storage protein families was under the control of a limited number of loci. While convicilin accumulation was mainly under the control of cis-regulatory regions, vicilins and legumins were controlled by both cis- and trans-regulatory regions. Some loci controlled both seed protein composition and protein content and a locus on LGIIa appears to be a major regulator of protein composition and of protein in vitro digestibility.

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Section: Introductionmentioning

confidence: 99%

A PQL (protein quantity loci) analysis of mature pea seed proteins identifies loci determining seed protein composition

Bourgeois¹,

Jacquin²,

Cassecuelle³

et al. 2011

Proteomics

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“…Fractionation of pea seeds into protein, starch and fiber is expanding rapidly in North America and Europe in response to the demand for plantbased protein. Pea seed storage proteins (SSPs) include legumin, vicilin and convicilin globulins and PA1 and PA2 albumins, whose nutritional and technological properties vary according to their amino-acid content and secondary structure 45,46 . We searched the pea genome assembly for SSP genes using all pea storage protein genes available in UNIPROT (Supplementary Notes) and found 12, 9, 2, 8 and 9 genes encoding legumin, vicilin, convicilin, PA1 and PA2, respectively, as well as a few pseudogenes (Supplementary Dataset 8).…”

Section: Paleohistory Of Modern Legume Genomesmentioning

confidence: 99%

A reference genome for pea provides insight into legume genome evolution

Kreplak¹,

Madoui²,

Cápal³

et al. 2019

Nat Genet

424

496

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ea (Pisum sativum L., 2n = 14) is the second most important grain legume in the world after common bean and is an important green vegetable with 14.3 t of dry pea and 19.9 t of green pea produced in 2016 (http://www.fao.org/faostat/). Pea belongs to the Leguminosae (or Fabaceae), which includes cool season grain legumes from the Galegoid clade, such as pea, lentil (Lens culinaris Medik.), chickpea (Cicer arietinum L.), faba bean (Vicia faba L.) and tropical grain legumes from the Milletoid clade, such as common bean (Phaseolus vulgaris L.), cowpea (Vigna unguiculata (L.) Walp.) and mungbean (Vigna radiata (L.) R. Wilczek). It provides significant ecosystem services: it is a valuable source of dietary proteins, mineral nutrients, complex starch and fibers with demonstrated health benefits 1-4 and its symbiosis with N-fixing soil bacteria reduces the need for applied N fertilizers so mitigating greenhouse gas emissions 5-7. Pea was domesticated ~10,000 years

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“…The chemical score of the protein for the selected pasta was evaluated based on amino acid requirements for adults published by WHO/FAO/UNU [33]. The calculation of amino acids adjusted for digestibility of the pasta was obtained considering a weighted average of digestibility; values previously published by Repo-Carrasco-Valencia [8] for quinoa, by Pereira Monteiro et al [34] for Lupinus albus, and by Gabriel et al [35] for pea were used.…”

Section: Theoretical Nutritional Value Of the Obtained Pasta Obtainedmentioning

confidence: 99%

Development of gluten-free and egg-free pasta based on quinoa (Chenopdium quinoa Willd) with addition of lupine flour, vegetable proteins and the oxidizing enzyme POx

Linares-García

Repo‐Carrasco‐Valencia

Glorio‐Paulet

et al. 2019

Eur Food Res Technol

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The aim of this research was to develop gluten-free (GF) and egg-free quinoa pasta with high nutritional value. Extruded and non-extruded quinoa (red and white) flour, potato starch, tara gum, and potato, pea and rice protein isolates were investigated in different recipes, some of them included egg white as an initial reference point. Results showed that extruded quinoa flour, potato starch and tara gum had deteriorating effects on GF and egg-free pasta firmness and cooking quality. Lupine flour addition itself was not able to replace egg white when added in the same amounts, but after increasing the concentration to 12%, the firmness and cooking quality decreasing effects could be improved again, especially when tara gum was absent in the formulations. In the final recipe, the content of lupine flour was increased to 30% because its protein is complementary to the quinoa protein. From the three studied protein isolates, pea protein was superior to potato or rice protein, addition of the oxidizing enzyme POx could even further improve texture firmness. After these trials, the final recipe containing lupine flour, pea protein and POx showed satisfying GF noodle quality and possessed a valuable nutritional composition with high protein and dietary fibre content.

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Variation in seed protein digestion of different pea (Pisum sativum L.) genotypes by cecectomized broiler chickens: 1. Endogenous amino acid losses, true digestibility and in vitro hydrolysis of proteins

Cited by 26 publications

References 30 publications

A PQL (protein quantity loci) analysis of mature pea seed proteins identifies loci determining seed protein composition

A PQL (protein quantity loci) analysis of mature pea seed proteins identifies loci determining seed protein composition

A reference genome for pea provides insight into legume genome evolution

Development of gluten-free and egg-free pasta based on quinoa (Chenopdium quinoa Willd) with addition of lupine flour, vegetable proteins and the oxidizing enzyme POx

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