scholarly journals Reduction in the content of antinutritional substances in pea seeds (Pisum sativum L.) by different treatments

2011 ◽  
Vol 50 (No. 11) ◽  
pp. 519-527 ◽  
Author(s):  
R. Dvořák ◽  
A. Pechová ◽  
L. Pavlata ◽  
J. Filípek ◽  
J. Dostálová ◽  
...  
Keyword(s):  
Pisum Sativum ◽  
Seed Treatment ◽  
Production Traits ◽  
Pisum Sativum L ◽  
Heat Treated ◽  
Pea Seeds ◽  
Reactor Temperature ◽  
Pre Treatment ◽  
Pea Seed ◽  
Representative Samples

The goal of the trial was to reduce the content of antinutritional substances in pea (Pisum sativum L.) seeds in order to enhance its use in livestock nutrition. A variety of field pea (Pisum sativum L.) with a high content of antinutritional substances and favourable production traits (Gotik) was chosen. Native and heat-treated pea seeds were used to collect representative samples (n = 6) for analytical purposes. The technology (V-0 technology, Czech patent No. 285745) was further modified by adjusting the reactor temperature, the duration of exposure to that temperature, and the duration of ageing of the material treated in this way (V-I and V-II technologies). The methodology of treatment is based on exposing pea seeds to vapour, organic acids and selected oxides.The monitored parameters included antinutritional substances. As far as the antinutritional substances were concerned, the content of trypsin inhibitors in native pea seeds (P) was around 15.4 ± 0.5 TIU. After treatment with technologies V-0, V-I, and V-II its activity dropped by 83.8, 80.5 and 83.8%, respectively. The pre-treatment titre of lectins (P) was 717 ± 376. It dropped by 70.3, 35.7 and 73.2% after treatment with technologies V-0, V-I and V-II, respectively. The content of tannins measured by the amount of gallic acid in native pea seeds was 49.1 ± 2.7 mg per kg. It dropped by 41.4, 32.0 and 46.2% after the application of the above-mentioned technologies. The content of indigestible oligosaccharides causing flatulence was less affected by the treatments. The pre-treatment content of raffinose was 9.5 ± 0.5 g/kg. The drop associated with the treatment was 9.5, 6.3 and 10.5%, respectively. The pre-treatment content of stachyose was 21.4 ± 0.8 g/kg and after treatment with technologies V-0 and V-II it dropped by 7.0% and by 16.4%, respectively. The application of technology V-I did not result in a drop in the content of stachyose. The content of verbascose in native pea seeds was 16.1 g/kgand the treatment with technologies V-0; V-I and V-II resulted in a drop by 7.5, 5.6 and 20.5%, respectively. As for the detected phenolic acids, with the exception of caffeic acid, not a drop, but an increase in their content was recorded. Isoflavone oestrogens such as daidzein and genistein also recorded a small increase in their content. The results of the trial lead us to conclude that the above-described methods of pea seed treatment, especially the V-II variant, proved to be useful and can be recommended for practical use.  

scholarly journals Proteome Map of Pea (Pisum Sativum L.) Embryos Containing Different Amounts of Residual Chlorophylls

2018 ◽  
Author(s):  
Tatiana Mamontova ◽  
Elena Lukasheva ◽  
Gregory Mavropolo-Stolyarenko ◽  
Carsten Proksch ◽  
Tatiana Bilova ◽  
...  
Keyword(s):  
Pisum Sativum ◽  
Seed Protein ◽  
High Efficiency ◽  
Animal Feed ◽  
Intracellular Localization ◽  
Food Protein ◽  
Protein Patterns ◽  
Pisum Sativum L ◽  
Pea Seeds ◽  
Pea Seed

Due to low culturing costs and high seed protein contents, legumes represent the main global source of food protein. Pea (Pisum sativum L.) is one of the major economically important legume crops, impacting both animal feed and human nutrition. Therefore, the quality of pea seeds needs to be ensured in the context of sustainable crop production and nutritional efficiency. Obviously, changes in seed protein patterns might directly affect both of these aspects. Thus, here we address the pea seed proteome in more detail and provide, to the best of our knowledge, the most comprehensive annotation of the functions and intracellular localization of pea seed proteins. Accordingly, 1938 and 1989 non-redundant proteins were identified in yellow and green pea seeds, in total. Only 35 and 44 proteins, respectively, could be additionally identified after protamine sulfate precipitation (PSP) potentially indicating the high efficiency of our experimental workflow. In total 981 protein groups could be assigned to 34 functional classes, which were to a large extent differentially represented in yellow and green seeds. Closer analysis of these differences by processing of the data in KEGG and String databases revealed their possible relation to a higher metabolic status and reduced longevity of green seeds.

scholarly journals Proteome Map of Pea (Pisum Sativum L.) Embryos Containing Different Amounts of Residual Chlorophylls

2018 ◽  
Author(s):  
Tatiana Mamontova ◽  
Elena Lukasheva ◽  
Gregory Mavropolo-Stolyarenko ◽  
Carsten Proksch ◽  
Tatiana Bilova ◽  
...  
Keyword(s):  
Pisum Sativum ◽  
Seed Protein ◽  
High Efficiency ◽  
Animal Feed ◽  
Intracellular Localization ◽  
Food Protein ◽  
Protein Patterns ◽  
Pisum Sativum L ◽  
Pea Seeds ◽  
Pea Seed

Due to low culturing costs and high seed protein contents, legumes represent the main global source of food protein. Pea (Pisum sativum L.) is one of the major economically important legume crops, impacting both animal feed and human nutrition. Therefore, the quality of pea seeds needs to be ensured in the context of sustainable crop production and nutritional efficiency. Obviously, changes in seed protein patterns might directly affect both of these aspects. Thus, here we address the pea seed proteome in more detail and provide, to the best of our knowledge, the most comprehensive annotation of the functions and intracellular localization of pea seed proteins. Accordingly, 1938 and 1989 non-redundant proteins were identified in yellow and green pea seeds, in total. Only 35 and 44 proteins, respectively, could be additionally identified after protamine sulfate precipitation (PSP) potentially indicating the high efficiency of our experimental workflow. In total 981 protein groups could be assigned to 34 functional classes, which were to a large extent differentially represented in yellow and green seeds. Closer analysis of these differences by processing of the data in KEGG and String databases revealed their possible relation to a higher metabolic status and reduced longevity of green seeds.

β-Amyrin Synthase1 Controls the Accumulation of the Major Saponins Present in Pea (Pisum sativum)

2021 ◽  
Author(s):  
Vanessa Vernoud ◽  
Ludivine Lebeigle ◽  
Jocelyn Munier ◽  
Julie Marais ◽  
Myriam Sanchez ◽  
...  
Keyword(s):  
Pisum Sativum ◽  
Bitter Taste ◽  
Crop Improvement ◽  
Functional Protein ◽  
Saponin Biosynthesis ◽  
Physiological Quality ◽  
Pea Seeds ◽  
Identification And Characterization ◽  
Pea Seed

Abstract The use of pulses as ingredients for the production of food products rich in plant proteins is increasing. However, protein fractions prepared from pea or other pulses contain significant amounts of saponins, glycosylated triterpenes which can impart an undesirable bitter taste when used as an ingredient in foodstuffs. In this paper, we describe the identification and characterization of a gene involved in saponin biosynthesis during pea seed development, by screening mutants obtained from two Pisum sativum TILLING (Targeting Induced Local Lesions in Genomes) populations in two different genetic backgrounds. The mutations studied are located in a gene designated PsBAS1 (β-amyrin synthase1) which is highly expressed in maturing pea seeds and which encodes a protein previously shown to correspond to an active β-amyrin synthase. The first allele is a nonsense mutation, while the second mutation is located in a splice site and gives rise to a mis-spliced transcript encoding a truncated, non-functional protein. The homozygous mutant seeds accumulated virtually no saponin without affecting seed nutritional or physiological quality. Interestingly, BAS1 appears to control saponin accumulation in all other tissues of the plant examined. These lines represent a first step in the development of pea varieties lacking bitterness off-flavours in their seeds. Our work also shows that TILLING populations in different genetic backgrounds represent valuable genetic resources for both crop improvement and functional genomics.

Proximate and mineral composition of field peas

1997 ◽  
Vol 77 (1) ◽  
pp. 101-103 ◽  
Author(s):  
T. D. Warkentin ◽  
A. G. Sloan ◽  
S. T. Ali-Khan
Keyword(s):  
Pisum Sativum ◽  
Key Words ◽  
Mineral Composition ◽  
Seed Yield ◽  
Total Protein ◽  
Field Pea ◽  
Pisum Sativum L ◽  
Field Peas ◽  
Pea Seeds ◽  
Proximate And Mineral Composition

Field pea seeds from 10 cultivars grown at two locations in Manitoba in 1986 and 1987 were analyzed for proximate and mineral profiles. Cultivars differed significantly in their level of total protein, crude fat, ADF, and all minerals tested. However, differences were not extremely large and were comparable to European reports. Location-year also had a significant effect on the levels of total protein, ADF, and all minerals tested. In most cases, the warmest location-year produced relatively higher levels of minerals, ash, and total protein, and lower seed yield than the coolest location-year. Key words: Field pea, Pisum sativum L., mineral

Feeding stem–leaf–pod explants of pea (Pisum sativum L.) with d-chiro-inositol or d-pinitol modifies composition of α-d-galactosides in developing seeds

2010 ◽  
Vol 20 (4) ◽  
pp. 213-221 ◽  
Author(s):  
Lesław B. Lahuta ◽  
Wojciech Święcicki ◽  
Tomasz Dzik ◽  
Ryszard J. Górecki ◽  
Marcin Horbowicz
Keyword(s):  
Pisum Sativum ◽  
Soluble Carbohydrates ◽  
Raffinose Family Oligosaccharides ◽  
Developing Seeds ◽  
Pisum Sativum L ◽  
Pea Seeds ◽  
Low Levels ◽  
Stem Leaf

AbstractFeeding stem–leaf–pod explants with d-chiro-inositol and d-pinitol was used as a method to modify α-d-galactosides in developing pea (Pisum sativum) seeds. Four genotypes differing in the composition of raffinose, stachyose and verbascose (raffinose family oligosaccharides or RFOs) in seeds – high RFOs (cv. Tiny), low RFOs (SZD175) and low verbascose (cv. Hubal and cv. Wt 506) – were studied. Although seeds of all examined pea lines were able to take up both d-chiro-inositol and d-pinitol, only d-chiro-inositol was effectively converted into its galactosides: mainly fagopyritol B1 (O-α-d-galactopyranosyl-(1 → 2)-d-chiro-inositol) and fagopyritol B2 (O-α-d-galactopyranosyl-(1 → 6)-O-α-d-galactopyranosyl-(1 → 2)-d-chiro-inositol). In seeds of pea lines naturally containing low levels of verbascose (cv. Hubal) and low RFOs (SZD175), the enhanced accumulation of fagopyritols depressed the RFO level by c. 64 and 20%, respectively. Moreover, in both genotypes, about 25 and 30% of total galactose bound in α-d-galactosides occurred in fagopyritols. d-Pinitol present in the pea seeds was converted into monogalactosides, but their accumulation was several-fold lower than that of fagopyritols and did not significantly influence the accumulation of RFOs. Pea seeds with the composition of soluble carbohydrates modified by feeding with either of the cyclitols were able to complete germination.

scholarly journals The Fate of l-Phenylalanine Fed to Germinating Pea Seeds, Pisum sativum (L.) var. Alaska, during Imbibition

1971 ◽  
Vol 47 (1) ◽  
pp. 119-123 ◽  
Author(s):  
Constance Nozzolillo ◽  
K. B. Paul ◽  
C. Godin
Keyword(s):  
Pisum Sativum ◽  
Pisum Sativum L ◽  
Pea Seeds

SCREENING OF FIELD PEA BREEDING LINES FOR PEA SEED-BORNE MOSAIC VIRUS

1979 ◽  
Vol 59 (1) ◽  
pp. 171-175 ◽  
Author(s):  
S. T. ALI-KHAN ◽  
R. C. ZIMMER
Keyword(s):  
Pisum Sativum ◽  
Mosaic Virus ◽  
Field Pea ◽  
Research Station ◽  
Chenopodium Amaranticolor ◽  
Breeding Lines ◽  
Pisum Sativum L ◽  
Local Lesion Host ◽  
Extensive Program ◽  
Pea Seed

Pea seed-borne mosaic virus (PSbMV) was first identified in Canadian field pea (Pisum sativum L.) breeding lines in 1974. Since then, an extensive program has been underway to eradicate this virus from the breeding lines. At the Morden Research Station, nearly 2000 breeding lines were evaluated. The virus was assayed by infectivity tests using the local lesion host Chenopodium amaranticolor, and by a gel immunodiffusion test. PSbMV was detected in 1361 lines. The level of infection within lines varied from 1 to 3%. Due to the restricted extent of the virus in the breeding lines, it was possible to continue the breeding program without a serious loss in germplasm.

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