scholarly journals Identification and Assessment of the Potential Allergenicity of 7S Vicilins in Olive (Olea europaeaL.) Seeds

2016 ◽  
Vol 2016 ◽  
pp. 1-11 ◽  
Author(s):  
Jose C. Jimenez-Lopez ◽  
Adoración Zafra ◽  
Lucía Palanco ◽  
José Fernando Florido ◽  
Juan de Dios Alché
Keyword(s):  
Structural Analysis ◽  
Storage Proteins ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Raw Material ◽  
Olive Seed ◽  
Bioinformatic Approaches ◽  
Species Specific ◽  
Olive Seeds ◽  
Potential Use

Olive seeds, which are a raw material of interest, have been reported to contain 11S seed storage proteins (SSPs). However, the presence of SSPs such as 7S vicilins has not been studied. In this study, following a search in the olive seed transcriptome, 58 sequences corresponding to 7S vicilins were retrieved. A partial sequence was amplified by PCR from olive seed cDNA and subjected to phylogenetic analysis with other sequences. Structural analysis showed that olive 7S vicilin contains 9α-helixes and 22β-sheets. Additionally, 3D structural analysis displayed good superimposition with vicilin models generated fromPistaciaandSesamum. In order to assess potential allergenicity, T and B epitopes present in these proteins were identified by bioinformatic approaches. Different motifs were observed among the species, as well as some species-specific motifs. Finally, expression analysis of vicilins was carried out in protein extracts obtained from seeds of different species, including the olive. Noticeable bands were observed for all species in the 15–75 kDa MW interval, which were compatible with vicilins. The reactivity of the extracts to sera from patients allergic to nuts was also analysed. The findings with regard to the potential use of olive seed as food are discussed.

Molecular and structural analysis of electrophoretic variants of soybean seed storage proteins

2003 ◽  
Vol 64 (3) ◽  
pp. 701-708 ◽  
Author(s):  
Nobuyuki Maruyama ◽  
Takako Fukuda ◽  
Shiori Saka ◽  
Nauko Inui ◽  
Junko Kotoh ◽  
...  
Keyword(s):  
Structural Analysis ◽  
Storage Proteins ◽  
Soybean Seed ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Electrophoretic Variants

Characterization of olive seed storage proteins

2007 ◽  
Vol 29 (5) ◽  
pp. 439-444 ◽  
Author(s):  
Wei Wang ◽  
Juan de Dios Alché ◽  
Marìa Isabel Rodríguez-García
Keyword(s):  
Storage Proteins ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Olive Seed

SDS–PAGE of seed proteins in Festuca (Poaceae): taxonomic implications

1991 ◽  
Vol 69 (7) ◽  
pp. 1425-1432 ◽  
Author(s):  
S. G. Aiken ◽  
S. E. Gardiner
Keyword(s):  
Native Species ◽  
Storage Proteins ◽  
Polyacrylamide Gel Electrophoresis ◽  
Seed Proteins ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Banding Patterns ◽  
Ungerminated Seed ◽  
Sds Page ◽  
Species Specific

Taxonomically useful descriptors were provided by the banding patterns of seed storage proteins obtained when extracts of bulked, ungerminated seed samples from commercially available North American native species of Festuca were analyzed by sodium dodecylsulphate polyacrylamide gel electrophoresis (SDS–PAGE). The banding patterns for three species of rough fescues (section Breviaristatae Krivot) indicate that although the taxa are closely related, F. campestris Rydb. (2n = 56) does not appear to be an autoploid of either F. altaica Trin. (2n = 28) or F. hallii (Vasey) Piper (2n = 28). A distinct band corresponding to a molecular weight of 57 000 occurred in the seed protein profiles of all native and commercial samples of Festuca L. analyzed. The profile for F. californica Vasey, questionably section Breviaristatae, also has a band at this position, and is very different from that of F. altaica, F. campestris, and F. hallii. Species-specific banding patterns were observed for F. brachyphylla Schultes, F. saximontana Rydb., F. idahoensis Elmer, and F. trachyphylla (Hackel) Krajina (F. ovina L. s.l., F. longifolia Thuill., F. ovina var. duriuscula auct. amer.). The results support the recognition of subgenus Schedonorus (Beauv.) Peter., and sections Breviaristatae Krivot and Festuca. Key words: Poaceae, Festuca, SDS–PAGE seed proteins.

scholarly journals Identification of species-specific peptide markers in cold-pressed oils

2020 ◽  
Vol 10 (1) ◽  
Author(s):  
Klaudia Kotecka-Majchrzak ◽  
Agata Sumara ◽  
Emilia Fornal ◽  
Magdalena Montowska
Keyword(s):  
Storage Proteins ◽  
Seed Storage ◽  
High Sensitivity ◽  
Seed Storage Proteins ◽  
Global Market ◽  
Evening Primrose ◽  
Allergenic Proteins ◽  
Species Specific ◽  
Cold Pressed ◽  
Specific Peptide

AbstractIn recent years, cold-pressed vegetable oils have become very popular on the global market. Therefore, new versatile methods with high sensitivity and specificity are needed to find and combat fraudulent practices. The objective of this study was to identify oilseed species-specific peptide markers, using proteomic techniques, for authentication of 10 cold-pressed oils. In total, over 380 proteins and 1050 peptides were detected in the samples. Among those peptides, 92 were found to be species-specific and unique to coconut, evening primrose, flax, hemp, milk thistle, nigella, pumpkin, rapeseed, sesame, and sunflower oilseed species. Most of the specific peptides were released from major seed storage proteins (11 globulins, 2S albumins), and oleosins. Additionally, the presence of allergenic proteins in the cold-pressed oils, including pumpkin Cuc ma 5, sunflower Hel a 3, and six sesame allergens (Ses i 1, Ses i 2, Ses i 3, Ses i 4, Ses i 6, and Ses i 7) was confirmed in this study. This study provides novel information on specific peptides that will help to monitor and verify the declared composition of cold-pressed oil as well as the presence of food allergens. This study can be useful in the era of widely used unlawful practices.

scholarly journals Histological Features of the Olive Seed and Presence of 7S-Type Seed Storage Proteins as Hallmarks of the Olive Fruit Development

2018 ◽  
Vol 9 ◽  
Author(s):  
Adoración Zafra ◽  
Mohammed M’rani-Alaoui ◽  
Elena Lima ◽  
Jose Carlos Jimenez-Lopez ◽  
Juan de Dios Alché
Keyword(s):  
Fruit Development ◽  
Storage Proteins ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Histological Features ◽  
Olive Fruit ◽  
Olive Seed

scholarly journals Wheat (Triticum aestivum L.) TaHMW1D Transcript Variants Are Highly Expressed in Response to Heat Stress and in Grains Located in Distal Part of the Spike

Plants ◽  
2021 ◽  
Vol 10 (4) ◽  
pp. 687
Author(s):  
Chan Seop Ko ◽  
Jin-Baek Kim ◽  
Min Jeong Hong ◽  
Yong Weon Seo
Keyword(s):  
Heat Stress ◽  
High Temperature ◽  
Temperature Stress ◽  
Storage Proteins ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Grain Filling ◽  
High Temperature Stress ◽  
Two Dimensional Gel Electrophoresis ◽  
Transcript Variants

High-temperature stress during the grain filling stage has a deleterious effect on grain yield and end-use quality. Plants undergo various transcriptional events of protein complexity as defensive responses to various stressors. The “Keumgang” wheat cultivar was subjected to high-temperature stress for 6 and 10 days beginning 9 days after anthesis, then two-dimensional gel electrophoresis (2DE) and peptide analyses were performed. Spots showing decreased contents in stressed plants were shown to have strong similarities with a high-molecular glutenin gene, TraesCS1D02G317301 (TaHMW1D). QRT-PCR results confirmed that TaHMW1D was expressed in its full form and in the form of four different transcript variants. These events always occurred between repetitive regions at specific deletion sites (5′-CAA (Glutamine) GG/TG (Glycine) or (Valine)-3′, 5′-GGG (Glycine) CAA (Glutamine) -3′) in an exonic region. Heat stress led to a significant increase in the expression of the transcript variants. This was most evident in the distal parts of the spike. Considering the importance of high-molecular weight glutenin subunits of seed storage proteins, stressed plants might choose shorter polypeptides while retaining glutenin function, thus maintaining the expression of glutenin motifs and conserved sites.

scholarly journals A Single Seed Protein Extraction Protocol for Characterizing Brassica Seed Storage Proteins

Agronomy ◽  
2021 ◽  
Vol 11 (1) ◽  
pp. 107
Author(s):  
Mahmudur Rahman ◽  
Lei Liu ◽  
Bronwyn J. Barkla
Keyword(s):  
Seed Protein ◽  
Storage Proteins ◽  
Protein Extraction ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Protein Yield ◽  
Tissue Type ◽  
Single Seed ◽  
Material Optimization ◽  
Hazardous Chemical

Rapeseed oil-extracted expeller cake mostly contains protein. Various approaches have been used to isolate, detect and measure proteins in rapeseeds, with a particular focus on seed storage proteins (SSPs). To maximize the protein yield and minimize hazardous chemical use, isolation costs and the loss of seed material, optimization of the extraction method is pivotal. For some studies, it is also necessary to minimize or avoid seed-to-seed cross-contamination for phenotyping and single-tissue type analysis to know the exact amount of any bioactive component in a single seed, rather than a mixture of multiple seeds. However, a simple and robust method for single rapeseed seed protein extraction (SRPE) is unavailable. To establish a strategy for optimizing SRPE for downstream gel-based protein analysis, yielding the highest amount of SSPs in the most economical and rapid way, a variety of different approaches were tested, including variations to the seed pulverization steps, changes to the compositions of solvents and reagents and adjustments to the protein recovery steps. Following SRPE, 1D-SDS-PAGE was used to assess the quality and amount of proteins extracted. A standardized SRPE procedure was developed and then tested for yield and reproducibility. The highest protein yield and quality were obtained using a ball grinder with stainless steel beads in Safe-Lock microcentrifuge tubes with methanol as the solvent, providing a highly efficient, economic and effective method. The usefulness of this SRPE was validated by applying the procedure to extract protein from different Brassica oilseeds and for screening an ethyl methane sulfonate (EMS) mutant population of Brassica rapa R-0-18. The outcomes provide useful methodology for identifying and characterizing the SSPs in the SRPE.

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