Chemical composition of forage watermelon fruit at different maturity stage or storage length

This study aimed to assess the chemical responses of forage watermelon fruit at different maturity stages or storage lengths, performing two experimental tests. In the first test, four maturity stages were assessed: 30, 45, 60, and 75 days after anthesis, with four replicates. In the second test, fruits were maintained under three storage lengths: T1D (harvest day), T3M (3 months after harvest), and T6M (6 months after harvest), with eight replicates. Experimental design was completely randomized in both experimental tests. Fruit maturity stage did not affect crude protein, total carbohydrate, neutral detergent fiber, in vitro dry matter digestibility (IVDMD), pulp firmness, soluble solids content and total pectin content, but increased acid detergent fiber content from 45 days after anthesis. Storage length up to six months after harvest increased ash, crude protein and IVDMD, and reduced the content of soluble solids. Forage watermelon fruit can be harvested from 30 to 75 days after anthesis equivalent to 75 - 120 days after planting, and they can be stored under tree shade up to 6 months after harvest.(AU)

Sulfur modulates yield and storage proteins in soybean grains

This study evaluated the nutritional quality, yield, and storage protein modulation in soybean grains in response to levels and sources of sulfur (S) in a dystrophic Ultisol. We used five levels of S (0, 50, 100, 150 and 200 mg kg –1 ) and four sources of S (elemental S pastille - ESPA, gypsum - GY, gypsite - GI and elemental S powder - ESPO). Plants treated with 50 mg kg –1 of GY, GI, and ESPO and 200 mg kg –1 of ESPA had the largest grain yield values. Low S supply resulted in lower yields for all S sources tested. Sulfur deficiencies were observed at all levels for ESPA, resulting in lower concentrations of globulin and higher concentration of glutelin and albumin in the grains, possibly because the S content in the leaf was below the range adequate for soybean, leading to in lower yield values. In general, the application of S sources (GY, GI, and ESPO) increased all protein fractions. The results show that proper application of S is essential to optimize soybean yield and increase storage proteins in the grains. The granulometry of ESPA and ESPO fertilizers was a key factor for the availability of S to soybean plants. This study presents relevant information on S fertilization of soybeans, which could provide better grain nutritional quality and increased storage proteins with benefits to animal health.

Sulfur modulates yield and storage proteins in soybean grains

This study evaluated the nutritional quality, yield, and storage protein modulation in soybean grains in response to levels and sources of sulfur (S) in a dystrophic Ultisol. We used five levels of S (0, 50, 100, 150 and 200 mg kg –1 ) and four sources of S (elemental S pastille - ESPA, gypsum - GY, gypsite - GI and elemental S powder - ESPO). Plants treated with 50 mg kg –1 of GY, GI, and ESPO and 200 mg kg –1 of ESPA had the largest grain yield values. Low S supply resulted in lower yields for all S sources tested. Sulfur deficiencies were observed at all levels for ESPA, resulting in lower concentrations of globulin and higher concentration of glutelin and albumin in the grains, possibly because the S content in the leaf was below the range adequate for soybean, leading to in lower yield values. In general, the application of S sources (GY, GI, and ESPO) increased all protein fractions. The results show that proper application of S is essential to optimize soybean yield and increase storage proteins in the grains. The granulometry of ESPA and ESPO fertilizers was a key factor for the availability of S to soybean plants. This study presents relevant information on S fertilization of soybeans, which could provide better grain nutritional quality and increased storage proteins with benefits to animal health.(AU)

Agronomic biofortification with selenium impacts storage proteins in grains of upland rice.

BACKGROUND: Selenium (Se) is an essential element for humans and animals. Rice is one of the most commonly consumed cereals in the world, so the agronomic biofortification of cereals with Se may be a good strategy to increase the levels of daily intake of Se by the population. This study evaluated the agronomic biofortification of rice genotypes with Se and its effects on grain nutritional quality. Five rates of Se (0, 10, 25, 50, and 100 g ha -1 ) were applied as selenate via the soil to three rice genotypes under field conditions. RESULTS: Selenium concentrations in the leaves and polished grains increased linearly in response to Se application rates. A highly significant correlation was observed between the Se rates and the Se concentration in the leaves and grains, indicating high translocation of Se. The application of Se also increased the concentration of albumin, globulin, prolamin, and glutelin in polished grains. CONCLUSION: Biofortifying rice genotypes using 25 g Se ha -1 could increase the average daily Se intake from 4.64 to 66 µg day-1 . Considering that the recommended daily intake of Se by adults is 55 µg day-1 , this agronomic strategy could contribute to alleviating widespread Se malnutrition. © 2019 Society of Chemical Industry.

Natural Variability of Allergen Levels in Conventional Soybeans: Assessing Variation across North and South America from Five Production Years.

Soybean (Glycine max L. Merrill) is one of eight major allergenic foods with endogenous proteins identified as allergens. To better understand the natural variability of five soybean allergens (Gly m 4, Gly m 5, Gly m 6, Gly m Bd 28k, and Gly m Bd 30k), validated enzyme-linked immunosorbent assays (ELISAs) were developed. These ELISAs measured allergens in 604 soybean samples collected from locations in North and South America over five growing seasons (2009-2013/2014) and including 37 conventional varieties. Levels of these five allergens varied 5-19-fold. Multivariate statistical analyses and pairwise comparisons show that environmental factors have a larger effect on allergen levels than genetic factors. Therefore, from year to year, consumers are exposed to highly variable levels of allergens in soy-based foods, bringing into question whether quantitative comparison of endogenous allergen levels of new genetically modified soybean adds meaningful information to their overall safety risk assessment.

Chemical compounds related to nutraceutical and industrial qualities of non-transgenic soybean genotypes.

BACKGROUND: Information about the chemical profile of soybean seed is valuable for breeding programs aimed at obtaining value-added products to meet the demands of niche markets. The objective of this study was to determine seed composition of non-transgenic soybean genotypes with specialty characters in different environments of Argentina. RESULTS: Protein and oil contents ranged from 396 to 424 g kg⁻¹ and from 210 to 226 g kg⁻¹, respectively. Oleic and linolenic acid ratio, the general indicator of oil quality, varied from 2.7 to 3.8. The oil contained high levels of total tocopherols (1429-1558 mg kg⁻¹) and the meal exhibited high levels of total isoflavones (2.91-4.62 mg g⁻¹). The biplot showed that oleic, linoleic and linolenic acids, γ-, δ- and total tocopherols, genistin, malonyl daidzin and genistin, acetyl daidzin and glycitin and total isoflavones allowed the greatest discrimination among the genotypes studied. CONCLUSION: Different chemical profiles of each non-transgenic genotype analyzed were established and, therefore, their identity was defined. These results are important for breeders who intend to obtain new genotypes with improved meal and oil quality, as well as for processors and exporters, who could use them directly as raw material for soyfood processing for nutraceutical purposes.

Comparative proteomic analysis of off-type and normal phenotype somatic plantlets derived from somatic embryos of Feijoa (Acca sellowiana (O. Berg) Burret).

Morphological disorders in a relevant portion of emerged somatic embryos have been a limiting factor in the true-to-type plantlet formation in Acca sellowiana. In this sense, the present study undertook a comparison between normal phenotype and off-type somatic plantlets protein profiles by means of the 2-D DIGE proteomics approach. Off-type and normal phenotype somatic plantlets obtained at 10 and 20 days conversion were evaluated. Results indicated 12 exclusive spots between normal and off-type plantlets at 10 days conversion, and 17 exclusive spots at 20 days conversion. Also at 20 days conversion, 4 spots were differentially expressed, up- or down-regulated. Two proteins related to carbohydrate metabolism were only expressed in off-types at 10 days conversion, suggesting a more active respiratory pathway. A vicilin-like storage protein was only found in off-types at 20 days conversion, indicating that plantlets may present an abnormality in the mobilization of storage compounds, causing reduced vigor in the development of derived plantlets. The presence of heat shock proteins were only observed during formation of normal phenotype somatic plantlets, indicating that these proteins may be involved in normal morphogenesis of plantlets formed. These new findings shed light on possible genetic or epigenetic mechanisms governing A. sellowiana morphogenesis.

Biochemical aspects of a serine protease from Caesalpinia echinata Lam. (Brazilwood) seeds: a potential tool to access the mobilization of seed storage proteins.

Several proteins have been isolated from seeds of leguminous, but this is the first report that a protease was obtained from seeds of Caesalpinia echinata Lam., a tree belonging to the Fabaceae family. This enzyme was purified to homogeneity by hydrophobic interaction and anion exchange chromatographies and gel filtration. This 61-kDa serine protease (CeSP) hydrolyses H-D-prolyl-L-phenylalanyl-L-arginine-p-nitroanilide (K(m) 55.7 µM) in an optimum pH of 7.1, and this activity is effectively retained until 50 °C. CeSP remained stable in the presence of kosmotropic anions (PO(4) (3-), SO(4) (2-), and CH(3)COO(-)) or chaotropic cations (K(+) and Na(+)). It is strongly inhibited by TLCK, a serine protease inhibitor, but not by E-64, EDTA or pepstatin A. The characteristics of the purified enzyme allowed us to classify it as a serine protease. The role of CeSP in the seeds cannot be assigned yet but is possible to infer that it is involved in the mobilization of seed storage proteins.

One-step multiplex PCR method for the determination of pecan and Brazil nut allergens in food products.

BACKGROUND: A one-step polymerase chain reaction (PCR) method for the simultaneous detection of the major allergens of pecan and Brazil nuts was developed. Primer pairs for the amplification of partial sequences of genes encoding the allergens were designed and tested for their specificity on a range of food components. RESULTS: The targeted amplicon size was 173 bp of Ber e 1 gene of Brazil nuts and 72 bp of vicilin-like seed storage protein gene in pecan nuts. The primer pair detecting the noncoding region of the chloroplast DNA was used as the internal control of amplification. The intrinsic detection limit of the PCR method was 100 pg mL(-1) pecan or Brazil nuts DNA. The practical detection limit was 0.1% w/w (1 g kg(-1)). The method was applied for the investigation of 63 samples with the declaration of pecans, Brazil nuts, other different nut species or nuts generally. In 15 food samples pecans and Brazil nuts allergens were identified in the conformity with the food declaration. CONCLUSION: The presented multiplex PCR method is specific enough and can be used as a fast approach for the detection of major allergens of pecan or Brazil nuts in food.

Effects of calcium and pressure treatment on thermal gelation of soybean protein.

The effect of calcium and high-pressure (HP) treatment on the heat gelation of soybean proteins was investigated. In the presence of calcium (2 to 25 mM), the gelation of dispersions of soybean protein isolate (SPI), a beta-conglycinin-enriched fraction (7SEF), and a glycinin-enriched fraction (11SEF) started with protein having a lower degree of denaturation. The gels from these dispersions had greater stiffness than the samples without added calcium. HP treatment had different effects on heat-induced gelation depending on the presence of calcium and on the nature of the proteins. In the absence of calcium, gels with low stiffness were formed after HP treatment, compared with untreated samples, and regardless of the sample type (SPI, 7SEF, 11SEF). In the presence of calcium, gel stiffness was increased after HP treatment of dispersions containing beta-conglycinin (SPI and 7SEF), while the opposite effect was observed for 11SEF. In the presence of calcium, HP treatment promoted a greater contribution of hydrophobic interactions in SPI and 7SEF. In the dispersions containing beta-conglycinin, these conditions also promoted the appearance of a heterogeneous distribution of molecular sizes, from enormous aggregates to dissociated species. Our results suggest that, in the presence of calcium, HP treatment has an opposite effect on the ability of glycinin and beta-conglycinin to participate in the formation of a 3-dimensional network upon heating.

Comparative proteomical analysis of zygotic embryo and endosperm from Coffea arabica seeds.

During coffee seed development, proteins are predominantly deposited in cotyledons and in the endosperm. Reserve proteins of the 11S family are the most abundant globulins in coffee seeds, acting as a nitrogen source during roasting and guaranteeing flavor and aroma. The aim of the present study was to compare the protein profiles of endosperm and zygotic embryos of coffee seeds. Proteins were extracted from whole seed as well as from embryo and endosperm, separately. Total proteins were analyzed by two-dimensional electrophoresis (2-DE) followed by identification by mass spectrometry (MS). The most abundant spots observed in the gels of coffee seeds were excised, digested with trypsin, and identified by MS as subunits of the 11S globulin. Spots with identical pI and molecular masses were also observed in the protein profiles of coffee endosperm and embryo, indicating that 11S protein is also highly expressed in those tissues. Peptide sequence coverage of about 20% of the entire 11S globulin was obtained. Three other proteins were identified in the embryo and endosperm 2-DE profiles as a Cupin superfamily protein, an allergenic protein (Pru ar 1), exclusive to the endosperm 2D map, and a hypothetical protein, observed only in the zygotic embryo profile.