Characterization of seed storage protein patterns of four Iranian Pistachios using SDS-PAGE (original) (raw)
Analysis of Seed Proteins in Groundnut Cultivars (Arachis hypogaea L
The seed protein contents and protein banding pattern were studied in commonly cultivated groundnut cultivars. The groundnut cultivars such as ICGV00351, TMV-7, CO-4,CO-6 and TG-374 were used for quantitative and qualitative analysis of seed proteins. The protein contents varied among the different varieties of groundnut. The maximum protein content was observed in CO-6 followed by CO-4, TMV-7, ICGV00351 and TG-374. There was a slight differences in protein content among the different cultivars. All the five cultivars of groundnut were subjected to SDS-PAGE analysis. The results revealed that the variation in total number of bands and MW-Rf values. The maximum number of MW-Rf value was noticed in TG-374 and ICGV00351, and the minimum MW-Rf value was 11 recorded in CO-6 and TMV-7.
Characterization and Identification of Seed Storage Protein of Twelve Lettuce Cultivars
Biosciences, Biotechnology Research Asia, 2016
We used SDS-PAGE to evaluate and characterize the protein patterns of seed storage proteins in 12 lettuce cultivars. Total protein content of lettuce seeds in all cultivars did not show any significant difference. Results of SDS-PAGE pattern of a few protein bands were up regulated whereas some other bands showed down regulation. The identified protein patterns may be used protein marker for lettuce cultivars. The seed storage protein analyses helps in characterization and identification of diversity in lettuce crop varieties, cultivars and their wild varieties and also provides information on phylogenetic relationship of the accessions. It is also known that variation in protein bands provide information on the relationship among the used seeds. SDS-PAGE of seed protein using Tris-glycine buffer was performed to study the relationships within 12 cultivars of Lactuca sativa L. (lettuce). In the present study, SDS-PAGE was used to investigate and characterize the protein patterns of seed storage proteins in order to find protein bands as markers for cultivar characterization. Data were analyzed by clustering method and similarity coefficients using NTSYSpc version 2.02i. Thevalidity of cluster analysis of SDS-PAGE seed proteins profile data was discussed.
Evaluation of some cereals, plants and tubers through protein composition
Journal of protein chemistry, 1999
Wild and cultivated maize, sorghum, rice, amaranth, soybean, and cassava were screened for variability in seed storage proteins. Total seed proteins, albumin (Alb-1 and Alb-2), globulin, alcohol-soluble (A1 and A2), and glutelin (G1 and G2) fractions were investigated by means of sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The comparison was done by the obtained protein patterns and their relative amounts. Using quantitative analysis of the protein composition and the electrophoretic patterns, the relationships between total proteins and amount of individual proteins were determined. Electrophoretic patterns of extracted proteins from investigated samples showed that the main protein subunits were concentrated between 10 and 45 kDa. Variation was found in major fractions and minor bands. Electrophoretic patterns of the protein fractions are directly related to the genetic background of the protein and can be identified and used to certify the genetic makeup...
Characterization of sunflower seed and kernel proteins
Helia, 2010
Total sunflower proteins, storage proteins, and helianthinin (11S) and 2S albumin fractions and their respective subunits in seeds and kernels of three sunflower hybrids were analyzed. Protein contents were analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and coupled with densitometry. The SDS-PAGE profiles of the seed and kernel proteins in the crude extracts for all genotypes showed a very similar number of protein bands (thirty two) in the electrophoretograms. Three polypeptide groups of helianthinin fraction were detected. Two of these were acidic (α, Mw = 36,800 -42,900 Da and α', Mw = 31,000 -35,300 Da), while one was basic (β, Mw=21,000 -29,600 Da). The molecular weight of the 2S albumin proteins ranged from 11,500 to 20,100 Da. According to our results, there were significant differences among the seed and kernel protein contents. The 2S albumin content was significantly higher in kernels than in whole seeds of sunflower hybrids (P<0.05). By contrast, the 11S helianthinin content was significantly higher in seeds (where it ranged from 61.75 to 67.70% of totally extracted proteins) than in kernels (varied from 57.36 to 61.51% of totally extracted proteins) of sunflower hybrids (P<0.05).
Comparative seed storage protein profiling of kabuli chickpea genotypes
Pak. J. Bot, 2009
Seed storage protein profiling of mung bean genotypes was performed by SDS-PAGE. Total soluble seed proteins from mung bean seeds were resolved on 12% gels in 22 protein polypeptide bands with molecular weights ranging from 16 to 103 kDa. Very low level of variability was observed in tested genotypes. Dendrogram based on electrophoretic data grouped the 13 genotypes into three clusters at 93% homology. A total of 5 genotypes (NM 13-1, NM 2006, NM 92, Chakwal 97 and Mung 88) were grouped together in the cluster-1. The 2 nd cluster consisted of one genotype i.e. AZRI 2006 which was most divergent in the tested germplasm. Seed storage peptide i.e., MSSP-19 differentiated the genotype, AZRI 2006 from rest of tested genotypes and thus can be used for its identification. Remaining seven genotypes grouped together in the 3 rd cluster. Based on seed storage protein marker i.e. MSSP-82, NM 2006, can also be differentiated from one of its parent genotype i.e., NM 92. Uniprot and NCBI protein databases were searched for already reported and characterized seed storage proteins in mung bean. Based on information retrieved from the databases and search engines, the resolved protein peptides mainly belong to 8S and 7S vicilin, 2S and 11S globulin and 2S albumin. In conclusion, electrophoresis (SDS-PAGE) of seed storage proteins provided an economic way to assess genetic variation in mung bean germplasm.
The aim of the experiment was to study the effect of germination on the three varieties of horse gram seed storage proteins. Seeds were germinated for 24, 48, 72, 96 and 110h in a dark place. Germinated seeds were frozen at -18 0 C for 12h to stop the germination process. Spouted seeds were freeze-dried and ground to pass through a 40 mesh sieve for analysis. Total proteins, water soluble and water insoluble proteins were estimated by standard methods. Seed storage protein profiles of three varieties germinated horse gram were analysed by sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE). Extracted protein fractions from germinated horse gram seeds in different solvents were studied by HPLC. The highest amount of storage protein degradation was observed in all varieties after 72-80h of germination. Characterization of protein fractions by HPLC showed that albumins/globulins, prolamins and glutelins increases slightly during germination time, as germinating seeds usually accompany by interconversion and production of new compounds. Electrophoregrams for each variety were shown and the high molecular weight proteins band intensity decreases during different germination period were noted. Genetic diversity of germinated horse gram was evaluated by constructing the dendrogram for high molecular weight (HMW) and low molecular weight (LMW) gluten subunit bands. In conclusion, SDS-PAGE of germinated seed storage proteins can be economically used to assess genetic variation and relation in germplasm. The specific bands of germinated seed storage protein profiles may be used as markers for identification of the mutants/genotypes.
Profile and Functional Properties of Seed Proteins from Six Pea (Pisum sativum) Genotypes
International Journal of Molecular Sciences, 2010
Extractability, extractable protein compositions, technological-functional properties of pea (Pisum sativum) proteins from six genotypes grown in Serbia were investigated. Also, the relationship between these characteristics was presented. Investigated genotypes showed significant differences in storage protein content, composition and extractability. The ratio of vicilin:legumin concentrations, as well as the ratio of vicilin + convicilin: Legumin concentrations were positively correlated with extractability. Our data suggest that the higher level of vicilin and/or a lower level of legumin have a positive influence on protein extractability. The emulsion activity index (EAI) was strongly and positively correlated with the solubility, while no significant correlation was found between emulsion stability (ESI) and solubility, nor between foaming properties and solubility. No association was evident between ESI and EAI. A moderate positive correlation between emulsion stability and foam capacity was observed. Proteins from the investigated genotypes expressed significantly different emulsifying properties and foam capacity at different pH values, whereas low foam stability was detected. It appears that genotype has considerable influence on content, composition and OPEN ACCESS technological-functional properties of pea bean proteins. This fact can be very useful for food scientists in efforts to improve the quality of peas and pea protein products.
2015
To survey of genetic relation and diversity among peanut genotypes, 11 cultivars of peanut were planted in the year 2013 at a research farm in Lasht-e Nesha in randomized complete block design with three replications. Protein bands were analyzed with the Total lab software and results showed that the 17 visible major bands were showed on the vertical gel. Increase of expression levels in a specific protein (band No.11 approximately 26 kDa weight) was expressed in all cultivars. Cluster analysis with UPGMA method on the basis of protein bands and cut the dendrogam at 50% similarity, divided the cultivars in 4 groups. According to the results, Genotypes 7, 8, 9, 10 and 11 in the first group, genotype 3, 4 and 5 in the second groups and Genotypes 1 and 2, were in the third and fourth groups separately. In general, the results of this study showed that the seed storage proteins of peanut cultivars were suitable for evaluation of genetic diversity and dividing the cultivars in separately...
Nutrients
There are growing public health movements to transition towards diets that are plant-based. However, confusion exists with concerns that plant-based proteins (including nuts) may be inferior with respect to protein quality. The present publication evaluates the evolution of protein quality concepts and explains the protein science related to pistachios. Pistachio nuts are a plant-based complete protein providing all nine EAAs in addition to an array of nutrients and phytochemicals. They have a PDCAAS of 73 and 81%, (raw and roasted pistachios, respectively), higher than that of many other tree nuts. From an environmental perspective transitioning towards plant-based diets (including nuts) could have potential to reduce total/green water footprints. Dietary guidelines are evolving yet nuts such as pistachios do not always have a clear place within these. Now appears to be a pertinent time to look at protein quality from the perspective of whole daily diets and dietary patterns, facto...