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.

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

2018 ◽  
Vol 19 (12) ◽  
pp. 4066 ◽  
Author(s):  
Tatiana Mamontova ◽  
Elena Lukasheva ◽  
Gregory Mavropolo-Stolyarenko ◽  
Carsten Proksch ◽  
Tatiana Bilova ◽  
...  
Keyword(s):  
Pisum Sativum ◽  
Crop Production ◽  
Seed Protein ◽  
High Efficiency ◽  
Animal Feed ◽  
Intracellular Localization ◽  
Food Protein ◽  
Protein Patterns ◽  
Pisum Sativum L ◽  
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 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. Apparently, changes in seed protein patterns might directly affect both of these aspects. Thus, here, we address the pea seed proteome in detail and provide, to the best of our knowledge, the most comprehensive annotation of the functions and intracellular localization of pea seed proteins. To address possible intercultivar differences, we compared seed proteomes of yellow- and green-seeded pea cultivars in a comprehensive case study. The analysis revealed totally 1938 and 1989 nonredundant proteins, respectively. Only 35 and 44 proteins, respectively, could be additionally identified after protamine sulfate precipitation (PSP), potentially indicating the high efficiency of our experimental workflow. Totally 981 protein groups were 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 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 Profiling of Seed Proteome in Pea (Pisum sativum L.) Lines Characterized with High and Low Responsivity to Combined Inoculation with Nodule Bacteria and Arbuscular Mycorrhizal Fungi

Molecules ◽  
2019 ◽  
Vol 24 (8) ◽  
pp. 1603 ◽  
Author(s):  
Mamontova ◽  
Afonin ◽  
Ihling ◽  
Soboleva ◽  
Lukasheva ◽  
...  
Keyword(s):  
Pisum Sativum ◽  
Soil Microorganisms ◽  
Molecular Mechanisms ◽  
High Efficiency ◽  
Arbuscular Mycorrhizal ◽  
Cellular Respiration ◽  
Food Protein ◽  
Pisum Sativum L ◽  
Productivity Gain ◽  
Seed Proteome

Legume crops represent the major source of food protein and contribute to human nutrition and animal feeding. An essential improvement of their productivity can be achieved by symbiosis with beneficial soil microorganisms—rhizobia (Rh) and arbuscular mycorrhizal (AM) fungi. The efficiency of these interactions depends on plant genotype. Recently, we have shown that, after simultaneous inoculation with Rh and AM, the productivity gain of pea (Pisum sativum L) line K-8274, characterized by high efficiency of interaction with soil microorganisms (EIBSM), was higher in comparison to a low-EIBSM line K-3358. However, the molecular mechanisms behind this effect are still uncharacterized. Therefore, here, we address the alterations in pea seed proteome, underlying the symbiosis-related productivity gain, and identify 111 differentially expressed proteins in the two lines. The high-EIBSM line K-8274 responded to inoculation by prolongation of seed maturation, manifested by up-regulation of proteins involved in cellular respiration, protein biosynthesis, and down-regulation of late-embryogenesis abundant (LEA) proteins. In contrast, the low-EIBSM line K-3358 demonstrated lower levels of the proteins, related to cell metabolism. Thus, we propose that the EIBSM trait is linked to prolongation of seed filling that needs to be taken into account in pulse crop breeding programs. The raw data have been deposited to the ProteomeXchange with identifier PXD013479.

scholarly journals Purification, properties and amino acid sequence of a low-Mr abundant seed protein from pea (Pisum sativum L.)

1985 ◽  
Vol 225 (1) ◽  
pp. 239-247 ◽  
Author(s):  
J A Gatehouse ◽  
J Gilroy ◽  
M S Hoque ◽  
R R D Croy
Keyword(s):  
Amino Acid ◽  
Pisum Sativum ◽  
Amino Acid Sequence ◽  
Storage Protein ◽  
Seed Protein ◽  
Storage Proteins ◽  
Ricinus Communis ◽  
Pisum Sativum L ◽  
New Type ◽  
Pea Seeds

The seeds of pea (Pisum sativum L.) contain several proteins in the albumin solubility fraction that are significant components of total cotyledonary protein (5-10%) and are accumulated in developing seeds concurrently with storage-protein synthesis. One of these proteins, of low Mr and designated ‘Psa LA’, has been purified, characterized and sequenced. Psa LA has an Mr of 11000 and contains polypeptides of Mr 6000, suggesting that the protein molecules are dimeric. The amino acid sequence contains 54 residues, with a high content (10/54) of asparagine/aspartate. It has no inhibitory action towards trypsin or chymotrypsin, and is distinct from the inhibitors of those enzymes found in pea seeds, nor does it inhibit hog pancreatic alpha-amylase. The protein contains no methionine, but significant amounts of cysteine (four residues per polypeptide), suggesting a possible role as a sulphur storage protein. However, its sequence is not homologous with low-Mr (2S) storage proteins from castor bean (Ricinus communis) or rape (Brassica napus). Psa LA therefore represents a new type of low-Mr seed protein.

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.

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