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.     

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.     

Surface physicochemical properties of globulin-P amaranth protein

Globulin-P, the polymerized 11S amaranth globulin, is composed of 280 kDa unitary molecules (UM, 23%) and aggregates larger than 500 kDa (A, 70%). Antibodies against these proteins were prepared to study their surface characteristics and to assess their homology with other storage proteins. Results showed that globulin-P unitary molecules and aggregates had similar reactive surfaces. A polypeptide of 56 kDa was found to be the most reactive to the antibodies assayed, followed by the acidic polypeptides. Such results support previous information, according to which these polypeptides appeared to be the most exposed on the molecule surface. Globulin-P fraction presented cross-reactivity with the remaining amaranth protein fractions: 11S-globulin, glutelins, and albumins. Globulin-P and 11S-globulin showed similar reactive surfaces whereas glutelin and albumins presented a lower cross-reactivity. The reactivity of the glutelin fraction depended on its sequence. Globulin-P fraction presented cross-reactivity with quinoa globulins, and to a lesser extent with globulins of sunflower and rice. Moreover, the anti-Gp serum was unable to detect either conformational or sequence epitopes in globulins of soybean, wheat, buckwheat, rice, and rye.     

Proteome profiling of seed storage proteins reveals the nutritional potential of Salicornia brachiata Roxb., an extreme halophyte

Salicornia brachiata is an extreme halophyte that grows in salty marshes and is considered to be a potential alternative crop for seawater agriculture. Salicornia seeds are rich in protein, and its tender shoots are eaten as salad greens. Seed storage proteins were fractionated by sequential extraction using different solvents, including distilled water for albumins, NaCl (1.0 M) for globulins, NaOH (0.1 N) for glutelins, and ethanol (70% v/v) for prolamins. Globulins accounted for 54.75% of the total seed storage proteins followed by albumins (34.30%) and glutelins (8.70%). The fractionated proteins were characterized using 2D-diagonal SDS-PAGE and matrix-assisted laser desorption/ionization-time of flight (MALDI-TOF) mass spectrometry. The globulin fraction, composed of seven intermolecular disulfide-linked polypeptide pairs of molecular mass 63.5, 62.5, 54.7, 53.0, 43.2, 38.5, and 35.1 kDa, encompassed a basic and an acidic subunit. Two-dimensional gels revealed approximately 32 spots, with isoelectric points and molecular masses ranging from 4.93 to 11.6 and from ～5.2 to ～109.4 kDa, respectively. Protein spots were identified by MALDI-TOF MS peptide mass fingerprint analysis and further classified. Homology analysis demonstrated that 19% of the proteins were involved in metabolism, 16% were involved in signaling, and 15% were regulatory proteins. Peptide mass fingerprint analysis confirmed the presence of inter- and intramolecular disulfide linkages in the globulin fraction. Sulfur-rich proteins are of high nutritional value, and disulfides make S. brachiata a potential source of dietary supplementation.     

Protein Distribution Pattern in Floury and Vitreous Endosperm of Maize Grain

Alpha‐amino nitrogen compounds of floury and vitreous parts of hand‐dissected endosperm from eight maize (Zea mays L.) inbred lines, representing a broad range of vitreousness (42–95%), were isolated as nonprotein nitrogen, albumin‐globulins, zeins, and true glutelins. The three protein classes averaged, respectively, 13, 48, and 35% of total nitrogen in floury endosperm, and 4, 79, and 15% of that in vitreous endosperm. For six inbreds, floury endosperm was richer in 27 kDa γ‐zein than vitreous endosperm; the reverse was found for an Argentine flint inbred (ARGL 256), and only traces of 27 kDa γ‐zein occurred in both floury and vitreous endosperm of inbred F113. Results were compared with protein distribution patterns reported in the literature of whole endosperm of wild‐type and mutant genotypes of maize, and with wild relatives of maize, Tripsacum, and teosintes. When percentage of salt‐soluble nitrogen increased from 2% (Tripsacum) to 22% (in double mutant Oh43o2;bt2), zeins decreased from 87 to 22%, and true glutelins increased from 11 to 57%. The pattern of whole endosperm of Zea perennis was very similar to that of the vitreous endosperm of line ARGL 256. The mean pattern for whole endosperm of six o2 inbred lines was identical to that of floury endosperm of eight wild‐type lines, consistent with a lack of synthesis of α‐zeins due to the mutation in the O2 gene.     

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.     

Characterization of protein fractions from Bt-transgenic and non-transgenic maize varieties using perfusion and monolithic RP-HPLC. Maize differentiation by multivariate analysis

Protein fractions from transgenic Bt and non-transgenic maize varieties, extracted by the Osborne solvent fraction procedure, were characterized for the first time by perfusion and monolithic RP-HPLC in very short analysis times. Albumins and globulins from different transgenic Bt maizes as well as from their non-transgenic isogenic varieties were eluted in four peaks using perfusion RP-HPLC, whereas prolamins and glutelins were separated in seven peaks. Monolithic RP-HPLC enabled the separation of maize proteins in a large number of peaks showing 6 and 10 main peaks for albumins and globulins, respectively. Prolamins migrated at retention times higher than 5 min as seven peaks, whereas glutelins were separated in three main peaks appearing at retention times higher than 6.0 min. Moreover, chromatograms of the whole protein extracts showed 8 and 11 components for perfusion and monolithic RP-HPLC, respectively. A comparison of the chromatograms of the whole protein extracts relative to transgenic and non-transgenic varieties evidenced quantitative differences on the percentages of area, mainly for peaks 2 and 3 by perfusion RP-HPLC and for peaks 3 and 7 by monolithic RP-HPLC. A discriminant analysis based on these proteic profiles was carried out to classify and predict transgenic Bt maize lines, achieving 100% correct classification using perfusion RP-HPLC.     

Effect of Transglutaminase on Protein Electrophoretic Pattern of Rice,Soybean, and Rice‐Soybean Blends

The interactions taking place in composite dough containing rice flour and soybean proteins (5% w/w) in the presence of transglutaminase, an enzyme with cross‐linking activity, were studied using different electrophoretic analyses. The interaction between rice proteins and soybean proteins was intensified by the formation of new intermolecular covalent bonds catalyzed by transglutaminase and the indirect formation of disulfide bonds among proteins. The main protein fractions involved in those interactions were both β‐conglycinin and glycinin of soybean and the glutelins of the rice flour, although albumins and globulins were also cross‐linked. The addition of soybean proteins to rice flour improves the amino acid balance and they also might play an important role on the rice dough properties because soybean proteins interact with rice proteins, yielding protein aggregates of high molecular weight.     

Flour Protein Composition and Functional Properties of Transgenic Rye Lines Expressing HMW Subunit Genes of Wheat

Flours from nonsprouted (ns) kernels and dried sprouted (s) kernels of transgenic rye expressing HMW glutenin subunits (HMW‐GS) 1Dy10 (L10) or 1Dx5+1Dy10 (L5+10) from wheat were compared with flours from the corresponding wildtype rye (Lwt). The crude protein content of nonsprouted flours ranged from 9.2% (Lwt) to 10.4% (L5+10) and was lowered by ≈1% due to sprouting. Flour proteins were separated into albumins/globulins, prolamins, and glutelin subunits by a modified Osborne fractionation and into SDS‐soluble and insoluble fractions. Portions of the prolamin fractions were reduced in the same manner as glutelins. The different fractions were then characterized and quantified by RP‐HPLC on C₈ silica gel. The proportion of albumins/globulins did not significantly differ between transgenic lines and wildtype. The proportions of alcohol‐insoluble glutelins and SDS‐insoluble proteins drastically increased in transgenic rye due to a shift of HMW and γ‐75k secalins into the polymeric fractions. Significant differences in the proportion of highly polymeric proteins between nonsprouted and sprouted flours could not be detected. The quantitative data demonstrated that the expression of HMW‐GS led to a higher degree of polymerization of storage proteins in rye flour. The HMW‐GS combination 1Dx5+1Dy10 showed stronger effects than 1Dy10 alone. The analyzed flours contained two HMW secalins (R1, R2), whose amino acid compositions were closely related to those of 1Dy10 and 1Dx5, respectively. The amounts of R1 in Lwt flours determined by RP‐HPLC were 221 mg (ns) and 186 mg (s) per 100 g and those of R2 were 344 mg (ns) and 298 mg (s), respectively. These amounts increased to 240 mg (ns)/201 mg (s) (R1) and 479 mg (ns)/432 mg (s) (R2) in L10 flours. In L5+10 flours, the amount of R1 decreased to 150 mg (ns)/132 mg (s) while R2 increased to 432 mg (ns)/338 mg (s). The amount of HMW‐GS 1Dy10 was almost the same as that of R2 in L10 flours but was strongly increased in L5+10 flour (633 mg [ns]/538 mg [s]). HMW‐GS 1Dx5 was, by far, the major subunit in L5+10 flours (987 mg 7[ns]/896 mg [s]). The summarized amounts of all HMW subunits increased from ≈0.5 g (Lwt) to ≈1.1 g (L10) and ≈2.0 g (L5+10). Thus only L10 flours were similar to wheat flours in HMW subunit content. The baking performance of L10 flour determined by a microbaking test was improved compared with Lwt flour, whereas L5x10 flour showed very poor properties obviously due to the strongly increased proportion of highly cross‐linked glutelins. The breadmaking quality of flours from 1Dy10 seeds and wildtype seeds was reduced by the same degree when flours from sprouted seeds were analyzed.     

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 the proteins from Vigna unguiculata seeds

The proteins from Vigna unguiculata (L.) Walp. (cowpea) seeds were investigated. Globulins constitute over 51% of the total seed protein, with albumins composing approximately 45%. The globulins may be fractionated by native electrophoresis or anion exchange chromatography into three main components, which were termed (in decreasing order of anodic mobility) alpha-vignin, beta-vignin, and gamma-vignin. alpha-Vignin, with a sedimentation coefficient of 16.5S, is a major, nonglycosylated globulin, composed of a major 80 kDa subunit, which upon reduction, produces two polypeptides (20 and 60 kDa). beta-Vignin, with a sedimentation coefficient of 13S, is a major, glycosylated globulin, composed of two main polypeptides (55 and 60 kDa) with no disulfide bonds. Finally, gamma-vignin, a minor globulin, is composed by one main type of subunit (22 kDa), which upon reduction, is converted into a single, apparently heavier polypeptide chain (30 kDa) due to the presence of an internal disulfide bond. Immunological analyses revealed structural homology between beta-vignin and beta-conglutin (the vicilin from Lupinus seeds) but not between alpha- or gamma-vignins and their Lupinus counterparts. Haemagglutination activity toward trypsinized rabbit erythrocytes was found exclusively in the albumin fraction and was strongly inhibited by N-acetylglucosamine or chitin.     

Uptake and Distribution of Arsenic in Chickpea: Effects on Seed Yield and Seed Composition

Chickpea plants were grown in arsenic (As)–contaminated soils (5 mg kg^?1 of dry soil) and investigated for As uptake, distribution, and effects on growth, yield, and quality of seeds. The roots accumulated the greatest As (7 mg kg^?1 dry weight), followed by stem (4.8 mg), leaves (4.0 mg), and seeds (0.7 mg). Arsenic inhibited the growth of the roots and shoots (as dry weight) by 65% and 60%, respectively, over controls. The shoot/root ratio declined from 4.3 in the control to 3.5 in As-treated plants. The seed yield (g) and number of pods plant^?1 decreased by 66 and 53%, respectively, over controls. A marked increase in membrane damage coupled with reduction in chlorophyll and relative leaf water content occurred in As-treated plants. The contaminated plants showed 34% and 25% decrease over control in sucrose content in their leaves and seeds, respectively. The accumulation of seed reserves such as starch, proteins, sugars, and minerals was inhibited significantly due to As-treated plants. Storage proteins such as albumins, globulins, glutelins and prolamins decreased significantly with larger effect on glutelins. The contents of minerals such as calcium (Ca), phosphorus (P), and iron (Fe) declined greatly in the seeds of As-treated plants. The accumulation of amino acids such as lysine, methionine?+?cystine, phenylalanine?+?tyrosine, proline, threonine, tryptophan, and valine was inhibited significantly in the seeds of As-applied plants compared to the control. The findings indicated that As application markedly reduced the quality of the chickpea seeds, especially in terms of proteins and minerals.     

Predicting Protein Composition,Biochemical Properties,and Dough-Handling Properties of Hard Red Winter Wheat Flour by Near-Infrared Reflectance

Breadmaking quality in wheat is one of several considerations that plant breeders face when developing new cultivars. In routine breeding programs, quality is assessed by small-scale dough-handling and bake tests, and to some extent, by biochemical analysis of gluten proteins. An alternative, not yet fully examined, method for wheat flour quality assessment is near-infrared reflectance (NIR) spectrophotometry. The present study was performed on 30 genotypes of hard red winter wheat grown during two crop years at eight to nine locations in the Great Plains area of the United States. Biochemical testing consisted of measuring protein fractions from size-exclusion HPLC (M _r > 100k, M _r 25–100k, and M _r < 25k designated as glutenin, gliadins, and albumin and globulins, respectively), pentosan content, and SDS sedimentation volume. Dough-handling properties were measured on a mixograph and recorded as the time to peak dough development, the peak resistance, the width of the mixing curve, and the width of the curve at 2 min past peak. Partial least squares analyses on diffuse NIR spectra (1,100–2,498 nm) were developed for each constituent or property. When applied to a separate validation set, NIR models for glutenin content, gliadin content, SDS sedimentation volume, and mixograph peak resistance demonstrated reference vs. predicted correlations ranging from r = 0.87 to r = 0.94. Such models were considered sufficiently accurate for screening purposes in breeding programs. NIR spectra were responsive to each constituent or property at a level higher than expected from a correlation between the constituent or property and protein content (recognizing that protein content is modeled by NIR with high accuracy).     

Purification and Analysis of Wheat Grain Polyphenol Oxidase (PPO) Protein

Wheat (Triticum aestivum L.) breeding programs have used various whole kernel assays to estimate polyphenol oxidase (PPO) activity, thereby identifying germplasm that has a greater chance of producing consumer products with superior color. However, the enzymes involved in these assays are poorly understood and the purification and characterization of a wheat kernel PPO protein has not been reported previously. A PPO from wheat bran was purified using ammonium sulfate precipitation, ion and size‐exclusion chromatography, and continuous elution electrophoresis. The purified protein migrated at 67 kDa on SDS‐PAGE under denaturing and reducing conditions, exhibited PPO activity in the presence of SDS, and eluted at 45 kDa on SDS‐PAGE under nondenaturing and nonreducing conditions. N‐terminal sequence analysis of peptide fragments obtained from tryptic digests confirmed the purified wheat bran protein as a PPO. This wheat PPO protein showed the greatest sequence identity to grape (Vitis vinifera) and pineapple (Ananas comosus) PPO. The purified wheat PPO shares no more sequence identity with the deduced amino acid sequence of a previously isolated partial wheat PPO sequence than it does to PPO from other plant taxa widely divergent from wheat. Based on immunoblot analysis, purified PPO from wheat bran appears to be a processed, mature form lacking an estimated 14–16 kDa transit peptide required for plastid localization.     

油菜花粉谷蛋白酶解物的制备

以陈放1年的油菜蜂花粉为原料,对破壁脱脂后的花粉中各组分蛋白含量进行了研究,其中谷蛋白的含量约占总蛋白含量的55.7%,清蛋白为39.O%,球蛋白和醇蛋白只有3.2%和2.1%.以谷蛋白为原料,在单因素试验的基础上,利用响应面分析法对油菜花粉谷蛋白最佳酶解条件进行了研究.结果表明,Alcalase碱性蛋白酶水解油菜花粉谷蛋白的最佳水解条件为底物浓度6%,pH值9.0,水解温度60℃,酶底比1460U/g,水解时间2h,谷蛋白酶法改性后抗羟基自由基的活性能达到70.0%.     

Opportunities and Challenges in Processing of By‐product of Rice Milling Protein as a Food Ingredient

The by‐product of rice milling (BRM), known as commercial rice bran, is the coproduct of rice processing. It is a mixture of outer layers of the grain, the embryo, and some of the starchy endosperm, and these are separated from brown rice to produce white, milled rice. This mixture contains a high concentration of protein (12–20%) in comparison with that of brown rice (7.1–8.3%) or white rice (6.3–7.1%) and is therefore an abundant and cheap protein source. Nearly 70% of the proteins in BRM are albumins and globulins, which are high in solubility, digestibility, and nutritional value. The BRM proteins are hypoallergenic and gluten‐free. With these properties, this type protein has many advantages as a unique and valuable protein source in markets such as protein supplements. The BRM protein can be extracted by physical, alkali, and enzymatic methods, which give yields ranging from 13% to more than 90%. This review highlights the opportunities and challenges in processing of BRM protein as a food ingredient.     

Levels of Protein and Protein Composition in Hard Winter Wheat Flours and the Relationship to Breadmaking

Protein and protein fractions were measured in 49 hard winter wheat flours to investigate their relationship to breadmaking properties, particularly loaf volume, which varied from 760 to 1,055 cm³ and crumb grain score of 1.0–5.0 from 100 g of flour straight‐dough bread. Protein composition varied with flour protein content because total soluble protein (SP) and gliadin levels increased proportionally to increased protein content, but albumins and globulins (AG), soluble polymeric proteins (SPP), and insoluble polymeric protein (IPP) levels did not. Flour protein content was positively correlated with loaf volume and bake water absorption (r = 0.80, P < 0.0001 and r = 0.45, P < 0.01, respectively). The percent SP based on flour showed the highest correlation with loaf volume (r = 0.85) and low but significant correlation with crumb grain score (r = 0.35, P < 0.05). Percent gliadins based on flour and on protein content were positively correlated to loaf volume (r = 0.73, P < 0.0001 and r = 0.46, P < 0.001, respectively). The percent IPP based on flour was the only protein fraction that was highly correlated (r = 0.62, P < 0.0001) with bake water absorption followed by AG in flour (r = 0.30, P < 0.05). Bake mix time was correlated positively with percent IPP based on protein (r = 0.86) but negatively with percent SPP based on protein (r = ‐0.56, P < 0.0001).     

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.     

Molecular Characteristics of Corn Fiber Gum and Their Influence on CFG Emulsifying Properties

The molecular characteristics of two purified arabinoxylan fractions derived from corn kernels, corn fiber gum-1 and -2 (CFG-1 and -2), have been studied and correlated with emulsifying properties. CFG-1 and -2 fractions were isolated from different corn fiber sources by 1) a sequential alkaline extraction and H₂O₂ bleaching to produce CFG-1; and 2) additional H₂O₂ treatment of the alkali-extracted residue at pH 11.5, yielding CFG-2. Multiangle laser light-scattering and online viscosity were used to measure the molar mass, polydispersity, structure compactness, and intrinsic viscosity of the generated CFG fractions. Emulsification properties in an oil-in-water emulsion system with 10:1 oil-to-gum ratio was investigated by measuring turbidity of an aliquot from the bottom of the diluted emulsion over 10 days. The isolated CFG-2 from each fiber source was higher in weight-average molar mass (M_w) polydispersity) (M_w/M_n) and structure compactness, and also lower in solution weight-average intrinsic viscosity (η_w) than the corresponding CFG-1. Average M_w and η_w values were 244–491 kDa and 1.35–1.84 dL/g, respectively. The emulsion stabilizing capacity of CFG-2 from each fiber source was superior to the corresponding CFG-1.     

Seed protein electrophoretic characterization of cowpea (Vigna unguiculata) germplasm from IITA gene bank

Summary The total seed protein, globulin and albumin fractions of 20 cowpea (V. unguiculata) accessions from IITA gene bank were investigated by SDS-polyacrylamide gel electrophoresis. Total seed protein extracts were prepared from the defatted meal by homogenisation and centrifugation in Tris-glycine buffer. The globulins and albumins were obtained from the total protein extract by exhaustive dialysis against sodium acetate buffer. Two main total seed protein electrophoretic patterns were observed with respect to the 39 and 20 kD subunits, which were present in six out of the twenty accessions analysed. While there was no correlation between seed colour and total seed protein banding pattern, the six insect-resistant cultivars were characterized by the presence of the 39 and 20 kD subunits. The globulins were the predominant class of the total seed proteins and consisted mainly of 64, 58, 56 and 14 kD subunits which make up CP1 and CP2, the major globulins. The albumins in all accessions were a heterogeneous protein fraction consisting of both high and low molecular weight subunits. It was suggested that the insect-resistant cultivars may be genetically related and that the 39 and 20 kD subunits may be involved in the insect resistance mechanism.