Effects of Wheat Cultivar and Nitrogen Application on Storage Protein Composition and Breadmaking Quality

Influences of cultivar and nitrogen application on protein concentration and composition, and amount and size‐distribution of different protein components, were investigated in 10 spring wheat cultivars (Triticum aestivum L.) with widely varying gluten strength, grown under four nitrogen fertilizer conditions. The results showed that cultivar differences in gluten strength were determined by storage protein composition, differences in total amount of HMW glutenin subunits, the glutenin‐to‐gliadin ratio, and the relationship between SDS‐soluble and SDS‐insoluble protein polymers. Negative correlations were found between protein parameters related to gluten strength and bread volume. No cultivar stability for gluten strength in relation to differences in nitrogen application was found. Thus, the gluten strength was influenced by the nitrogen application in all the investigated cultivars. Increased nitrogen supply correlated significantly to an increase in all protein components containing gliadins and glutenins, but not to those containing albumins and globulins. The increase in protein components containing gliadins and glutenins correlated significantly with an increase in protein concentration and bread volume.     

Characterization of globulins from common vetch (Vicia sativa L.)

The proteins from Vicia sativa L. (common vetch) seeds were investigated. Protein comprises approximately 11.4% of the seed fresh weight, >50.8% of which is composed by globulins and 43.6% by albumins. The globulins may be fractionated into two main components, which were named alpha-vicinin (comprising 73% of the total globulin fraction, and hence >37% of the total seed protein) and beta-vicinin. Two minor globulin components are also present, gamma-vicinin and delta-vicinin. alpha-Vicinin, the legumin-like globulin, with a sedimentation coefficient of 10.6 S, is a nonglycosylated, disulfide-bond-containing globulin, composed of a group of subunits with molecular masses ranging from 50 to 78 kDa. Upon reduction, each of these subunits releases a heavy polypeptide chain (34-66 kDa) and a light polypeptide chain (21-23 kDa). beta-Vicinin, the vicilin-like globulin, with a sedimentation coefficient of 7.7 S, is a nonglycosylated globulin that contains no disulfide bonds and consists of two major polypeptides with molecular masses of 58 and 66 kDa. gamma-Vicinin is a minor, glycosylated, disulfide-bond-containing globulin. In the reduced form, it comprises six polypeptide chains with molecular masses of 12, 19, 21, 22, 23, and 31 kDa. Finally, delta-vicinin is a minor, highly glycosylated globulin that exhibits hemagglutinating activity. It is composed of a major 47 kDa polypeptide and two minor (33 and 38 kDa) polypeptides. N-terminal sequencing of the delta-vicinin 47 kDa polypeptide revealed no homology to any other known storage protein.     

Characterization of Protein Fractions of Rice Bran to Devise Effective Methods of Protein Solubilization

Proteins from the defatted brans of representative rice cultivars were fractionated into albumins, globulins, prolamins, and acid-soluble glutelins, accounting for 34, 15, 6, and 11% of the total bran proteins, respectively. The remaining insoluble residue protein, after treatment with 0.1M sodium hydroxide, resulted in the solubilization of 95% of the residue protein, representing 32% of the total bran protein. The relative molecular mass (M_r) values determined by size-exclusion HPLC were 10–100 kDa, 10–150 kDa, 33–150 kDa, and 25–100 kDa for the fully dissociated polypeptides of albumins, globulins, prolamins, and acid-soluble glutelins, respectively. Despite a breakdown of disulfide bonds of the residue protein during sodium hydroxide solubilization, the M_r of the majority of the fully dissociated polypeptides of this fraction ranged from 45 to 150 kDa. Insolubility of residue protein was due mainly to its strong aggregation and extensive disulfide bond cross-linking. Efficient methods may be developed for solubilizing up to 98% of rice bran protein by the use of dissociating and disulfide breaking agents currently in use in the food industry.     

Storage proteins from Lathyrus sativus seeds

The proteins from Lathyrus sativus Linn. (chickling vetch or grass pea) seeds were investigated. Protein constitutes approximately 20% of the seed dry weight, >60% of which is composed by globulins and 30% by albumins. A single, 24 kDa polypeptide comprises more than half of the protein present in the albumin fraction. The globulins may be fractionated into three main components, which were named alpha-lathyrin (the major globulin), beta-lathyrin, and gamma-lathyrin. alpha-Lathyrin, with a sedimentation coefficient of approximately 18S, is composed of three main types of unglycosylated subunits (50-66 kDa), each of which produce, upon reduction, a heavy and a light polypeptide chain, by analogy with 11S. beta-Lathyrin, with a sedimentation coefficient of 13S, is composed by a relatively large number of subunits (8-66 kDa). Two major polypeptides are glycosylated and exhibit structural similarity with beta-conglutin from Lupinus albus. One of these possesses an internal disulfide bond. gamma-Lathyrin, with a sedimentation coefficient of approximately 5S, contains two interacting, unglycosylated polypeptides, with no disulfide bonds: the major 24 kDa albumin and the heavier (20 kDa) polypeptide chain of La. sativus lectin.     

Electrophoretic patterns of seed globulins in the Old-WorldLupinus species

Summary Electrophoretic analysis of seed globulins was performed to investigate relationships between the Old-WorldLupinus species. The analysis covered 11 species described earlier and the recently reported taxon,Lupinus anatolicus nom. nud. With only two exceptions, particular species were represented by various accessions. In total, 110 accessions were examined. SDS-PAGE of reduced globulins was carried out in a discontinuous buffer system. The results showed a marked difference between the smooth-seeded and the rough-seeded species. In the group of smooth-seeded lupins pronounced interspecific differences were recorded. The rough-seeded species formed a rather homogenous group, well distinguishable from the smooth-seeded species. Though no distinct interspecific differences were recorded in the rough-seeded group, most of the 34 investigatedL. atlanticus accessions could be distinguished due to a characteristic, prominent polypeptide band with approx. M_r 27 kDa. The recently reported smooth-seeded taxon,L. anatolicus, showed a species-specific SDS-PAGE globulin pattern. Some of the presented results were announced in the form of a poster at the VIIth International Lupin Conference, Evora, Portugal, April 18–23,1993.     

Proteomic analysis of high protein soybean (Glycine max) accessions demonstrates the contribution of novel glycinin subunits

Limited biochemical information is available on soybean accessions that have seed protein content greater than 45% of the seed dry weight. SDS-PAGE analysis of seed proteins from nine soybean accessions revealed significantly higher amount of seed storage proteins in these accessions when compared with that of soybean cultivar Williams 82. High-resolution two-dimensional gel electrophoretic analysis of seed proteins revealed significant differences among several seed storage protein components in these accessions. A total of 51 protein spots were identified using peptide mass fingerprinting (MALDI-TOF MS). The contribution of these proteins to the overall protein content of the accessions was quantified using Delta2D image analysis software. Results showed that among the majority of the nine accessions, the largest difference in higher protein quantity was within the seed 11S storage globulins. The high protein trait from PI407788A was successfully transferred to an experimental line, LG99-469, demonstrating that this trait was transferable and robust.     

Proteolysis in model sourdough fermentations

Model wheat doughs started with six different lactic acid bacteria (LAB), with or without a commercial baker's yeast culture, were used to study proteolysis in sourdough fermentations. Cell counts, pH, and free amino acid concentration were measured. Sequential extraction of dough samples was performed to separate wheat proteins. The salt-soluble protein fraction (albumins and globulins) was analyzed by RP-HPLC and SDS-PAGE, whereas propanol-soluble (gliadins) and insoluble (glutenins) protein fractions were analyzed by SDS-PAGE only. Multivariate statistical methods were used for the analysis of results. The presence of yeasts and LAB affected RP-HPLC and SDS-PAGE patterns of the salt-soluble fraction in a complex way. The only changes in the gluten proteins that could be related to the presence of LAB were the appearance of new protein fragments (20 and 27 kDa) from gliadins and the degradation of high molecular weight glutenin subunits.     

Estimating Gliadin and Albumin Variation at Intra‐ and Interaccession Level in USDA Oriental Wheat (Triticum turgidum L. subsp. turanicum (Jakubz.) (A. Lőve & D. Lőve) Collection Using Capillary Zone Electrophoresis

Interest in so‐called ancient wheats (einkorn, emmer, oriental wheat, and spelt) has increased steadily in the last few decades. Oriental wheat (Triticum turgidum L. subsp. turanicum (Jakubz.) (A. Lőve & D. Lőve) is a neglected and underutilized tetraploid species that has survived over the centuries in some areas of the Near East and central Asia. Very little attention has been devoted by researchers to the evaluation and characterization of the oriental wheat germplasm. Knowledge of the variation of seed storage proteins within a germplasm collection is very useful for breeders interested in increasing the genetic bases of modern wheat cultivars. In this study, capillary zone electrophoresis (CZE) was used to analyze the gliadin and albumin extracts relative to 74 accessions belonging to the oriental wheat collection maintained at the USDA gene bank. Fourteen gliadin patterns were observed. Among the six most frequent patterns, one was widely predominant, being observed in 29 accessions, whereas eight were single types. Two profiles showing similar frequencies within the collection together with six single types were recognized for the albumins. The combination of the observed gliadin and albumin profiles gave rise to 25 combinations. In general, accessions collected in the same country shared the same combinations. This suggests that some accessions could be duplicates of the same genetic stock. Accessions collected in Iran and Turkey, which are indicated as the countries in which oriental wheat originated, were characterized by a higher degree of polymorphism.     

Effect of Nitrogen Fertilization on Quantity of Flour Protein Components,Dough Properties,and Breadmaking Quality of Wheat

Three winter wheat varieties with differing breadmaking quality were grown at two locations in two years at 0 or 3 × 60 kg of nitrogen application. The effect of nitrogen on amount of different components of gluten proteins was determined by reverse-phase HPLC. A high amount of nitrogen led generally to a significant increase of total protein content. However, this increase was obvious only for the gluten proteins; albumins and globulins remained nearly unaffected. The effect of increased protein content on gliadin to glutenin (gli-glu) ratio was inconsistent. While increased protein content increased the gli-glu ratio in the variety Capo, the opposite was true for the variety Renan. Gli-glu ratio of the variety Lindos showed no discernible tendency. As total protein content increased, the ratio of low molecular weight (LMW) to high molecular weight (HMW) glutenins decreased consistently, i.e., in all varieties, in both years and locations. Change of LMW to HMW ratio showed a significant negative correlation to sedimentation value and bread volume. There was no consistent change in the ratio between x- and y-type HMW subunits due to fertilization, as could be shown by densitometric measurements on SDS-PAGE gels. This ratio appeared to be dependent on the genotype and has decreased with decreasing quality. The amount of x-type subunits correlated closely with sedimentation value and bread volume. These results suggest that ratio of HMW glutenins, especially x-type subunits, to total protein content could be the best early detectable parameter with high predictive value for breadmaking quality.     

Diversity of seed globulins in Lathyrus sativus L. and some related species

Sodium dodecyl sulphate-polyacrylamide gel electrophoresis of reduced seed globulins covered 141 accessions of Lathyrus sativus and the following related species: L. amphicarpos, L. blepharicarpus, L. cicera, L. gorgoni, L. marmoratus, L. pseudocicera and L. stenophyllus. In the total examined material 71 globulin polypeptide bands were distinguished. The number of polypeptide bands detected in particular species varied from 14 in L. amphicarpos to 29 in L. sativus; all the species under study showed intraspecific variation due to individual variation and/or differences among accessions. Electrophoretic data were subjected to statistical analysis using hierarchical UPGMA grouping. Frequency distribution of polypeptide bands in L. sativus showed some correlations with geographical origin and certain seed characteristics (seed coat colour, seed weight) of the studied accessions. As regards interspecific relationships, the studied species showed to be distantly related taxa except for the rather closely allied L. cicera and L. marmoratus. The obtained results are compared with the electrophoretic seed albumin data reported earlier for the same taxa.     

Biochemical Characterization and Quantification of the Storage Protein (Secalin) Types in Rye Flour

Kernels of the rye cultivars Danko and Halo were milled into white flour and compared with flour of the wheat cultivar Rektor. Flour proteins were extracted stepwise with a salt solution (albumins‐globulins), 60% ethanol (prolamins), and 50% 2‐propanol under reducing conditions (glutelins). The quantification by reversed‐phase HPLC indicated that the extractable proteins of both rye flours consisted of ≈26% albumins‐globulins, 65% prolamins, and 9% glutelins. Compared with wheat flour, rye flours comprised significantly higher proportions of nonstorage proteins (albumins‐globulins) and lower proportions of polymerized storage proteins (glutelins). SDS‐PAGE revealed that the prolamin fractions of rye contained all four storage protein types (HMW, γ‐75k, ω, and γ‐40k secalins), whereas the glutelin fractions contained only HMW and γ‐75k secalins. The quantification of secalin types by RP‐HPLC showed a close relationship between the two cultivars.The γ‐75k secalins contributed nearly half (≈46%) of the total storage proteins, followed by γ‐40k secalins (24%) and ω secalins (17%); HMW secalins (≈7%) were minor components, and 6% of eluted proteins were not identified. The amino acid composition of γ‐40k secalins corresponded to those of γ‐gliadins of wheat, whereas γ‐75k secalins were characterized by higher contents of glutamine and proline. Matrix‐assisted laser desorption/ionization and time of flight mass spectrometry (MALDI‐TOF MS) indicated molecular masses of about 52,000 (γ‐75k) and 32,000 (γ‐40k), respectively. N‐terminal amino acid sequences were homologous with those of wheat γ‐ gliadins except for position 5 (asparagine in γ‐75k and glutamine in γ‐40k secalins) and position 12 (cysteine in γ‐75k secalins). The N‐terminal amino acid sequences of HMW and ω‐secalins were homologous with those of the corresponding protein types of wheat. Gel‐permeation HPLC of prolamin fractions revealed that rye flours contained a significantly higher proportion of ethanol‐soluble oligomeric proteins than wheat flour.     

Immunochemical and Electrophoretic Analysis of the Modification of Wheat Proteins in Extruded Flour Products

Antibodies specific for wheat proteins were used to identify protein fractions modified during extrusion of Hard Red Spring wheat flour (14% protein) under four different combinations of extrusion conditions (18 and 24% feed moisture and 145 and 175°C die temperature). Antibody binding was assessed on immunoblots of proteins extracted from flour and extrudates separated by SDS‐PAGE. Antibodies to high molecular weight glutenin subunits (HMW‐GS) and to B‐group low molecular weight glutenin subunits (LMW‐GS) recognized intact subunits from both flour and extrudates. Antibodies to C‐group LMW‐GS had diminished binding to extruded proteins. Glutenin‐specific antibodies also recognized protein in the extrudates migrating as a smear at molecular weights higher than intact subunits, indicating cross‐linked proteins. Antibodies recognized albumins or globulins in flour but not in extrudates, evidence that these fractions undergo significant modification during extrusion. Acid‐PAGE and antibody reaction of gliadins extracted in 1M urea and in 70% ethanol revealed total loss of cysteine‐containing α, β, γ‐gliadins but no obvious effects on sulfur‐poor ω‐gliadins, suggesting gliadin modification involves replacing intramolecular disulfides with intermolecular disulfide cross‐links. Identifying protein fractions modified during different extrusion conditions may provide new options for tailoring extrusion to achieve specific textural characteristics.     

Jojoba seed meal proteins associated with proteolytic and protease inhibitory activities

The jojoba, Simmondsia chinensis, is a characteristic desert plant native to the Sonoran desert. The jojoba meal after oil extraction is rich in protein. The major jojoba proteins were albumins (79%) and globulins (21%), which have similar amino acid compositions and also showed a labile thrombin-inhibitory activity. SDS-PAGE showed two major proteins at 50 kDa and 25 kDa both in the albumins and in the globulins. The 25 kDa protein has trypsin- and chymotrypsin-inhibitory activities. In vitro digestibility of the globulins and albumins resembled that of casein and soybean protein concentrates and was increased after heat treatment. The increased digestibility achieved by boiling may be attributed to inactivation of the protease inhibitors and denaturation of proteins.     

Patterns of diversity in Cannabis

Summary A Cannabis germplasm collection was evaluated for traits relevant to the use of hemp as an arable source of paper pulp. The traits were related to stem yield and quality, psychoactive potency, resistance to root-knot nematodes and plant morphology. The present study is directed at diversity for these traits considered together. For the interpretation of diversity patterns, accessions were grouped on the basis of the presumed purpose and status of domestication resulting in the recognition of four plant-use groups: fibre cultivars, fibre landraces, drug strains, and truly wild or naturalized populations. Principal component analysis showed that stem quality, phenological development, psychoactive potency and host reactions to root-knot nematodes explained most of the total variation among accessions. The plant-use groups were reasonably well separated in the principal component space. Discriminant analysis showed that the a priori defined plant-use groups could be discriminated quite well on the basis of linear combinations of all agronomic and morphological traits. The contents of bark fibre and cannabinoids had the highest grouping value. Reallocations concerned mainly old fibre cultivars which were placed in the group of fibre landraces due to a low content of bark fibre.A genetic characterization of accessions was based on electrophoretic patterns of seed proteins. Isoelectric ocusing patterns of bulk seed extracts showed variation for the presence of six out of 45 protein bands in the H range from 4.75 to 6.40. Banding patterns were however independent from any grouping based on origin or gronomic and morphological traits and did not reflect expected common ancestry of accessions.     

Characterization of Monomeric and Glutenin Polymeric Proteins of Hard Red Spring Wheats During Grain Development by Multistacking SDS-PAGE and Capillary Zone Electrophoresis

Three cultivars of hard red spring (HRS) wheats with identical high molecular weight (HMW) glutenin subunit composition (5+10 type, Glu-D1d) but different dough properties and breadmaking quality were used in this study. The synthesis and accumulation characteristics of different protein fractions during grain development were examined. Samples were collected at three-day intervals from anthesis to maturity between day 10 to day 37. The nonreduced SDS-extractable glutenin aggregates of developing grains were characterized by a multistacking SDS-PAGE procedure to obtain information on the size distribution and polymerization of glutenin aggregates. The HMW to low molecular weight (LMW) glutenin subunit ratio was determined for its relationship to polymerization of the various glutenin aggregates of different molecular sizes. Glutenin proteins were quantified using an imaging densitometer. In addition, albumins and globulins, α- and β-gliadins, γ-gliadins, and ω-gliadins were separated by capillary zone electrophoresis. The results indicated that albumins-globulins, gliadins, and glutenins in developing grains were present at 10 days after anthesis or earlier. Albumin-globulins decreased in proportion, while gliadins increased in proportion during grain development. Polymerization of glutenin aggregates occurred 10 days after anthesis or earlier and increased significantly throughout the grain-filling period until maturity. Larger aggregates of glutenin increased in proportion, while smaller ones decreased in proportion during grain development. Ratio of polymers to monomers increased significantly from day 10 to day 22 of grain development and then remained constant until grain maturity. Glutenin polymers arrived at their maximum in proportion to total SDS-extractable proteins or monomers at day 22 after anthesis while the molecular size of these polymers continued to increase, as indicated by a rapid increase in proportion of HMW to LMW glutenin subunits. Significant differences were found in accumulation rates of glutenin polymers among the three cultivars. Cultivars Kulm and Grandin, with better breadmaking quality, appeared to have greater rates of accumulation and HMW subunit synthesis or formation of larger polymers than did Sharp, a cultivar with poorer quality. Significant differences were found among the three cultivars in the proportion of albumins-globulins and gliadins during grain development. However, no significant differences were found among the cultivars in the proportion of albumins-globulins, α-, β-, γ-, and ω-gliadins at grain maturity. Varietal differences in breadmaking quality were due mainly to the differences in glutenin polymers such as ratio of polymeric to monomeric proteins, molecular size distribution, and ratio of HMW to LMW glutenin subunits among wheat cultivars of 2*, 7+9, and 5+10 subunit types. The better breadmaking cultivars might be characterized with higher proportions of glutenins and greater proportion of HMW subunits in total SDS-extractable proteins than the poorer quality cultivar. However, more genotypes need to be examined.     

Characterization of the soluble allergenic proteins of cashew nut (Anacardium occidentale L.)

The allergens associated with cashew food allergy have not been well-characterized. We sought to identify the major allergens in cashew nut by performing IgE immunoblots to dissociated and reduced or nonreduced cashew protein extracts, followed by sequencing of the peptides of interest. Sera from 15 subjects with life-threatening reactions to cashews and 8 subjects who tolerate cashews but have life-threatening reactions to other tree nuts were compared. An aqueous cashew protein extract containing albumin/globulin was separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and subjected to IgE immunoblotting using patient sera. Selected IgE reactive bands were subjected to N-terminal amino acid sequencing. Each of the 15 sera from cashew-allergic subjects showed IgE binding to the cashew protein extract. The dominant IgE-binding antigens in the reduced preparations included peptides in the 31-35 kD range, consistent with the large subunits of the major storage 13S globulin (legumin-like protein). Low-molecular-weight polypeptides of the 2S albumin family, with similarity to the major walnut allergen Jug r 1, also bound IgE. The sera from eight patients who tolerate cashew but displayed allergies to other tree nuts showed only minimal or no IgE binding to cashew. Cashew food allergy is associated with the presence of IgE directed against the major seed storage proteins in cashew, including the 13S globulin (legumin group) and 2S albumins, both of which represent major allergen classes in several plant seeds. Thus, the legumin-group proteins and 2S albumins are again identified as major food allergens, which will help further research into seed protein allergenicity.     

The influence of European and American wild germplasm in hop (<Emphasis Type="Italic">Humulus lupulus</Emphasis> L.) cultivars

Microsatellite variation at the nuclear and chloroplast genomes was evaluated for wild European and wild American hops, in order to assess the genetic diversity and origin of cultivated hops. Seven nuclear loci and 32 chloroplast loci were used in the analysis of 182 hop accessions including wild European (68), wild American (48), and cultivars (66). A total of 116 alleles were identified using 7 nuclear microsatellites showing different averages of polymorphism and distribution in the wild American and European accessions and cultivars. Two main groups were established as revealed by several statistical analyses; one including European wild accessions and cultivars and a second group consisting of American wild accessions. Three polymorphic chloroplast microsatellite loci were detected, six alleles were scored which defined a total of five haplotypes that were exclusive or presented different distribution between American and European wild accessions. A major influence of the wild European haplotypes was detected among hop cultivars. To the best of our knowledge, this is the first work reporting the use of chloroplast microsatellites in hops.     

Population diversity of the Vicia sativa agg. (Fabaceae) in the flora of the former USSR deduced from RAPD and seed protein analyses

The genetic diversity of 58 wild and weedy populations representing taxa within the V. sativa aggregate from the former USSR, 4 cultivars of V. sativa, 2 accessions of V. cordata and 3 accessions of V. macrocarpa from Mediterranean countries were analysed using randomly amplified DNA fragments (RAPDs) and seed protein electrophoresis (SDS-PAGE). Interspecific variation between taxa in the V. sativa aggregate could readily be detected using both techniques. RAPDs and seed protein patterns were found to be an effective means of identifying accessions that cannot be identified clearly by morphological criteria alone. RAPD and seed protein analysis revealed a clear relationship between observed genetic variation of populations and their geographical distribution. Populations from each region had their own gene pools. Geographical variation was detected in V. segetalis. The degree of genetic divergence between local populations was usually related to proximity. In several locations where wild and weedy populations of different V. sativa agg. taxa grow sympatrically, intermediate forms could be detected at the DNA and protein levels. Both RAPD and seed protein analysis support the view that the V. sativa aggregate consists of 8 taxa warranting recognition at the species level. Several species in this aggregate are evolving intra-specific groups which can readily be detected at the molecular level.     

Effect of Microbial Transglutaminase on Dough Proteins of Hard and Soft (Triticum aestivium) and Durum (Triticum durum) Wheat Cultivars

Microbial transglutaminase (MTGase), a protein‐glutamine γ‐glutamyl transferase (E.C. 2.3.2.13), catalyzes acyl transfer reactions by introducing a covalent cross‐link between l ‐lysine and l ‐glutamine residues. The use of this enzyme has been proposed as an improver to increase dough strength. The objective of this study was to assess and compare the effect of MTGase on different fractions of dough proteins found in hard, soft, and durum wheat. Three different concentrations of the MTGase (0, 5, and 10U/g of gluten) were tested. Moisture, protein, and dry gluten contents were determined for each concentration in addition to rheological measurements done with the farinograph. Following each treatment, the dough proteins were extracted and analyzed by SE‐HPLC and RP‐HPLC. Soluble polymeric protein, gliadins, albumins, and globulins were quantified in addition to the gliadin subclasses and glutenin subunit types. The combustion procedure was used to determine the amount of insoluble polymeric protein. Differences were observed in susceptibility to MTGase catalysis among the dough proteins of the cultivars studied: the cultivar Cortazar (soft wheat) was the most susceptible. The proteins of this cultivar had a characteristically higher amount of ω and α+β gliadins when compared with the other cultivars. As reported earlier, solubility of high molecular weight glutenin subunits and ω‐gliadins was reduced because of the MTGase treatment. However, all gliadin subclasses, including the γ and α+β gliadins, also participated in cross‐linking. The proteins of the cultivar Altar (durum wheat) were the least susceptible to the effects of MTGase. Albumins and globulins did not show any reduction in solubility, implying that they did not participate in cross‐linking.     

Characterization of yam bean (Pachyrhizus erosus) proteins

Seed proteins from Mexican yam bean seeds (Pachyrhizus erosus L.) were sequentially extracted according to the Osborne classification. Albumins were the major fraction (52.1-31.0%), followed by globulins (30.7-27.5%). The minor protein fraction was prolamins (0.8%). Defatting with chloroform/methanol remarkably affected the distribution of protein solubility classes; albumins were the most affected fraction (4.3-17.5%). Electrophoretic patterns of albumins showed bands at 55, 40, 35, and 31 kDa. After reduction of the globulin fraction exhibited two triplets, one from 35 to 31 kDa and the second from 19 to 21 kDa, these could be compared to the acid and basic polypeptides of 11S-like proteins. Prolamins showed one band at 31 kDa, and glutelins after reduction showed three main bands at 52, 27, and 14 kDa. Trypsin inhibitors were assayed in saline extracts; the values found (1232-2608 IU/g of meal) were lower than those of other legumes. In general, yam bean seed proteins showed an excellent balance of all essential amino acids; albumins contain the highest amount of essential amino acids.