Biochemical characterization of soluble proteins in pecan [Carya illinoinensis (Wangenh.) K. Koch

Pecans (cv. Desirable) contained approximately 10% protein on a dry weight basis. The minimum nitrogen solubility (5.9-7.5%) at 0.25-0.75 M trichloroacetic acid represented the nonprotein nitrogen. Among the solvents assessed for protein solubilization, 0.1 M NaOH was the most effective, while borate saline buffer (pH 8.45) was judged to be optimal for protein solubilization. The protein solubility was minimal in the pH range of 3-7 and significantly increased on either side of this pH range. Increasing the NaCl concentration from 0 to 4 M significantly improved ( approximately 8-fold increase) protein solubilization. Following Osborne protein fractionation, the alkali-soluble glutelin fraction (60.1%) accounted for a major portion of pecan proteins followed by globulin (31.5%), prolamin (3.4%), and albumin (1.5%), respectively. The majority of pecan polypeptides were in the molecular mass range of 12-66 kDa and in the pI range of 4.0-8.3. The pecan globulin fraction was characterized by the presence of several glycoprotein polypeptides. Lysine was the first limiting essential amino acid in the defatted flour, globulin, prolamin, and alkaline glutelin fractions. Leucine and tryptophan were the first limiting essential amino acids in albumin and acid glutelin fractions, respectively. Rabbit polyclonal antibodies detected a range of pecan polypeptides in the 12-60 kDa range, of which the globulin fraction contained the most reactive polypeptides.     

Wheat Proteins Extracted from Flour and Batter with Aqueous Ethanol at Subambient Temperatures

Contact of wheat flour with aqueous ethanol may enrich protein by starch displacement or deplete protein by extraction depending on 1) extraction conditions and 2) the form of the substrate. Extraction at subambient temperatures has not been described for specific gliadins for either dry flour with the protein in native configurations or for wet, developed batter or dough. This limits the ability to interpret technologies such as the cold-ethanol method. Here, we describe specific albumin and gliadin composition of flour extracts by capillary zone electrophoresis CZE in 0–100% (v/v) ethanol from –12 to 22°C. Extraction was reduced for albumin and gliadin protein as the temperature was reduced and the concentration range for extraction narrowed. Extraction dropped precipitously between 0 and –7°C for both albumins and gliadins. Electrophoretically defined gliadins extracted in constant proportion at 22°C and 30–80%(v/v) ethanol, but at lower temperature, the α-gliadins were enriched and β-gliadins depleted in the 30–55% (v/v) range. For extracts from wheat flour batter, depletion of α and β and enrichment of γ relative to the dry flour contact suggested that the electrophoretically slow migrating γ- and ω-proteins are less well incorporated to the dough matrix than electrophoretically fast migrating α and β types.     

Relationship Between Malting Quality Traits and Hordeins as Affected by Timing of Nitrogen Fertilizer Application

The application of nitrogen (N) fertilizer in malting barley is necessary to obtain good yield, but it also influences kernel protein content, which affects malting quality. The negative correlation between kernel protein content and malting extract is due to the hordein proteins. The aim of this study was to determine the effect of N application timing on hordein fractions and how this influences malt quality. Reversed‐phase high‐performance liquid chromatography (RP‐HPLC) was used to determine the hordein fractions in the two‐ and six‐row barley parents and their doubled‐haploid progeny, for two seasons for one location, and two locations in the second season. There were no changes in hordein level in response to timing of N application over years and locations. The two‐row parent had the lowest hordein level and the six‐row progeny had the highest. Total hordein content of the two‐row progeny and six‐row parent were similar. The supply of additional N in the form of fertilizer rather than the timing of all N applications influenced the production of all hordein fractions. There were significant correlations between hordein fractions and malting quality that also were reported in other studies. Kernel plumpness showed significant negative correlations with D, C, and B hordeins and total hordein content when half of the fertilizer was applied at planting and the other half at the six‐leaf stage. Absorption showed significant positive correlation with C hordeins and a negative correlation with the B‐to‐C ratio, also when the second half of the N was given at the six‐leaf stage.     

Influence of Rice Proteins on Eating Quality of Cooked Rice and on Aroma and Flavor of Sake

An improved method for the extraction of storage proteins from rice endosperm under conditions safe for producing food was developed. The contribution of the protein extracts to the eating quality of cooked rice and to the aroma and flavor of sake was examined. Sensory analysis was performed to evaluate the eating quality of cooked rice enriched with the protein extracts. Prolamin‐enrichment increased the hardness of cooked rice, and glutelin‐enrichment degraded the appearance of cooked rice. Physical analyses confirmed that prolamin‐enrichment changed, whereas the glutelin‐enrichment did not change the physical properties of cooked rice. Light and scanning electron microscopy of rice protein extracts revealed small particles of the prolamin extract and larger aggregated particles of the glutelin extract; these features remained after heating. The aroma and flavor of sake were negatively affected by the addition of the protein extracts. Especially, addition of prolamin significantly lowered the evaluation score of the aroma obtained by sensory analysis.     

Wet Processing of Barley Grains into Concentrates of Proteins, β‐Glucan,and Starch

An improved wet method was developed to process barley into fractions concentrated in protein, (1‐3)(1‐4)‐β‐d ‐glucan (BG), starch, or other carbohydrates (CHO). Alkaline concentration, solvent to barley flour ratio (SFR), and extraction temperature were evaluated for their effects on concentration and recovery of protein, BG, starch, oil, ash, and other CHO in each fraction type. Results show that the three parameters and their interactions all had significant effects, resulting in varying nutrient concentrations and recovery rates in each type of fractions. For protein fractions, protein content varied from 37.7 to 75.2%, protein recovery from 8.5 to 75.7%, and increasing alkaline concentration and SFR improved nutrient recovery. For BG fractions, BG content ranged from 21.5 to 87.0%, BG recovery from 28.6 to 78.0%, and increasing alkaline concentration decreased BG content but increased its recovery significantly. For starch fractions, starch content varied from 76.9 to 93.9%, starch recovery from 33.6 to 63.9%, and all parameters had little effect on the nutrient concentrations, but alkaline concentration and SFR improved recovery of starch, other CHO, and mass. Overall, the improved wet method was effective in concentrating the major nutrients from barley into their respective fractions, but process optimization through manipulating the three parameters is necessary to achieve a maximum concentration or recovery rate of a nutrient of interest in a specific fraction.     

Endosperm structure affects the malting quality of barley (Hordeum vulgare L.)

Twenty-seven barley (Hordeum vulgare L.) samples collected from growing sites in Scandinavia in 2001 and 2002 were examined to study the effect of endosperm structure on malting behavior. Samples were micromalted, and several malt characteristics were measured. Samples were classified as having a mealier or steelier endosperm on the basis of light transflectance (LTm). Because endosperm structure is greatly dependent on protein content, three barley sample pairs with similar protein contents were chosen for further analysis. During malting, the steelier barley samples produced less root mass, but showed higher respiration losses and higher activities of starch-hydrolyzing enzymes. Malts made from steelier barley had a less friable structure, with more urea-soluble D hordein and more free amino nitrogen and soluble protein. The reason for these differences may lie in the structure or localization of the hordeins as well as the possible effects of endosperm packing on water uptake and movement of enzymes.     

Distribution and Structural Variation of Nonstarch Polysaccharides in Milling Fractions of Hull‐less Barley with Variable Amylose Content

Three hull‐less barley genotypes containing starches with variable amylose content (23.8% normal, 4.3% waxy, 41.8% high‐amylose barley) were pearled to 10% and then roller‐milled to produce pearling by‐products (PBP), flour, and fiber‐rich fractions (FRF). PBP were enriched in arabinoxylans, protein, and ash and contained small amounts of starch and β‐glucans. FRF were considerably enriched in β‐glucans and arabinoxylans. The solubility of β‐glucans was higher in PBP than in FRF. The solubility of arabinoxylans was higher in FRF than in PBP. Small amounts of arabinogalactans detected in barley were concentrated in the outer portion of the barley kernel. The content and solubility of nonstarch polysaccharides (NSP) in various milling fractions was also dependent on the type of barley. To obtain more detailed information about the content and molecular structure of NSP, each milling fraction was sequentially extracted with water, alkaline [Ba(OH)₂], again with water, and finally with NaOH. These extractions resulted in four sub‐fractions: WE, Ba(OH)₂, Ba(OH)₂/H₂O, and NaOH. β‐Glucans and arabinoxylans exhibited structural heterogeneity derived from differences in their location within the kernel as well as from the genetic origin of barley. The WE arabinoxylans from FRF and flour had a substantially lower degree of branching than those from PBP. The WE arabinoxylans from FRF of high‐amylose and normal barley contained more unsubstituted Xylp residues but fewer doubly‐substituted and singly‐substituted Xylp at O‐2 than their counterparts from PBP. The WE arabinoxylans from FRF of waxy barley had a relatively high content of doubly‐substituted, but very few singly‐substituted Xylp residues. In all three barley genotypes, the ratio of tri‐ to tetrasaccharides in β‐glucans from PBP was higher than from flour and FRF. Substantial differences in the molecular weight of NSP in different milling fractions were also observed.     

Proteins Extracted from Defatted Wheat Germ: Nutritional and Structural Properties

The main by‐product of the wheat germ oil extraction process is a defatted wheat germ meal, which has a relatively high protein content, making it an attractive and promising source of vegetable proteins. Four protein fractions (albumin, globulin, prolamine, and glutelin) and protein isolate from defatted wheat germ flour (DWGF) were fractionated and then characterized by amino acid analysis, SDS‐PAGE, and differential scanning calorimetry (DSC). Albumin was the major fraction (34.5%) extracted, followed by globulin (15.6%), glutelin (10.6%), and prolamine (4.6%). Protein isolate was mainly composed of albumin and globulin. These protein fractions and protein isolate showed an excellent balance of all essential amino acids, with a relatively high level of glutamic acid, arginine, leucine, and glycine, whereas cystine was lacking. All the estimated nutritional quality parameters based on amino acids composition showed that defatted wheat germ proteins had good nutritional quality. Nonreduced and reduced SDS‐PAGE analyses showed that S‐S bonds ere deficient in the structure of wheat germ proteins. The albumin fraction consisted of 19 major polypeptide bands with M_r 14,000–84,000. The globulin fraction showed four distinct polypeptides or polypeptide group bands with M_r 55,000, 37,000–43,000, 24,000, and 12,000–20,000, which may be the components of the 8S‐type and 11S‐like proteins. The prolamine fraction showed a predominant doublet‐like band at M_r 17,000–16,000, while the glutelin fraction showed five major polypeptide bands with M_r 39,000, 20,000, 18,000, 17,000, and 14,000. Protein isolate and DWGF showed very similar SDS‐PAGE patterns. Except for prolamine and glutelin fractions without detectable calorimetric response, the globulin fraction possessed the highest thermal stability (T_d = 83.80°C, ΔH =1.36 J/g ), followed by protein isolate (T_d = 80.05°C, ΔH = 0.76 J/g), while the albumin fraction was lowest (T_d = 69.72°C, ΔH = 0.53 J/g). The findings on defatted wheat germ proteins are important for their potential application as functional food ingredients.     

Effects of Temperature,Sonication Time,and Power Settings on Size Distribution and Extractability of Total Wheat Flour Proteins as Determined by Size‐Exclusion High‐Performance Liquid Chromatography

The size‐exclusion (SE) HPLC profile of total protein extract obtained by sonication of flour samples at ambient temperature showed marked instability on reinjection. Instability was related to the presence of flour proteases that were inactivated by thermal treatment of flour samples at 60°C. Extraction of flour protein by sonication was a function of ultrasonic energy (sonication time × power product) delivered to flour sample. As protein solubility increased, the proportions of the earliest eluted SE‐HPLC fractions (F1 and F2) increased. Oversonication of proteins evidenced by a decrease in F1 amount at the benefit of F2 occurred below the sonication energy level needed for total protein extraction. Ultrasonic energy level was adjusted to allow total protein extraction while limiting oversonication. The sonication procedure was applied on 27 flour samples of contrasting dough strength to extract total proteins. Absolute amount of protein extractable by sonication, determined from SE‐HPLC area, was strongly correlated with flour protein content. Very significant and equivalent relationships were found between alveographic W index and absolute amount of either unextractable protein extract or F1 of SE‐HPLC profile from total protein extract.     

Isolation and characterization of undenatured chlorogenic acid free sunflower (Helianthus annuus) proteins

A method for obtaining sunflower protein (SFP) isolate, nondenatured and free of chlorogenic acid (CGA), has been developed. During the isolating procedure, the extent of CGA removal and protein denaturation was monitored. The defatted flour contained 2.5% CGA as the main phenolic compound. Phenolic compounds were removed by aqueous methanol (80%) extraction, before protein extraction at alkaline pH and diafiltration. Differential scanning calorimetry and solubility tests indicated that no denaturation of the proteins had occurred. The resulting protein products were biochemically characterized, and the presence of protein-CGA complexes was investigated. SFPs of the studied variety were found to be composed of two main protein fractions: 2S albumins and 11S globulins. In contrast to what has been previously reported, CGA was found to elute as free CGA, not covalently associated to any protein fraction.     

Free-zone capillary electrophoresis analysis of hordein patterns at different stages of barley malting

We have carried out a comparison of hordein patterns at different stages of the malting process using free-zone capillary electrophoresis (FZCE). FZCE has proved to be a suitable technique for the separation and characterization of hordeins in barley seeds. Assays of protein extraction and electrophoretic procedures led us to conclude that hordeins were best extracted with 40% ethanol and analyzed using 50 mM phosphate-glycine, pH 2.5, containing 20% ACN and 0.05% HPMC, at 12.5 kV and 45 degrees C, with 10 s hydrodynamic injection at 0.5 psi and 50 microm i.d. x 31 cm uncoated fused-silica capillary. Our results afford useful information about changes in the composition of these proteins in barley during malting.     

Sequential extraction and quantitative recovery of gliadins, glutenins, and other proteins from small samples of wheat flour

Methods to sequentially extract and fractionate wheat flour proteins were evaluated to reliably quantify gliadins, glutenins, and albumins/globulins in single flour samples. Compositions of the resulting protein fractions were analyzed by RP-HPLC combined with SDS-PAGE. Unknown proteins were identified by mass spectrometry or N-terminal sequencing. The best separation and recovery of discrete albumin/globulin, gliadin, and glutenin fractions from the same flour sample was achieved by extraction with 0.3 M NaI in 7.5% 1-propanol followed by 2% SDS, 25 mM DTT in 25 mM TRIS, pH 8.0, and precipitation of the solubilized proteins with ammonium acetate/methanol followed by acetone. Average flour composition for the variety Butte86 was 10% albumin/globulin, 40% gliadin, and 48% glutenin. This method should be useful for determining flour composition in diverse samples and evaluating relationships between proteins and end-use functionality.     

Effect of Extraction Conditions on Yield,Composition, and Viscosity Stability of Barley β-Glucan Gum

Cereal β-glucan can function as a thickener, but endogenous β-glucanase enzymes of the grain cleave β-glucan, reducing its viscosity. Although different extraction techniques have been developed, the viscosity stability of β-glucan gum has not been reported. The objective of this study was to investigate the effect of extraction treatments on the yield, purity, and viscosity stability of barley β-glucan (BBG) gum. A regular barley cultivar, Condor, and a waxy cultivar blend were extracted at pH 7–10 and 55°C for 0.5 hr. Four extraction conditions were evaluated: 1) extraction at high pH with no additional heat treatment; 2) boiling of extract; 3) prior refluxing of flour with 70% ethanol; and 4) treatment of extract with thermostable α-amylase for purification. Viscosity of extracts was monitored for ≥24 hr at 25°C. The highest β-glucan purities were achieved with a boiled Condor extract at pH 7 (81.3% db, 4.1% yield) and with refluxed waxy barley extracted at pH 8 and treated with α-amylase and (79.3% db, 5.1% yield). Gums extracted without subsequent heat treatment or prior refluxing of flour had high protein (>17%) and starch (>24%) impurities, respectively. The viscosity of gums obtained without heating was unstable. Prior refluxing treatment was not sufficient to stabilize final extracts. Boiling extracts resulted in stable but low viscosity. Reflux followed by purification treatment produced the highest stable viscosity for 0.5% solutions of both Condor (64 mPa sec^-1, pH 7) and waxy (48.8 mPa sec^-1, pH 8) extracts. Stable BBG gum with high viscosity can be obtained using thermal treatments in combination with high pH. The potential use of such gums as thickeners in food systems needs to be assessed.     

Protein metabolism in rice seedling

The relationship between protein synthesis and degradation in germinating rice seed were studied with protein synthetic inhibitors. Both DNP and 8-AG inhibited the degradation of glutelin, the major storage protein in rice seed, while the inhibitors had no direct effect in the activity of rice seed proteinllse in vitro. The prevention can be partly ascribed to the Inhibition of proteinase synthesis because the inhibitors depressed the increase in proteinase activity during germination. When DNP treatment was started at the onset of germination, the degradation of glutelin in the endosperm was seriously inhibited and the endosperm remained rigid over 9 days of incubation at 30°C. In contrast, the inhibition was less efficient clent when the treatment was started in the later stage. It is suggested that the degradation of the storage protein in rice seed depends on the synthetic process of the hydrolytic enzymes which increase during germination. disintegrate the compartmentation of the endosperm and allow the storage proteins to come in contact with the existing proteinases     

Composition and Utilization of Barley Pearling By‐Products for Making Functional Pastas Rich in Dietary Fiber and β‐Glucans

Pearling by‐products and the pearled products of two commercial stocks of hulled barley, pearled according to an industrial process consisting of five consecutive pearling steps, were analyzed for β‐glucans, dietary fiber (total, soluble, and insoluble), protein, lipid, ash, and digestible carbohydrate. The data showed that the pearling flour fractions, abraded in the fourth and fifth hullers, contained interesting amounts of β‐glucans (3.9–5.1% db) from a nutritional point of view. These fractions were subsequently enriched in β‐glucans using a milling‐sieving process to double β‐glucan content (9.1–10.5% db). Functional pastas, enriched with β‐glucans and dietary fiber, were produced by substituting 50% of standard durum wheat semolina with β‐glucan‐enriched barley flour fractions. Although darker than durum wheat pasta, these pastas had good cooking qualities with regard to stickiness, bulkiness, firmness, and total organic matter released in rinsing water. The dietary fiber (13.1–16.1% wb) and β‐glucan (4.3–5.0% wb) contents in the barley pastas were much higher than in the control (4.0 and 0.3% wb, respectively). These values amply meet the FDA requirements of 5 g of dietary fiber and 0.75 g of β‐glucans per serving (56 g in the United States and 80 g in Italy). At present, the FDA has authorized the health claim “may reduce the risk of heart disease” for food containing β‐glucans from oat and psyllium only.     

Effect on Dough Functional Properties of Partial Fractionation,Redistribution, and In Situ Deposition of Wheat Flour Gluten Proteins Exposed to Water,Ethanol, and Aqueous Ethanol

The application of the cold‐ethanol laboratory fractionation method to the bulk separation of wheat starch and gluten is accompanied by incidental dissolution, removal, or redeposition of a small part of the functional gliadin protein. The new distribution resulting from process incidental redeposition of soluble components or by purposeful add‐back of soluble and leached components can lead to differences in functionality and more difficult recovery of native properties. To assess this issue, we exposed several wheat flour types to ethanol and water (50–90% v/v) solutions, water, and absolute ethanol at 22°C and –12°C. The exposure was mass conserving (leached components returned to substrate by evaporation of the solvent without separation of phases) or mass depleting (leached components not returned to substrate). The result of the mass‐conserving contact would be flour with altered protein distributions and intermolecular interactions. The result of the mass‐depleting contact would also include altered protein content. Furthermore, the mass‐conserving contact would model an industrial outcome for a cold‐ethanol process in which leached components would be added back from an alcohol solution. The leaching result was monitored by mixography of the flour, nitrogen analysis, and capillary zone electrophoresis of extracts. Although dough rheology was generally like that of the source flour, there were notable differences. The primary change for mass‐conserving contact was an increase in the time to peak resistance and a decrease in the rate of loss of dough resistance following peak resistance. These changes were in direct proportion to the amount of protein mobilized by the solvent. Leaching at 22°C, prevented dough formation for most aqueous ethanol concentrations and greatly reduced gliadin protein content. Minimal changes were noted for solvent contact at –12°C regardless of the ethanol concentration. The data suggested that 1) the conditions applied in cold‐ethanol enrichment of protein from wheat will generally preserve vital wheat gluten functionality, 2) functionality losses can be recovered by returning the solubilized fractions, and 3) the flour to which the gluten is added may require more mixing.     

Nutritional responses of rats to diets based on chickpea ( Cicer arietinum L.) seed meal or its protein fractions

The aim of this study was to isolate the protein fractions from chickpea, var. IAC-Marrocos, as well as to evaluate its in vivo nutritional protein quality. Among the proteins, albumins showed better nutritional value in the in vivo assays and amino acid contents, despite their higher trypsin inhibitor contents. Trypsin inhibitors were found to be heat labile in all samples, but the digestibility results for unheated and heated flour and albumins suggest that their contents are not very decisive. The PER values for casein (not supplemented) were very similar to those of heated flour and unheated or heated albumin and total globulins. The albumin and glutelin fractions showed the best results for PDCAAS, however, lower than those of casein. Despite the high digestibility of the globulin the very low essential amino acid content lowered its PDCAAS, and it had the lowest values.     

Optimizing Extraction of Zein and Glutelin‐Rich Fraction During Sequential Extraction Processing of Corn

This study was conducted to improve yields and qualities of corn protein co‐products produced by the sequential extraction process (SEP), a process using ethanol to fractionate corn in producing fuel ethanol. A two‐stage extraction protocol was evaluated to recover zein and subsequently recover a glutelin‐rich fraction (GRF). After the simultaneous oil‐extraction and ethanol‐drying step of SEP, zein was extracted from the anhydrous‐ethanol‐defatted, flaked corn by using 70% (v/v) ethanol at 60°C for 1.5 hr in a shaking water bath. Zein was recovered by ultrafiltering and then drying in a vacuum‐oven. Zein yield was 65% of the available zein in the flaked corn. SDS‐PAGE band patterns of the recovered zein closely resembled that of commercial zein. After zein extraction, the GRF was extracted using 45% ethanol and 55% 0.1M NaOH at 55°C for 2 hr. The extract was concentrated by ultrafiltration and then freeze‐dried. GRF yield was ≈65% of the available protein. Freeze‐dried GRF contained 90% crude protein (db), which classified the protein as a protein isolate. As with the protein concentrate from the original SEP, the GRF isolate was highly soluble in water at pH ≥ 7, had good emulsifying and foaming properties, formed stable emulsions, and was heat‐stable.     

Effects of Secondary Structures of Heated Egg White Protein on the Binding Between Prime Starch and Tailings Fractions in Fresh Wheat Flour

Dried egg white protein was heated at 120°C for 1 hr, added to a fresh wheat flour (protein 8.6%), and the protein and wheat flour were subjected to acetic acid (pH 3.5) fractionation. The results showed that egg white protein increased the binding between prime starch (PS) and tailings (T) fractions in wheat flour. Several conditions for heating of egg white protein were examined to determine 1) the effect of the amount of water added to the protein before heating; 2) the effect of heating time (hr) on protein at 120°C; and 3) the effect of heating temperature on the binding between PS and T fractions. The amount of protein per 50.0 g of wheat flour was further examined for the maximum binding between PS and T fractions. The heated egg white protein was analyzed by Fourier transform infrared (FT‐IR) spectroscopy, and the changes in the secondary structures (α‐helix, β‐sheets, and others) of the protein caused by heating were studied. When egg white protein was heated at 120°C for 8 hr, 9.0% of the α‐helix structures of egg white protein decreased to 3.0%, and 37.0% of the β‐sheet structures increased to 41.0%. The decrease of α‐helix and increase of β‐sheet structures of heated egg white protein were related to the increase in the binding between PS and T fractions in the same heated egg white protein and wheat flour sample. A relationship between the structural changes in heated egg white protein (180°C, 1 hr) and the binding between PS and T fractions in the heated egg white protein and wheat flour was also observed.     

Comparative Studies on Composition and Distribution of Phenolic Acids in Cereal Grain Botanical Fractions

The phenolic acid composition and concentration of four manually separated fractions (pericarp, aleurone layer, germ, and endosperm fractions) as well as whole grains of yellow corn, wheat, barley, and oats were analyzed by HPLC‐MS/MS following microwave‐assisted alkaline aqueous extraction. Phenolic acid compositions in whole grains and their fractions were similar, with minor differences among the grain fractions. Significant differences (P < 0.05), however, were observed in phenolic acid concentrations among cereal types, within cereal varieties, and among grain fractions, with yellow corn exhibiting the highest values. The concentrations of p‐coumaric and syringic acid in the pericarp were 10‐ to 15‐fold and 6‐ to 10‐fold higher, respectively, in yellow corn than in wheat, barley, and oats. In the aleurone layer, sinapic and vanillic acids in yellow corn were about 8‐ and 30‐fold more than in wheat. The germ fraction of wheat had 1.8 times more syringic acid than yellow corn germ. Grain fractions, excluding endosperm, had enhanced levels of phenolic acids compared with whole grain. Sinapic acid was more concentrated in the pericarp and germ of wheat, whereas isoferulic acid was concentrated in the germ of purple barley. Syringic and vanillic acids were concentrated in the pericarp and sinapic acid in the aleurone layer of yellow corn. These findings are important in understanding the composition and distribution of phenolic acids, and they act as a guide in identification of grain fractions for use as food ingredients. In addition, yellow corn fractions (aleurone and pericarp) may be potential alternative phenolic‐rich functional food ingredients in grain‐based food products.