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Yousseef, Manhal, Samuel Lubbers, Florence Housson, and Dominique Valentin. "Sensory evaluation as a tool in assessing the quality of new fermented products." Science and Technology Development Journal 17, no. 3 (September 30, 2014): 63–71. http://dx.doi.org/10.32508/stdj.v17i3.1501.
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Ten starter cultures of lactic acid bacteria were used to ferment five mixtures of milk and pea protein (0%, 10%, 20%, 30% and 40% of pea) to select the cocktail that can lead to products similar to traditional yogurt. Product quality evaluation was performed by comparing the sensory profile of 49 formulated products with the profile of a milk fermented by commercial lactic ferments. The sensory profiles were analyzed by means of three-way ANOVAs and a principal component analysis (PCA). Substitution of cow milk protein with 40% of pea proteins reduce starter cultures effects and decrease product quality. In contrast, until 30% of pea protein, starter cultures show positive and negative effects. For example, products fermented by Streptococcus thermophilus + Lactobacillus acidophilus with 30% pea protein have positive characters like creamy and smooth, but Lactobacillus delbrueckii subsp. Bulgaricus + Lactobacillus rhamnosus caused bad quality and negative characters like bitter and astringent even with 100% cow milk.
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Sirtori, Cesare R., Michela Triolo, Raffaella Bosisio, Alighiero Bondioli, Laura Calabresi, Viviana De Vergori, Monica Gomaraschi, et al. "Hypocholesterolaemic effects of lupin protein and pea protein/fibre combinations in moderately hypercholesterolaemic individuals." British Journal of Nutrition 107, no. 8 (October 28, 2011): 1176–83. http://dx.doi.org/10.1017/s0007114511004120.
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The present study was aimed to evaluate the effect of plant proteins (lupin protein or pea protein) and their combinations with soluble fibres (oat fibre or apple pectin) on plasma total and LDL-cholesterol levels. A randomised, double-blind, parallel group design was followed: after a 4-week run-in period, participants were randomised into seven treatment groups, each consisting of twenty-five participants. Each group consumed two bars containing specific protein/fibre combinations: the reference group consumed casein+cellulose; the second and third groups consumed bars containing lupin or pea proteins+cellulose; the fourth and fifth groups consumed bars containing casein and oat fibre or apple pectin; the sixth group and seventh group received bars containing combinations of pea protein and oat fibre or apple pectin, respectively. Bars containing lupin protein+cellulose ( − 116 mg/l, − 4·2 %), casein+apple pectin ( − 152 mg/l, − 5·3 %), pea protein+oat fibre ( − 135 mg/l, − 4·7 %) or pea protein+apple pectin ( − 168 mg/l, − 6·4 %) resulted in significant reductions of total cholesterol levels (P < 0·05), whereas no cholesterol changes were observed in the subjects consuming the bars containing casein+cellulose, casein+oat fibre or pea protein+cellulose. The present study shows the hypocholesterolaemic activity and potential clinical benefits of consuming lupin protein or combinations of pea protein and a soluble fibre, such as oat fibre or apple pectin.
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Moll, Pascal, Hanna Salminen, Christophe Schmitt, and Jochen Weiss. "Impact of microfluidization on colloidal properties of insoluble pea protein fractions." European Food Research and Technology 247, no. 3 (February 6, 2021): 545–54. http://dx.doi.org/10.1007/s00217-020-03629-2.
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AbstractMicrofluidization is a technique commonly used to disrupt and homogenize dispersions such as oil-in-water emulsions or cellular suspensions. In this study, we investigated its ability to alter the physicochemical properties of plant-derived insoluble protein aggregates such as those found in pea protein extracts. Insoluble pea protein dispersions (5% w/w, pH 7) were homogenized at 25–150 MPa for 1–5 cycles. Increasing the homogenization pressure and cycles decreased the particle size (d43) of the unhomogenized insoluble pea proteins from 180 ± 40 μm to 0.2 ± 0.0 μm (at ≥ 125 MPa), leading to more transparent dispersions. Furthermore, the solubility of the insoluble pea proteins increased from 23 ± 1% to 86 ± 4%. Treatments with chaotropic agents, dithiothreitol and urea, revealed that insoluble pea protein aggregates were stabilized not only by disulphide bonds but also by hydrogen bonds and hydrophobic interactions. These molecular interactions were disrupted by microfluidization. The study provides insights into the disruption mechanism of insoluble pea proteins by applying microfluidization and offers a mean to improve their technofunctional properties to facilitate further use in food manufacture.
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Häberer, C. D., K. Diepvens, N. Geary, and W. Langhans. "Intragastric infusion of pea protein hydrolysate reduces food intake more than pea protein." Appetite 49, no. 1 (July 2007): 295. http://dx.doi.org/10.1016/j.appet.2007.03.081.
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Strauch, Renee Cilliers, and Mary Ann Lila. "Pea protein isolate characteristics modulate functional properties of pea protein–cranberry polyphenol particles." Food Science & Nutrition 9, no. 7 (May 24, 2021): 3740–51. http://dx.doi.org/10.1002/fsn3.2335.
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Manso, María A., Tiziana Maria Cattaneo, Stefania Barzaghi, Cornelis Olieman, Rosina López-Fandiño, J. Leaver, J. Otte, et al. "Determination of Vegetal Proteins in Milk Powder by Sodium Dodecyl Sulfate–Capillary Gel Electrophoresis: Interlaboratory Study." Journal of AOAC INTERNATIONAL 85, no. 5 (September 1, 2002): 1090–95. http://dx.doi.org/10.1093/jaoac/85.5.1090.
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Abstract An interlaboratory study, with the participation of 8 laboratories, was conducted to evaluate a sodium dodecyl sulfate–capillary gel electrophoresis method for determination of adulteration of milk powder with soy and pea proteins. Calibration standards (0–8%, w/w, soy and pea protein in total protein) and adulterated skim milk powders (0–5%, w/w, soy and pea proteins in total protein) were produced. Vegetal proteins were determined after removal of milk proteins by pretreatment of the samples with tetraborate–EDTA buffer, pH 8.3. Repeatability standard deviations ranged from 9 to 15% and reproducibility standard deviations ranged from 25 to 30% in the samples containing 5% vegetal protein in total protein.
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Leterme, Pascal, Thierry Monmart, and Evelyne Baudart. "Amino acid composition of pea (Pisum sativum) proteins and protein profile of pea flour." Journal of the Science of Food and Agriculture 53, no. 1 (1990): 107–10. http://dx.doi.org/10.1002/jsfa.2740530112.
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Krefting, Jessica. "The Appeal of Pea Protein." Journal of Renal Nutrition 27, no. 5 (September 2017): e31-e33. http://dx.doi.org/10.1053/j.jrn.2017.06.009.
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Mihailovic, Vojislav, Aleksandar Mikic, Pero Eric, Sanja Vasiljevic, Branko Cupina, and Slobodan Katic. "Protein pea in animal feeding." Biotehnologija u stocarstvu 21, no. 5-6 (2005): 281–85. http://dx.doi.org/10.2298/bah0506281m.
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Niemi, Kevin J., Julius Adler, and Bruce R. Selman. "Protein Methylation in Pea Chloroplasts." Plant Physiology 93, no. 3 (July 1, 1990): 1235–40. http://dx.doi.org/10.1104/pp.93.3.1235.
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Menkhaus, Todd J., Cynthia Pate, Anthony Krech, and Charles E. Glatz. "Recombinant protein purification from pea." Biotechnology and Bioengineering 86, no. 1 (2004): 108–14. http://dx.doi.org/10.1002/bit.20039.
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Bhardwaj, Megha, Tobias Terzer, Petra Schrotz-King, and Hermann Brenner. "Comparison of Proteomic Technologies for Blood-Based Detection of Colorectal Cancer." International Journal of Molecular Sciences 22, no. 3 (January 26, 2021): 1189. http://dx.doi.org/10.3390/ijms22031189.
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Blood-based protein biomarkers are increasingly being explored as supplementary or efficient alternatives for population-based screening of colorectal cancer (CRC). The objective of the current study was to compare the diagnostic potential of proteins measured with different proteomic technologies. The concentrations of protein biomarkers were measured using proximity extension assays (PEAs), liquid chromatography/multiple reaction monitoring–mass spectrometry (LC/MRM-MS) and quantibody microarrays (QMAs) in plasma samples of 56 CRC patients and 99 participants free of neoplasms. In another approach, proteins were measured in serum samples of 30 CRC cases and 30 participants free of neoplasm using immunome full-length functional protein arrays (IpAs). From all the measurements, 9, 6, 35 and 14 protein biomarkers overlapped for comparative evaluation of (a) PEA and LC/MRM-MS, (b) PEA and QMA, (c) PEA and IpA, and (d) LC/MRM-MS and IpA measurements, respectively. Correlation analysis was performed, along with calculation of the area under the curve (AUC) for assessing the diagnostic potential of each biomarker. DeLong’s test was performed to assess the differences in AUC. Evaluation of the nine biomarkers measured with PEA and LC/MRM-MS displayed correlation coefficients >+0.6, similar AUCs and DeLong’s p-values indicating no differences in AUCs for biomarkers like insulin-like growth factor binding protein 2 (IGFBP2), matrix metalloproteinase 9 (MMP9) and serum paraoxonase lactonase 3 (PON3). Comparing six proteins measured with PEA and QMA showed good correlation and similar diagnostic performance for only one protein, growth differentiation factor 15 (GDF15). The comparison of 35 proteins measured with IpA and PEA and 14 proteins analyzed with IpA and LC/MRM-MS revealed poor concordance and comparatively better AUCs when measured with PEA and LC/MRM-MS. The comparison of different proteomic technologies suggests the superior performance of novel technologies like PEA and LC/MRM-MS over the assessed array-based technologies in blood-protein-based early detection of CRC.
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Renganathan, Hemamalini, Hema Vaidyanathan, Anna Knapinska, and Joe W. Ramos. "Phosphorylation of PEA-15 switches its binding specificity from ERK/MAPK to FADD." Biochemical Journal 390, no. 3 (September 5, 2005): 729–35. http://dx.doi.org/10.1042/bj20050378.
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Cell signalling pathways that regulate proliferation and those that regulate programmed cell death (apoptosis) are co-ordinated. The proteins and mechanisms that mediate the integration of these pathways are not yet fully described. The phosphoprotein PEA-15 (phosphoprotein enriched in astrocytes) can regulate both the ERK (extracellular-signal-regulated kinase)/MAPK (mitogen-activated protein kinase) pathway and the death receptor-initiated apoptosis pathway. This is the result of PEA-15 binding to the ERK/MAPK or the proapoptotic protein FADD (Fas-activated death domain protein) respectively. The mechanism by which binding of PEA-15 to these proteins is controlled has not been elucidated. PEA-15 is a phosphoprotein containing a Ser-104 phosphorylated by protein kinase C and a Ser-116 phosphorylated by CamKII (calcium/calmodulin-dependent protein kinase II) or AKT. Phosphorylation of Ser-104 is implicated in the regulation of glucose metabolism, while phosphorylation at Ser-116 is required for PEA-15 recruitment to the DISC (death-initiation signalling complex). Moreover, PEA-15 must be phosphorylated at Ser-116 to inhibit apoptosis. In the present study, we report that phosphorylation at Ser-104 blocks ERK binding to PEA-15 in vitro and in vivo, whereas phosphorylation at Ser-116 promotes its binding to FADD. We further characterize phospho-epitope-binding antibodies to these sites. We report that phosphorylation does not influence the distribution of PEA-15 between the cytoplasm and nucleus of the cell since all phosphorylated states are found predominantly in the cytoplasm. We propose that phosphorylation of PEA-15 acts as the switch that controls whether PEA-15 influences proliferation or apoptosis.
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Pillai, Prasanth KS, Yulinglong Ouyang, Andrea K. Stone, and Michael T. Nickerson. "Effect of different levels of esterification and blockiness of pectin on the functional behaviour of pea protein isolate–pectin complexes." Food Science and Technology International 27, no. 1 (May 25, 2020): 3–12. http://dx.doi.org/10.1177/1082013220924888.
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This research examines changes to the functional (solubility, emulsifying and foaming) properties of pea protein isolate when complexed with commercial citrus pectin of different structural attributes. Specifically, a high methoxy (P90; degree of esterification: 90.0%; degree of blockiness: 64.5%; galacturonic acid content 11.4%) and low methoxy (P29; degree of esterification: 28.6%; degree of blockiness: 31.1%; galacturonic acid: 70%) pectin at their optimum mixing ratios with pea protein isolate (4:1 pea protein isolate to P90; 10:1 pea protein isolate to P29) were assessed at the pHs associated with critical structure forming events during the complexation process (soluble complexation (pHc), pH 6.7 and 6.1; insoluble complex formation (pHϕ1), pH 4.0 and 5.0; maximum complexation (pHopt), pH 3.5 and 3.8; dissolution of complexes, pH 2.4 and 2.1; for admixtures of pea protein isolate–P90 and pea protein isolate–P29, respectively). Pea protein isolate solubility was improved from 41 to 73% by the presence of P90 at pH 6.0 and was also moderately increased at pH 4.0 and pH 5.0 by P90 and P29, respectively. The emulsion stability of both pea protein isolate–pectin complexes was higher than the homogeneous pea protein isolate at all critical pHs except pHopt as well as pHc for pea protein isolate–P29 only. P90, with the higher level blockiness and esterification, displayed better foaming properties at the maximal complexation pH when complexed with pea protein isolate than pea protein isolate–P29 or pea protein isolate alone. However at pHϕ2, pea protein isolate–P29 admixtures produced foams with 100% stability, increasing pea protein isolate foam stability by 85%. The enhanced functionality of pea protein isolate–pectin complexes based on the type of pectin used at critical pHs indicates they may be useful biopolymer ingredients in plant protein applications.
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Bobkov, S. V., and O. V. Uvarova. "Development of optimal method of obtaining pea isolated proteins for use in breeding for quality." Agricultural Science Euro-North-East 21, no. 4 (August 22, 2020): 408–16. http://dx.doi.org/10.30766/2072-9081.2020.21.4.408-416.
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The article provides the results of the experiments on determination of optimal parameters for obtaining isolated proteins from grains of cultivated and wild pea for use in breeding for quality. The flour of pea varieties Sophia, Rodnik and wild accession k-3370 (Pisum sativum L. ssp. Elatius) were used in the experiment. Isolated pea proteins were obtained based on alkaline extraction and isoelectric precipitation. The experiments were carried out with the use of complete and fractional factorial plans with two levels of factors. Extraction and precipitation of protein were conducted in two stages. One hundred grams of flour were used for extraction. Influence of factors (variety, pH, duration of extraction) on the yield of isolated protein, extraction efficiency, crude protein and fat content in protein isolates was studied. All isolates were characterized by high content of crude protein (90.2-93.1 %). It was determined that increase of pH higher than eight led to enhancement of protein yield and decrease of crude protein content. The results obtained raise the possibility of effective extraction at decreased level of pH that prevents the formation of toxic chemicals. Increase of pH promoted fat accumulation in protein isolate especially at the second stage of extraction. Thus, obtaining protein isolates for evaluation of pea genetic resources should be conducted during a single cycle of extraction and precipitation. The experiments have not revealed significant differences between cultivated and wild pea as to the technology of extraction. The results of the studies are important for evaluation of pea genetic resources according to functional properties of protein isolates.
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Barac, Miroljub, Mirjana Pesic, Sladjana Stanojevic, Aleksandar Kostic, and Slavica Cabrilo. "Techno-functional properties of pea (Pisum sativum) protein isolates: A review." Acta Periodica Technologica, no. 46 (2015): 1–18. http://dx.doi.org/10.2298/apt1546001b.
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Due to high nutritive quality, good techno-functional properties and low cost, legume protein products are becoming the most appropriate alternative to protein products of animal origin. In food industries, these products are usually used as techno-functional additives which provide specific characteristics of final food products. Legume proteins are commonly used as flour, concentrates, and isolates. The greatest application on industrial scale has soy proteins, and to a lesser extent, in the past 20 years, pea protein isolates. The modest use of pea protein is partly a result of insufficient information relating to their techno-functional properties. This paper is an overview of techno-functional properties of pea proteins and their isolates. Also, the paper deals with the possible use of limited enzymatic hydrolysis as a method for the improvement of their techno-functional properties.
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Guillin, Florence, Claire Gaudichon, Laetitia Guerin-Deremaux, Catherine Lefranc-Millot, Gheorghe Airinei, Robert Benamouzig, Nadezda Khodorova, Pierre-Henri Pomport, Juliette Martin, and Juliane Calvez. "Real Ileal Amino Acid Digestibility of Pea Protein Isolate As Compared to Casein in Healthy Adult Humans." Current Developments in Nutrition 5, Supplement_2 (June 2021): 497. http://dx.doi.org/10.1093/cdn/nzab041_012.
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Abstract Objectives In the current context of finding plant alternatives to animal proteins, pea would be a good option regarding its high protein content and its well-balanced amino acid (AA) profile. However, we must examine its digestibility, a main criteria of protein nutritional quality. The aim of this study was to determine the real ileal AA and nitrogen (N) digestibility (RIDAA and RIDN) of pea protein as compared to milk casein in humans. We also evaluated their respective nutritional qualities through the calculation of the digestible indispensable amino acid score (DIAAS) and the net postprandial protein utilization (NPPU). Methods Fifteen healthy adult volunteers completed the study and were equipped with a triple-lumen naso-ileal tube. They were given 9 portions of mashed potatoes containing either pea protein or casein isolates that were intrinsically labelled with 15N. PEG-4000 was perfused in the ileum as a non-absorbable marker to measure the intestinal flow rate. Ileal digesta were collected continuously by aspiration with a syringe over an 8-h postprandial period, while plasma and urine were sampled regularly. N and AA contents of digesta and protein isolates were measured using EA and U-HPLC. PEG-4000 content of the digesta was measured by turbidimetric method. Urea was extracted from plasma and urine samples. 15N enrichment was assessed in digesta, urea and protein isolates by EA-IRMS and in individual AAs by GC-C-IRMS. Results Mean RIDAA was 93.6 ± 2.9% and 96.8 ± 1.0% for pea protein and casein, respectively, with no significant difference between groups (P = 0.22). RIDN was 92.0 ± 2.7% and 94.0 ± 1.7% for pea protein and casein, respectively, and were not different (P = 0.11). The DIAAS was 1.00 for pea protein and 1.45 for casein. The NPPU was 67.0 ± 6.2% for pea protein and 70.7 ± 1.9% for casein and the difference was not significant (P = 0.15). Conclusions Overall, the bioavailability was not different between pea protein and casein in healthy adults. The DIAAS of pea protein reached 1, revealing the absence of limiting AA in regard to the requirements. Considering its AA composition and the digestibility results we obtained, pea protein can be qualified as a high-quality protein. Funding Sources Roquette
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Russouw, Pauline S., Jill Farrant, Wolf Brandt, Dennis Maeder, and George G. Lindsey. "Isolation and characterization of a heat-soluble protein from pea (Pisum sativum) embryos." Seed Science Research 5, no. 3 (September 1995): 137–44. http://dx.doi.org/10.1017/s0960258500002750.
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AbstractAn LEA-like protein has been isolated and characterized from pea (Pisum sativum) embryos. It is the most prevalent protein in a homogenate of pea axes heated for 10 min at 80°C and then centifuged for 10 min at 17000g(80°C supernatant fraction). It has a molecular mass of 11 kDa and is very rich in hydrophilic amino acids, notably aspartate, glutamate and glycine. The protein is not recognized by an antibody to the group II dehydrin C-terminal consensus sequence. Antibodies to the isolated protein recognize a number of larger proteins in the 80°C supernatant fraction of pea and other legumes (chick pea, soybean and bean) as well as gramineous seeds (wheat, maize and barley). The protein undergoes a substantial increase in α-helical content at high ionic strength but does not dimerize.
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Johnston, Alie J., Rebecca C. Mollard, Dianna Dandeneau, Dylan S. MacKay, Nancy Ames, Julianne Curran, Danielle R. Bouchard, and Peter J. Jones. "Acute effects of extruded pea fractions on glycemic response, insulin, appetite, and food intake in healthy young adults, results of a double-blind, randomized crossover trial." Applied Physiology, Nutrition, and Metabolism 46, no. 9 (September 2021): 1126–32. http://dx.doi.org/10.1139/apnm-2020-0571.
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Benefits of pulse consumption on glycemic control are well established; however, research examining the effects of pulse fractions incorporated into extruded products is limited. In a randomized, repeated-measures crossover study, adults (n = 26) consumed cereals made with oat flour (control), oat flour and pea starch (starch), oat flour and pea protein (protein), oat flour, pea starch and pea protein (starch+protein), oat flour, pea fibre and pea protein (fibre+protein), and pea fibre, pea starch and pea protein (fibre+starch+protein). Blood glucose (BG) and insulin concentrations, and appetite incremental area under the curve (iAUC) were calculated before (0–120 min) and after (120–200 min) the ad libitum meal for measurement of food intake. Pre-meal, overall mean BG and iAUC were lower following the protein, starch+protein, protein+fibre, and the fibre+starch+protein cereals compared with the starch and control. For pre-meal overall mean insulin concentrations, fibre+protein led to a lower response compared with control, starch+protein, and protein cereals. Fibre+starch+protein also led to lower insulin compared with protein cereal. Pre-meal insulin iAUC was lower following fibre+protein compared with control and protein cereals. The inclusion of yellow pea protein and fibre in oat-based breakfast cereal reduces postprandial glycemia; however this effect is dependent on fraction type. ClinicalTrials.gov: NCT02366572. Novelty: Inclusion of pulse protein and fibre in oat flour-based breakfast cereal reduces postprandial glucose response. The glycemic benefits of whole pulses are at least somewhat retained in some pulse fractions.
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Hou, Xingwei, Wes Taylor, and Paul Fields. "Effect of pea flour and pea flour extracts on Sitophilus oryzae." Canadian Entomologist 138, no. 1 (February 2006): 95–103. http://dx.doi.org/10.4039/n05-023.
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AbstractProtein-rich pea flour is an antifeedant and a repellent and is toxic to the rice weevil, Sitophilus oryzae (L.), but its mode of action is not known. Results showed that protein-rich pea flour had no fumigant effect on adult survival or offspring production of S. oryzae. In a contact experiment, immobilized weevils were fed every other day and had their abdomens brushed with protein-rich pea flour or wheat flour on the alternate days. Insects treated with protein-rich pea flour had an average longevity of 9.6 days, which was significantly shorter than that for insects treated with wheat flour (11.3 days) or brushed controls (17.6 days). These results suggest that toxins from the protein-rich pea flour may be able to penetrate the insect cuticle. Midguts from weevils fed protein-rich pea flour, a pea flour extract, or a mixture of pea peptides contained numerous bubbles. Midgut tissues in these treated adults were injured, as shown by dual staining with the fluorescent dyes calcein AM and propidium iodide. The volume of the bubbles increased rapidly when insects were fed protein-rich pea flour or pea flour extract. There were no bubbles found in the midguts of S. oryzae that fed on wheat kernels or wheat flour.
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Sujkowska, Marzena, Wojciech Borucki, and Władysław Golinowski. "Localizatlon of expansin-like protein in apoplast of pea (Pisum sativum L.) root nodules during interaction with Rhizobium leguminosarum bv. viciae." Acta Societatis Botanicorum Poloniae 76, no. 1 (2011): 17–26. http://dx.doi.org/10.5586/asbp.2007.002.
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During nodule development on pea roots, apoplast undergoes changes in activity of plant cell wall proteins such as expansins (EXPs). Because the accumulation of EXP protein has been correlated with the growth of various plant organs, we investigated using Western Blot and immunolocalization studies with antibody against PsEXP1, whether this protein was accumulated in the expanding cells of nodule. Immunoblot results indicated the presence of a 30-kDa band specific for pea root nodules. The EXP proteins content rose during growth of pea root nodules. Expansin(s) protein was localized in nodule apoplast as well as in the infection thread walls. The enhanced amount of expansin-like proteins in meristematic part of nodule, root and shoot was shown. The localization of this protein in the meristematic cell walls can be related to the loosening of plant cell wall before cell enlargement. Both, plant cell enlargement and infection thread growth require activity of expansin(s). Possible involvement of EXPs in the process of pea root nodule development is also discussed.
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Mamontova, Tatiana, Elena Lukasheva, Gregory Mavropolo-Stolyarenko, Carsten Proksch, Tatiana Bilova, Ahyoung Kim, Vladimir Babakov, et al. "Proteome Map of Pea (Pisum sativum L.) Embryos Containing Different Amounts of Residual Chlorophylls." International Journal of Molecular Sciences 19, no. 12 (December 15, 2018): 4066. http://dx.doi.org/10.3390/ijms19124066.
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Due to low culturing costs and high seed protein contents, legumes represent the main global source of food protein. Pea (Pisum sativum L.) is one of the major legume crops, impacting both animal feed and human nutrition. Therefore, the quality of pea seeds needs to be ensured in the context of sustainable crop production and nutritional efficiency. Apparently, changes in seed protein patterns might directly affect both of these aspects. Thus, here, we address the pea seed proteome in detail and provide, to the best of our knowledge, the most comprehensive annotation of the functions and intracellular localization of pea seed proteins. To address possible intercultivar differences, we compared seed proteomes of yellow- and green-seeded pea cultivars in a comprehensive case study. The analysis revealed totally 1938 and 1989 nonredundant proteins, respectively. Only 35 and 44 proteins, respectively, could be additionally identified after protamine sulfate precipitation (PSP), potentially indicating the high efficiency of our experimental workflow. Totally 981 protein groups were assigned to 34 functional classes, which were to a large extent differentially represented in yellow and green seeds. Closer analysis of these differences by processing of the data in KEGG and String databases revealed their possible relation to a higher metabolic status and reduced longevity of green seeds.
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Morts, Megan E., and Ingrid Silva. "PSIII-38 Pepsin-pancreatin protein digestibility of various protein sources intended for pet food." Journal of Animal Science 97, Supplement_3 (December 2019): 282. http://dx.doi.org/10.1093/jas/skz258.571.
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Abstract Pet food companies need quality protein ingredients to offer new and different options for pet owners. Evaluating these proteins with animal feeding trials are time consuming and expensive. An in vitro (benchtop) method could provide detailed information about protein quality for novel ingredients. Therefore, the objective of this experiment was to develop a pepsin-pancreatin digestibility assay and determine the appropriate incubation time for enzyme hydrolysis to approximate results from animal studies. Ingredients evaluated were faba beans, navy beans, spray-dried granulated egg, chick pea, pea protein concentrate (72% CP and 50% CP), green field peas, and sunflower meal. One gram of test ingredient was mixed with an HCl-pepsin solution and then incubated for 3 or 6 hours at 37°C before NaOH was added, stopping the pepsin reaction. Phosphate buffer with pancreatin was then added and the tubes were incubated for an additional 18 hours. Samples were then centrifuged, washed, filtered, and dried at 105°C overnight. Residual protein was determined with a modified Kjeldahl assay and was used to calculate protein digestibility. Data were analyzed using the GLIMMIX procedure for mixed models (SAS v 9.4, SAS Institute Inc, Cary, NC). There was no interaction between test ingredient and time (P = 0.63). Incubation time did not influence protein digestibility (P = 0.69). Test ingredient did impact protein digestibility. Spray-dried granulated egg, faba bean, green field pea, and pea protein concentrate (50% CP) did not differ with digestibilities above 97% (P < 0.0001). Navy bean had a digestibility of 93%. The lowest digestibilities were sunflower meal and pea protein concentrate (72% CP). Overall, the crude protein digestibility was higher than expected. This data would suggest other factors, such as the amount and activity of the enzyme used, should be altered to obtain digestibility values that are consistent with reported values from animal studies.
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Immonen, Mika, Angga Chandrakusuma, Juhani Sibakov, Minna Poikelispää, and Tuula Sontag-Strohm. "Texturization of a Blend of Pea and Destarched Oat Protein Using High-Moisture Extrusion." Foods 10, no. 7 (July 1, 2021): 1517. http://dx.doi.org/10.3390/foods10071517.
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Grain protein fractions have great potential as ingredients that contain high amounts of valuable nutritional components. The aim of this study was to study the rheological behavior of destarched oat and pea proteins and their blends in extrusion-like conditions with a closed cavity rheometer. Additionally, the possibility of producing fibrous structures with high-moisture extrusion from a blend of destarched oat and pea protein was investigated. In the temperature sweep measurement (60–160 °C) of the destarched oat protein concentrate and pea protein isolate blend, three denaturation and polymerization sections were observed. In addition, polymerization as a function of time was recorded in the time sweep measurements. The melting temperature of grain proteins was an important factor when producing texturized structures with a high-moisture extrusion. The formation of fibrillar structures was investigated with high-moisture extrusion from the destarched oat and pea protein blend at temperatures ranging from 140 to 170 °C. The protein–protein interactions were significantly influenced in the extruded samples. This was due to a decrease in the amount of extractable protein in selective buffers. In particular, there was a decrease in non-covalent and covalent bonds due to the formation of insoluble protein complexes.
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Lukaszewski, Katherine Marie, Caroline Grace Bowsher, Peter John Savory, and Michael James Emes. "Protein Phosphorylation in Pea Root Plastids." Plant and Cell Physiology 42, no. 6 (June 15, 2001): 642–49. http://dx.doi.org/10.1093/pcp/pce087.
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Baune, Marie-Christin, Sarah Schroeder, Franziska Witte, Volker Heinz, Ute Bindrich, Jochen Weiss, and Nino Terjung. "Analysis of protein-network formation of different vegetable proteins during emulsification to produce solid fat substitutes." Journal of Food Measurement and Characterization 15, no. 3 (February 4, 2021): 2399–416. http://dx.doi.org/10.1007/s11694-020-00767-9.
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AbstractPlant-based emulsion gels can be used as solid animal fat substitutes for vegan sausages. For this reason, commercially available protein isolates with different amino acid profiles from pea, soy and potato (Pea-1, Pea-2, Soy, Potato) have been tested for their ability to form shape stable emulsions gels at neutral pH and upon heating to 72 °C. In order to obtain emulsion gels that are as solid as possible, the protein concentrations in the continuous phase (CPC, 8.0–11.5% (w/w)) and the oil mass fractions (65–80%) were varied. For leguminous proteins, a positive correlation of both parameters on emulsion rigidity was shown, indicating that both, interfacial and protein–protein interactions, are involved in structure reinforcement. Firmness increased with increasing content in cysteine (Pea-1 < Pea-2 < Soy) and the interactions were of electrostatic, hydrophobic and hydrophilic nature. Potato emulsion rigidity was independent of CPC and oil content. The emulsions showed a much higher degree in crosslinking, and very low charge density. Temperature-sweep analysis and CLSM revealed that Potato protein gelled as consequence to low temperature stability. Hence, the structure reinforcement in Potato emulsions mainly contributed to the protein network, with 70% oil and CPC 11.5% forming a hybrid gel with highest firmness. However, gelling of Potato protein also resulted in interfacial adsorption of protein aggregates and reduced interfacial stability with increasing CPC. This was demonstrated in the amount of extractable fat which was 2.0 and 0.6% for Pea-1 and 2 emulsions, 6.4% for Soy and 34.4% of total fat for Potato emulsions.
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Guillin, Florence, Claire Gaudichon, Laetitia Guérin-Deremaux, Catherine Lefranc-Millot, Daniel Tomé, Nadezda Khodorova, Gheorghe Airinei, and Juliane Calvez. "Real Ileal Digestibility of Pea Protein Compared to Casein in Healthy Humans." Current Developments in Nutrition 4, Supplement_2 (May 29, 2020): 634. http://dx.doi.org/10.1093/cdn/nzaa049_027.
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Abstract Objectives The global demand for protein is growing and it seems mandatory to find alternatives to animal proteins that are of good nutritional quality, implying a good digestibility. Legumes are potential candidates, as their indispensable amino acid (IAA) profile is relatively balanced. The aim of this study is to compare the protein and AA ileal digestibility of pea protein and casein in humans using ileal sampling and intrinsically labelled proteins. Methods Sixteen healthy volunteers were intubated and were given twelve doses of mashed potatoes containing either pea protein or milk casein isolates. The proteins were intrinsically labelled with 15N. Polyethylene glycol (PEG) was perfused as a non-absorbable marker to measure the intestinal flow, and ileal digesta were collected during 8 hours after the ingestion of the first meal. PEG content was assessed using a turbidimetric assay. Real ileal nitrogen (N) digestibility was measured by assessing N content and 15N enrichment by EA-IRMS and calculated as follows: $$\begin{eqnarray} \begin{array} \text{Ileal fiow (mL/30 min)} &=& \rm{[PEG]_{solution}/[PEG]_{digesta}}\\ &&\times \text{ infusion rate} \times \rm{time} \end{array} \end{eqnarray}$$$$\begin{eqnarray} \begin{array} \text{Exogenous N fiow (mmol/30 min) } &=& \rm {N_{exo} = (\% DM \times \%N)}\\ &&/(14 \times 10) \times \text{ileal fiow} \times \rm{APE_{digesta}/APE_{meal}} \end{array} \end{eqnarray}$$$$\begin{eqnarray} \rm{Digestibility\ (\%)} = (\rm{N_{ingested} - N_{exo} / N_{ingested} \times 100}) \end{eqnarray}$$$$\begin{eqnarray} \text{WithDM = DryMatterofdigesta, APE = AtomPercentExcess} \end{eqnarray}$$ Results The first results were obtained on 7 subjects that were given pea protein (N = 3) or milk casein (N = 4). The mean ileal flow for all the volunteers was 1.83 ± 0.70 mL/30 min (mean ± SD), and was quite stable over time. The total N exogenous flow was 15.50 ± 5.83 mmol for pea protein and 13.56 ± 3.48 mmol for casein. The true ileal N digestibility was 95.40 ± 1.73% for pea protein and 95.42 ± 1.17% for casein. Ileal IAA digestibility is in progress. Conclusions The intermediate results show no difference between pea protein and casein in terms of ileal digestibility, suggesting that pea protein could be a promising plant-based alternative. AA digestibilities and data from the remaining 9 volunteers to be tested will complete the study. Funding Sources Roquette.
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Häberer, Doreen, Maria Tasker, Martin Foltz, Nori Geary, Margriet Westerterp, and Wolfgang Langhans. "Intragastric infusion of pea-protein hydrolysate reduces test-meal size in rats more than pea protein." Physiology & Behavior 104, no. 5 (October 2011): 1041–47. http://dx.doi.org/10.1016/j.physbeh.2011.07.003.
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Trencia, Alessandra, Anna Perfetti, Angela Cassese, Giovanni Vigliotta, Claudia Miele, Francesco Oriente, Stefania Santopietro, et al. "Protein Kinase B/Akt Binds and Phosphorylates PED/PEA-15, Stabilizing Its Antiapoptotic Action." Molecular and Cellular Biology 23, no. 13 (July 1, 2003): 4511–21. http://dx.doi.org/10.1128/mcb.23.13.4511-4521.2003.
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ABSTRACT The antiapoptotic protein PED/PEA-15 features an Akt phosphorylation motif upstream from Ser116. In vitro, recombinant PED/PEA-15 was phosphorylated by Akt with a stoichiometry close to 1. Based on Western blotting with specific phospho-Ser116 PED/PEA-15 antibodies, Akt phosphorylation of PED/PEA-15 occurred mainly at Ser116. In addition, a mutant of PED/PEA-15 featuring the substitution of Ser116→Gly (PEDS116→G) showed 10-fold-decreased phosphorylation by Akt. In intact 293 cells, Akt also induced phosphorylation of PED/PEA-15 at Ser116. Based on pull-down and coprecipitation assays, PED/PEA-15 specifically bound Akt, independently of Akt activity. Serum activation of Akt as well as BAD phosphorylation by Akt showed no difference in 293 cells transfected with PED/PEA-15 and in untransfected cells (which express no endogenous PED/PEA-15). However, the antiapoptotic action of PED/PEA-15 was almost twofold reduced in PEDS116→G compared to that in PED/PEA-15WT cells. PED/PEA-15 stability closely paralleled Akt activation by serum in 293 cells. In these cells, the nonphosphorylatable PEDS116→G mutant exhibited a degradation rate threefold greater than that observed with wild-type PED/PEA-15. In the U373MG glioma cells, blocking Akt also reduced PED/PEA-15 levels and induced sensitivity to tumor necrosis factor-related apoptosis-inducing ligand apoptosis. Thus, phosphorylation by Akt regulates the antiapoptotic function of PED/PEA-15 at least in part by controlling the stability of PED/PEA-15. In part, Akt survival signaling may be mediated by PED/PEA-15.
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Oleskina, Yu P., N. P. Yurina, T. I. Odintsova, Ts A. Egorov, A. Otto, B. Wittmeann-Liebold, and M. S. Odintsova. "Nucleoid proteins of pea chloroplasts: detection of a protein homologous to ribosomal protein." IUBMB Life 47, no. 5 (May 1999): 757–63. http://dx.doi.org/10.1080/15216549900201843.
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Markovic, Jordan, Milomer Blagojevic, Ivica Kostic, Tanja Vasic, Snezana Andjelkovic, Mirjana Petrovic, and Dragoslav Djokic. "Protein fractions of intercropped pea and oat for ruminant nutrition." Biotehnologija u stocarstvu 33, no. 2 (2017): 243–49. http://dx.doi.org/10.2298/bah1702243m.
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The quantification of the main crude protein (CP) fractions during the growing period of pea and oat mixtures may be used to optimize the forage management. The determination of protein fraction could improve balancing rations for ruminants. The first factor (A) is ratio of germinated seed in mixtures. The pea and oat were tested at two different mixture rates: A1 ? 50% pea + 50% oat and A2 ? 75% pea + 25% oat. The second factor (B) is a cutting time in three stages of growth: B1 ? a cutting of biomass at the start of flowering pea (10% of flowering), B2 ? a cutting of biomass at forming the first pods on 2/3 plants of pea, and B3 ? cutting of biomass at forming green seeds in 2/3 pods. Stage of growth and pea-oat ratio in mixtures are significantly related to the change in the quality and chemical composition of biomass. The highest level of crude protein was obtained in pea at flowering stage (184.85 g kg-1 dry matter (DM)). The high level of easily soluble protein and non-protein nitrogen compounds (over 50%) represent specific characteristics of the mixture. Unavailable fraction PC increased with plant maturation from 75.65 to 95.05 g kg-1 of CP.
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Stanisavljevic, Nemanja, Goran Vukotic, Ferenc Pastor, Desanka Suznjevic, Zivko Jovanovic, Ivana Strahinic, Djordje Fira, and Svetlana Radovic. "Antioxidant activity of pea protein hydrolysates produced by batch fermentation with lactic acid bacteria." Archives of Biological Sciences 67, no. 3 (2015): 1033–42. http://dx.doi.org/10.2298/abs150130066s.
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Nine Lactobacillus strains known for surface proteinase activity were chosen from our collection and tested for their ability to grow in pea seed protein-based medium, and to hydrolyze purified pea proteins in order to produce peptides with antioxidant (AO) activity. Two strains, Lactobacillus rhamnosus BGT10 and Lactobacillus zeae LMG17315, exhibited strong proteolytic activity against pea proteins. The AO activity of the pea hydrolysate fraction, MW <10 kDa, obtained by the fermentation of purified pea proteins with Lactobacillus rhamnosus BGT10, was tested by standard spectrophotometric assays (DPPH, ABTS, Fe3+-reducing capacity) and the recently developed direct current (DC) polarographic assay. The low molecular weight fraction of the obtained hydrolysate was separated using ion exchange chromatography, while the AO activity of eluted fractions was determined by means of a sensitive DC polarographic assay without previous concentration of samples. Results revealed that the fraction present in low abundance that contained basic peptides possessed the highest antioxidant activity. Based on the obtained results, it can be concluded that Lactobacillus rhamnosus BGT10 should be further investigated as a candidate strain for large-scale production of bioactive peptides from legume proteins.
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Aider, Mohammed, Maxime Sirois-Gosselin, and Joyce Irene Boye. "Pea, Lentil and Chickpea Protein Application in Bread Making." Journal of Food Research 1, no. 4 (October 30, 2012): 160. http://dx.doi.org/10.5539/jfr.v1n4p160.
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The objective of the present study was to determine if wheat flour could be successfully substituted with lentil, pea, and chickpea (pulses) proteins in bread making and to study the characteristics of the breads produced. Results of the study showed that addition of pulse proteins affected bread mass volume, color and hardness. The highest bread mass volume (4.27 ± 0.07 mL/g) was obtained with the control (unsupplemented) bread. Mass volumes decreased at the 3% supplementation level for all supplemented breads and no significant differences (P>0.05) were observed between the pulse proteins. At the 6% and 9% supplementation levels, significant differences were observed between the mass volumes of the breads. Chickpea protein gave the highest mass volume at both the 6% and 9% supplementation levels (3.72 ± 0.21 and 3.84 ± 0.27 mL/g, respectively) followed by lentil protein (3.43 ± 0.19 and 3.43 ± 0.07 mL/g, respectively). Breads supplemented with pea protein generally had the lowest mass volume. Bread crumb and white became darker as supplementation level was increased and in the lentil supplemented bread, a greener color appeared at the 6% and 9% supplementation levels. Hardness of the bread white for all supplemented samples was close to the control at the 3% supplementation level but significantly increased at the 9% supplementation level. Overall, pea proteins had the most significant effect on bread hardness and mass volume whereas chickpea protein concentrate showed the greatest potential for use as an ingredient in bread making.
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Pinckaers, Philippe J. M., Imre W. K. Kouw, Stefan H. M. Gorissen, Joan M. Senden, Lisette C. P. G. M. de Groot, Lex B. Verdijk, Tim Snijders, and Luc J. C. van Loon. "The Muscle Protein Synthetic Response to the Ingestion of a Plant-Based Protein Blend Is Not Different From Milk Protein in Healthy, Young Males." Current Developments in Nutrition 5, Supplement_2 (June 2021): 517. http://dx.doi.org/10.1093/cdn/nzab041_032.
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Abstract Objectives It has been reported that plant-based proteins are not as effective as animal-based proteins in their capacity to stimulate muscle protein synthesis rates. This has been attributed to the lower essential amino acid content and the selective deficiency in specific amino acids. It has been hypothesized that a blend of different plant-based proteins may complement each other and, as such, compensate for such deficits. This study compares post-prandial muscle protein synthesis rates following the ingestion of 30 g milk protein with the ingestion of a 30 g blend of wheat, corn, and pea protein in vivo, in healthy young males. Methods In a randomized, double blind, parallel-group design, 24 healthy young males (24 ± 4 y) received a primed continuous infusion of L-[ring-13C6]-phenylalanine and ingested 30 g milk protein (MILK), or a 30 g protein blend with 15 g wheat, 7.5 g corn, and 7.5 g pea protein (PLANT) in beverage form (n = 12 per group). Both interventional drinks were matched for leucine content. Blood and muscle biopsies were collected for 5 h following protein ingestion to assess post-prandial plasma amino acid profiles and myofibrillar protein synthesis rates. Data are expressed as mean ± SD. Results MILK increased plasma essential amino acid concentrations ∼2 fold more than PLANT over the 5 h post-prandial period (incremental area under curve (iAUC): 151 ± 31 vs 79 ± 12 mmol∙5 h∙L−1 respectively; P < 0.001). Similarly, the leucine iAUC was ∼16% greater for MILK vs PLANT (36 ± 7 vs 31 ± 4 mmol∙5 h∙L−1 respectively; P < 0.05). Ingestion of both MILK and PLANT increased myofibrillar protein synthesis rates when compared to basal post-absorptive values (P < 0.001), with no significant differences between treatments (0.053 ± 0.013 vs 0.064 ± 0.016%∙h−1, respectively; P > 0.05). Conclusions Ingestion of 30 g of a wheat, corn, and pea protein blend increases muscle protein synthesis rates in healthy, young males. The post-prandial muscle protein synthetic response to the ingestion of 30 g of a wheat, corn and pea protein blend does not differ from the ingestion of an equivalent amount of milk protein in healthy, young males. Funding Sources TiFN
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Mercier, Samuel, Sébastien Villeneuve, Martin Mondor, Hélène Drolet, Denis Ippersiel, François Lamarche, and Louis-Philippe Des Marchais. "Mixing Properties and Gluten Yield of Dough Enriched with Pea Protein Isolates." Journal of Food Research 1, no. 1 (January 31, 2012): 13. http://dx.doi.org/10.5539/jfr.v1n1p13.
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<p>Over the last few years, many studies were carried out on the use of legume-based ingredients to supplement cereal-based matrices and produce nutritionally enhanced products. However, little is known about the influence of supplementation on the mixing properties of the enriched cereal-based matrices. The objective of this work was to study the impact of supplementing cereal-based matrices with commercial pea protein isolate or pea protein isolate produced by ultrafiltration/diafiltration using a 50 kDa membrane on the dough mixing properties. Studies were performed using a PertenÒ Glutomatic to estimate gluten yield, namely in terms of gluten index, wet gluten, dry gluten and water binding capacity, and using a BrabenderÒ Farinograph to estimate water absorption, dough development time, stability, mixing tolerance index and minimum and maximum water content for dough formation. Four levels of pea protein isolate enrichment were considered: 0, 5, 10 and 15%. Results indicated that level of enrichment has little effect on measured mixing properties compared to the pea protein isolates considered. Isolate processed by membrane technologies takes part to the dough formation which does not seem to be the case with commercial isolate. Higher amount of water is required for dough formation with matrices enriched with commercial pea isolate compared to membrane processed isolate, while stronger dough properties are observed for matrices enriched with membrane processed isolate. This is attributable to the properties of the isolate, namely solubility and state of the proteins (native or denatured), which could impact how they interact with wheat proteins.</p>
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Małecki, Jan, Igor Tomasevic, Ilija Djekic, and Bartosz G. Sołowiej. "The Effect of Protein Source on the Physicochemical, Nutritional Properties and Microstructure of High-Protein Bars Intended for Physically Active People." Foods 9, no. 10 (October 15, 2020): 1467. http://dx.doi.org/10.3390/foods9101467.
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The purpose of this study was to investigate the effect of protein sources (algae, pumpkin, wheat, sunflower, rice, soy, hemp, pea, and whey) on selected physicochemical, nutritional, and structural parameters of high-protein bars. Texture properties, such as hardness, fracturability, cohesiveness, and adhesiveness, have changed depending on the type of protein used. A significant increase, in particular the hardness parameter relating to the control sample (whey protein concentrate—WPC80), was noted for bars containing algae, sunflower, and wheat proteins, with high values of the adhesiveness parameter concurrently. The use of proteins from algae, pea, and wheat resulted in a significant reduction in the water activity of the finished product compared to WPC80. Bars made with the use of wheat, hemp and pumpkin proteins had noticeably higher viscosities than other samples. Color of the tested bars measured by means of Computer Vision System (CVS) was from light cream (soy, pea) to dark green (hemp, pumpkin). Bars prepared of wheat and algae proteins had the highest nutritional value, while the lowest one was recorded in products containing sunflower and hemp proteins. There was a clear differentiation of amino acids (g/100 g) and microstructure in bars depending on the type of protein used. However, a slight similarity can be found between whey and soy proteins (amino acids) and between whey and sunflower proteins (microstructure). Obtained results suggest that selection of the right type of protein for a given application may have a significant impact on the physicochemical features and microstructure of high-protein bars and their nutritional values.
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Bladergroen, M. R., K. Badelt, and H. P. Spaink. "Infection-Blocking Genes of a Symbiotic Rhizobium leguminosarum Strain That Are Involved in Temperature-Dependent Protein Secretion." Molecular Plant-Microbe Interactions® 16, no. 1 (January 2003): 53–64. http://dx.doi.org/10.1094/mpmi.2003.16.1.53.
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Rhizobium leguminosarum strain RBL5523 is able to form nodules on pea, but these nodules are ineffective for nitrogen fixation. The impairment in nitrogen fixation appears to be caused by a defective infection of the host plant and is host specific for pea. A Tn5 mutant of this strain, RBL5787, is able to form effective nodules on pea. We have sequenced a 33-kb region around the phage-transductable Tn5 insertion. The Tn5 insertion was localized to the 10th gene of a putative operon of 14 genes that was called the imp (impaired in nitrogen fixation) locus. Several highly similar gene clusters of unknown function are present in Pseudomonas aeruginosa, Vibrio cholerae, Edwardsiella ictaluri, and several other animal pathogens. Homology studies indicate that several genes of the imp locus are involved in protein phosphorylation, either as a kinase or dephosphorylase, or contain a phosphoprotein-binding module called a forkhead-associated domain. Other proteins show similarity to proteins involved in type III protein secretion. Two dimensional gel electrophoretic analysis of the secreted proteins in the supernatant fluid of cultures of RBL5523 and RBL5787 showed the absence in the mutant strain of at least four proteins with molecular masses of approximately 27 kDa and pIs between 5.5 and 6.5. The production of these proteins in the wild-type strain is temperature dependent. Sequencing of two of these proteins revealed that their first 20 amino acids are identical. This sequence showed homology to that of secreted ribose binding proteins (RbsB) from Bacilus subtilis and V. cholerae. Based on this protein sequence, the corresponding gene encoding a close homologue of RbsB was cloned that contains a N-terminal signal sequence that is recognized by type I secretion systems. Inoculation of RBL5787 on pea plants in the presence of supernatant of RBL5523 caused a reduced ability of RBL5787 to nodulate pea and fix nitrogen. Boiling of this supernatant before inoculation restored the formation of effective nodules to the original values, indicating that secreted proteins are indeed responsible for the impaired phenotype. These data suggest that the imp locus is involved in the secretion to the environment of proteins, including periplasmic RbsB protein, that cause blocking of infection specifically in pea plants.
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McCurdy, D. W., and R. E. Williamson. "An actin-related protein inside pea chloroplasts." Journal of Cell Science 87, no. 3 (April 1, 1987): 449–56. http://dx.doi.org/10.1242/jcs.87.3.449.
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A pea chloroplast protein resembles vertebrate and algal actins by several chemical and immunological criteria. On two-dimensional polyacrylamide gels it migrated with a slightly lower relative molecular mass (Mr = 41,000) and slightly more basic isoelectric point than rabbit skeletal muscle actin. A monoclonal antibody to chicken gizzard actin reacted on immunoblots with rabbit skeletal actin, with Chara actin and with a 41,000 Mr band from pea chloroplasts. Pea and Chara bands of approximately 58,000 Mr were also stained. A DNase I-affinity column that bound muscle actin also bound 41,000 and 58,000 Mr chloroplast polypeptides. Similarities existed between enzymically and chemically generated fragments of the 41,000 Mr chloroplast polypeptide and rabbit muscle actin. The 41,000 Mr protein was protected from degradation by thermolysin only in preparations of intact, but not ruptured, isolated chloroplasts, indicating that this protein resides within the outer envelope membrane of these organelles. It is concluded that a 41,000 Mr protein with major similarities to actin occurs inside pea chloroplasts, and that a 58,000 Mr protein with some similarities to actin also probably exists within chloroplasts.
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Florowska, Anna, Adonis Hilal, Tomasz Florowski, and Małgorzata Wroniak. "Addition of Selected Plant-Derived Proteins as Modifiers of Inulin Hydrogels Properties." Foods 9, no. 7 (June 29, 2020): 845. http://dx.doi.org/10.3390/foods9070845.
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The aim of the study was to determine the effects of pea and soy protein addition (1, 3, 6 g/100 g) on inulin hydrogels properties. Inulin hydrogels (20 g/100 g) were obtained by thermal induction. It was stated that tested plant protein might be used as a modifier of inulin hydrogels properties. The addition of pea and soy protein to inulin hydrogels resulted in networks with more a compact and homogeneous structure. The increase of the protein concentration caused the structure of the hydrogels to get smoother, more cohesive, and less granular. Pea and soy protein addition (3–6 g/100 g) to hydrogels allowed to obtain higher values of yield stress, texture (firmness, adhesiveness) and spreadability parameters. At a protein concentration of 6 g/100 g, the firmness of inulin hydrogels was seven times higher for those with pea protein (1.87 N) and ten times higher for those with soy protein (2.60 N) compering to the control hydrogel (0.24 N). The transmission profiles of hydrogels with incorporated 6 g/100 g of soy proteins showed the slowest motion of the particles, which indicates the highest stability of gel. As the concentration of protein addition increased, a reduction in the lightness was observed.
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Yin, Baoru, Rujing Zhang, and Ping Yao. "Influence of Pea Protein Aggregates on the Structure and Stability of Pea Protein/Soybean Polysaccharide Complex Emulsions." Molecules 20, no. 3 (March 20, 2015): 5165–83. http://dx.doi.org/10.3390/molecules20035165.
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Congdon, B. S., B. A. Coutts, M. Renton, M. Banovic, and R. A. C. Jones. "Pea seed-borne mosaic virus in Field Pea: Widespread Infection, Genetic Diversity, and Resistance Gene Effectiveness." Plant Disease 100, no. 12 (December 2016): 2475–82. http://dx.doi.org/10.1094/pdis-05-16-0670-re.
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From 2013 to 2015, incidences of Pea seed-borne mosaic virus (PSbMV) infection were determined in semi-leafless field pea (Pisum sativum) crops and trial plots growing in the Mediterranean-type environment of southwest Australia. PSbMV was found at incidences of 2 to 51% in 9 of 13 crops, 1 to 100% in 20 of 24 cultivar plots, and 1 to 57% in 14 of 21 breeding line plots. Crops and plots of ‘PBA Gunyah’, ‘Kaspa’, and ‘PBA Twilight’ were frequently PSbMV infected but none of PSbMV resistance gene sbm1-carrying ‘PBA Wharton’ plants were infected. In 2015, 14 new PSbMV isolates obtained from these various sources were sequenced and their partial coat protein (CP) nucleotide sequences analyzed. Sequence identities and phylogenetic comparison with 39 other PSbMV partial CP nucleotide sequences from GenBank demonstrated that at least three PSbMV introductions have occurred to the region, one of which was previously unknown. When plants of ‘Greenfeast’ and PBA Gunyah pea (which both carry resistance gene sbm2) and PBA Wharton and ‘Yarrum’ (which carry sbm1) were inoculated with PSbMV pathotype P-2 isolate W1, resistance was overcome in a small proportion of plants of each cultivar, showing that resistance-breaking variants were likely to be present. An improved management effort by pea breeders, advisors, and growers is required to diminish infection of seed stocks, avoid sbm gene resistance being overcome in the field, and mitigate the impact of PSbMV on seed yield and quality. A similar management effort is likely to be needed in field pea production elsewhere in the world.
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Mazhar, H., and S. M. Basha. "Immunochemical characterisation of a methionine-rich protein from peanut." Australian Journal of Experimental Agriculture 44, no. 12 (2004): 1221. http://dx.doi.org/10.1071/ea03061.
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Peanuts (Arachis hypogeae L. cv. Florunner), like other legumes, are low in sulfur-containing amino acids such as methionine and cysteine. Previous research from our laboratory has resulted in the identification and isolation of a methionine-rich protein (MRP) from peanut. To determine the differential deposition pattern of MRP during seed development and its breakdown pattern during seed germination, immunological studies were conducted using antibodies raised against MRP. The results showed that MRP-3 was deposited very early (in the ‘white’ maturity stage), while the MRP-5 accumulated at a later (the ‘yellow’ maturity stage) stage of seed development. Germination studies showed that MRP-3 degraded after 8 days of germination, while MRP-5 degraded after 10 days of germination. The MRP-3 antibody detected homologous proteins in several other legumes and cereals such as pea, pigeon pea, chick pea, red lentil, brown lentil, rice and wheat, while the MRP-5 antibody reacted with extracts from pea, chick pea and French bean, thus showing a conservation of the MRP subunits across species.
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Näsi, Matti, and Tuomo Kiiskinen. "Leaf protein from green pulse crops and nutritive value of legume protein concentrates for poultry." Agricultural and Food Science 57, no. 2 (May 1, 1985): 117–23. http://dx.doi.org/10.23986/afsci.72192.
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Leaf protein concentrate (LPC) samples were prepared from four pulse crops, goat’s rue, pea, field bean and Persian clover. Their proximate composition was 42.5— 53.4 % crude protein, 2.1—7.9 % ether extract and 1.0—3.0 % crude fibre. The lysine content was 4.1—4.8 g/ 16 g N, that of sulphur amino acids 2.0—2.8 g and that of threonine 4.5—4.8 g. The contents of tannins varied from 2.2 to 5.5 %. The nutritional values of the LPC samples were assesed in digestibility and balance trials with male chickens of 16—18 weeks, LPC composing 25 % of the diets. LPC from pea had the highest digestibilities of organic matter (70.3 %), crude protein (77.6 %) and carbohydrates (54.9 %), while LPC from Persian clover had the lowest (P < 0.01). The true digestibilities of crude protein for goat’s rue, pea, field bean and Persian clover were, respectively, 70.0, 82.2, 69,7 and 56.8 % (P < 0.01). The digestibilities of nutrients in the present LPC samples were rather low compared to their minimal crude fibre content. A reason for this may be the contents of tannins. The AMEN values for the LPC’s of goat’s rue, pea, field bean and Persian clover were, respectively, 10.79, 13.15, 9.80 and 9.18 (P < 0.01). The gross energy metabolization ranged from 42.6 to 57.0 %.
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Hou, Xingwei, Paul Fields, and Wes Taylor. "Combination of protein-rich pea flour and pea extract with insecticides and enzyme inhibitors for control of stored-product beetles." Canadian Entomologist 136, no. 4 (August 2004): 581–90. http://dx.doi.org/10.4039/n03-077.
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AbstractProtein-rich pea flour and its extract are toxic to stored-product beetles and, at a concentration of 0.1%, can control these insects in a granary. To reduce the concentration of protein-rich pea flour needed to control stored-product beetles, natural products or currently used grain protectants (diatomaceous earth, neem, Bacillus thuringiensis (Berliner), malathion, and pyrethrum) were mixed with protein-rich pea flour in wheat. Mixtures were tested against the rice weevil, Sitophilus oryzae (L.) (Coleoptera: Curculionidae), the red flour beetle, Tribolium castaneum (Herbst) (Coleoptera: Tenebrionidae), and the rusty grain beetle, Cryptolestes ferrugineus (Stephens) (Coleoptera: Cucujidae). Neem and protein-rich pea flour acted synergistically against T. castaneum. Malathion and protein-rich pea flour acted synergistically against S. oryzae. Protein-rich pea flour combined with diatomaceous earth or pyrethrum acted additively against S. oryzae. All other combinations acted antagonistically. An extract from protein-rich pea flour reduced feeding of S. oryzae, and three enzyme inhibitors, piperonyl butoxide, profenofos, and diethyl maleate, were tested for their possible synergistic effects on feeding deterrence and mortality. Piperonyl butoxide and pea extract had additive effects, and diethyl maleate had no effect on the feeding and mortality of insects. Profenofos alone killed all insects in 3 days. The flour consumption of S. oryzae was positively correlated with LT50 (time to 50% mortality) in flour disks treated with pea extract.
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Moreno, Cecilia, Luis Mojica, Elvira González de Mejía, Rosa María Camacho Ruiz, and Diego A. Luna-Vital. "Combinations of Legume Protein Hydrolysates Synergistically Inhibit Biological Markers Associated with Adipogenesis." Foods 9, no. 11 (November 17, 2020): 1678. http://dx.doi.org/10.3390/foods9111678.
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The objective was to investigate the anti-adipogenesis potential of selected legume protein hydrolysates (LPH) and combinations using biochemical assays and in silico predictions. Black bean, green pea, chickpea, lentil and fava bean protein isolates were hydrolyzed using alcalase (A) or pepsin/pancreatin (PP). The degree of hydrolysis ranged from 15.5% to 35.5% for A-LPH and PP-LPH, respectively. Antioxidant capacities ranged for ABTS•+ IC50 from 0.3 to 0.9 Trolox equivalents (TE) mg/mL, DPPH• IC50 from 0.7 to 13.5 TE mg/mL and nitric oxide (NO) inhibition IC50 from 0.3 to 1.3 mg/mL. LPH from PP–green pea, A–green pea and A–black bean inhibited pancreatic lipase (PL) (IC50 = 0.9 mg/mL, 2.2 mg/mL and 1.2 mg/mL, respectively) (p < 0.05). For HMG-CoA reductase (HMGR) inhibition, the LPH from A–chickpea (0.15 mg/mL), PP–lentil (1.2 mg/mL), A–green pea (1.4 mg/mL) and PP–green pea (1.5 mg/mL) were potent inhibitors. Combinations of PP–green pea + A–black bean (IC50 = 0.4 mg/mL), A–green pea + PP–green pea (IC50 = 0.9 mg/mL) and A–black bean + A–green pea (IC50 = 0.6 mg/mL) presented synergistic effects to inhibit PL. A–chickpea + PP–lentil (IC50 = 0.8 mg/mL) and PP–lentil + A–green pea (IC50 = 1.3 mg/mL) interacted additively to inhibit HMGR and synergistically in the combination of A–chickpea + PP–black bean (IC50 = 1.3 mg/mL) to block HMGR. Peptides FEDGLV and PYGVPVGVR inhibited PL and HMGR in silico, showing predicted binding energy interactions of −7.6 and −8.8 kcal/mol, respectively. Combinations of LPH from different legume protein sources could increase synergistically their anti-adipogenic potential.
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VLACHOSTERGIOS, D. N., C. A. DORDAS, and A. S. LITHOURGIDIS. "FORAGE YIELD, PROTEIN CONCENTRATION AND INTERSPECIFIC COMPETITION IN RED PEA-CEREAL INTERCROPS." Experimental Agriculture 51, no. 4 (January 29, 2015): 635–50. http://dx.doi.org/10.1017/s0014479714000519.
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SUMMARYRed pea (Lathyrus cicera L.) is an underutilized protein crop with broad adaptability. Intercrops of red pea with winter cereals have not been studied. A two years field study was conducted with the objective to determine the productivity of intercropping systems of red pea with barley (Hordeum vulgare L.) and triticale (xTriticosecale Wittmack) in two seeding ratios (60:40 and 80:20). Growth rate, dry matter yield, protein content and yield were determined. Several indices were used to evaluate the intercropping systems and analyse competition and interrelationships between mixture components. Growth rate of cereals was lower in the mixtures than in the monocrops. Dry matter yield were the highest in barley monocrop and its intercrop with red pea at 60:40 seeding ratio. Red pea monocrop showed the highest crude protein concentration followed by its intercrops. The land equivalent ratio, relative crowding coefficient (K), actual yield loss (AYL) and system productivity index values were greater for the red pea-barley 60:40 mixture, indicating an advantage of intercropping. The partial K, aggressivity, competitive ratio and partial AYL values indicated red pea as the dominated species in the intercrops. The highest monetary advantage value was recorded for the red pea-barley mixture (60:40). The results indicate that red pea-barley mixture (60:40) was the most productive and produced better forage quality and thus could be adopted by the farmers as alternative option for forage production.
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Fiory, Francesca, Pietro Formisano, Giuseppe Perruolo, and Francesco Beguinot. "Frontiers: PED/PEA-15, a multifunctional protein controlling cell survival and glucose metabolism." American Journal of Physiology-Endocrinology and Metabolism 297, no. 3 (September 2009): E592—E601. http://dx.doi.org/10.1152/ajpendo.00228.2009.
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PED/PEA-15 is a 15-kDa ubiquitously expressed protein implicated in a number of fundamental cellular functions, including apoptosis, proliferation, and glucose metabolism. PED/PEA-15 lacks enzymatic function and serves mainly as a molecular adaptor. PED/PEA-15 is an endogenous substrate for protein kinase C (PKC), calcium/calmodulin-dependent protein kinase II (CAM kinase II), and Akt. In particular, PKC phosphorylates PED/PEA-15 at Ser104 and CAM kinase II or Akt at Ser116, modifying its stability. Evidence obtained over the past 10 years has indicated that PED/PEA-15 regulates cell survival by interfering with both intrinsic and extrinsic apoptotic pathways. In addition, it may also control cell proliferation by interfering with ERK1/2-mediated pathways. Indeed, PED/PEA-15 has been identified as an ERK1/2 interactor, which modifies its subcellular localization and targeting to a specific subset of substrates. Increased PED/PEA-15 levels may affect tumorigenesis and cancer progression as well as sensitivity to anticancer agents. Moreover, PED/PEA-15 affects astrocyte motility and increases susceptibility to skin carcinogenesis in vivo. PED/PEA-15 expression is regulated at the transcriptional and the posttranslational levels. Increased PED/PEA-15 expression has been identified in individuals with type 2 diabetes early during the natural history of the disease. Evidence generated over the past 10 years indicated that this defect contributes to altering glucose tolerance by impairing insulin action and insulin secretion and might play a role in the development of diabetes-associated neurological disorders. Strategies are being devised to target key signaling events in PED/PEA-15 action aimed at improving glucose tolerance and at facilitating cancer cell death.
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Nesterenko, O. G., S. V. Litvinov, and N. M. Rashydov. "The protein expression changes during the signaling systems interaction in stressed pea seedlings." Faktori eksperimental'noi evolucii organizmiv 22 (September 9, 2018): 154–61. http://dx.doi.org/10.7124/feeo.v22.941.
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Aim. The plant’s signaling systems functioning under stress impact is expressed in changes of the genes expression and protein synthesis. The purpose of this study is to investigate the effect of stressors and their combinations on pea seedlings at the molecular level, qualitative and quantitative changes in the spectrum of plant proteins. Methods. This phenomenon were investigated on four experimental groups: control seedlings, plants irradiated with gamma rays in the dose of 10 Gy, pea exposed to salt stress (0.22 Mol/L NaCl solution) and both stressors consequently. Proteins were isolated from each group and analyzed using ultra-high performance liquid chromatography. Results and conclusions. We observed the modification of expression of eight identified proteins: transketolase, malate dehydrogenase (43.52 kDa and 41.98 kDa), translation elongation factor EF-2 subunit, 14-3-3-like protein, heat shock cognate protein 80, heat shock cognate 70 kDa-like, 14-3-3-like protein B. Their significant role in the stress signals transduction and in the processes of forming an active response to the adverse factors is confirmed by concentration fluctuations between groups. The largest number of proteins has changed in response to the combined effect of ionizing radiation and salinity. Each factor by itself cause changes in less quantity of proteins.Keywords: signaling systems, proteins, pea seedlings, stress factors.
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García-Segovia, Purificación, Marta Igual, and Javier Martínez-Monzó. "Beetroot Microencapsulation with Pea Protein Using Spray Drying: Physicochemical, Structural and Functional Properties." Applied Sciences 11, no. 14 (July 20, 2021): 6658. http://dx.doi.org/10.3390/app11146658.
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Beetroot is a root vegetable with carotenoids, phenols, vitamins, minerals, and water-soluble betalain pigments such as betacyanins (red-violet color) and betaxanthins (yellow-orange color), which have many nutritional and health benefits. Its use in the food industry is mainly as a powdered natural dye. This study aims to investigate the effect of adding pea protein to beetroot juice as an encapsulating agent, and the spray-dried temperature on the physicochemical, structural, and functional properties of the powder. The spray drying was conducted at 125 and 150 °C with 3.5% and 7% pea protein used in the mixtures with the beetroot juice. The water content, bulk density, porosity, hygroscopicity, water solubility, water absorption index, color, and microstructure of the obtained powder were determined. In addition, betacyanin, total phenols, antioxidant capacity, and powder encapsulate efficiency were analyzed. Using pea protein in the spray drying of beetroot juice had shown high yields of spray drying and good characteristics of the powdered product. Beetroot powder with 7% of pea protein was more porous and luminous, and less hygroscopic than beetroot powder with 3.5% of pea protein. However, the use of 7% of pea protein increased the amount of water immobilized by the samples and reduced the soluble solids present in the product compared to beetroot powder with 3.5% of pea protein. The use of 7% of pea protein protected beetroot bioactive compound higher than the use of 3.5%. Higher spray-drying temperature (150 °C) significantly decreased phenols content and antioxidant capacity of the beetroot powders (p < 0.05). Results showed using 7% pea protein mixed with beetroot juice and a 125 °C spray-drying temperature gave the most content of the studied bioactive compounds and antioxidant capacity. Moreover, the proposal gives more stable powders from a functionality viewpoint because it showed the higher encapsulate efficiency.
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Shen, Shian, Hongwei Hou, Chunbang Ding, Deng-Jin Bing, and Zhen-Xiang Lu. "Protein content correlates with starch morphology, composition and physicochemical properties in field peas." Canadian Journal of Plant Science 96, no. 3 (June 1, 2016): 404–12. http://dx.doi.org/10.1139/cjps-2015-0231.
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Protein and starch are two major components in field peas. In this study, we investigated the starch morphologies, compositions, and thermal properties between high protein peas (approximately 30%) and other market types of field peas (yellow, green, maple, and marrowfat peas, with approximately 23% protein contents). For the shape and size, high protein peas had the compound starch granules that could be easily fragmented into small irregular and polygonal granules, whereas other pea types had oval or kidney-like starch granules with high percentage of large granule sizes. High protein peas had significantly lower starch contents (27.2%–34.2%) than other pea types (45.5%–47.4%). However, the amylose content (74.6%–89.2%) in high protein peas were significantly higher that of other pea types (50.1%–54.1%). Our differential scanning calorimeter (DSC) data showed that the onset temperature (To), peak temperature (Tp), and conclusion temperature (Tc) of starch gelatinization in high protein peas were significantly higher than those of other pea types, whereas the enthalpy change (ΔH) of high protein peas was significantly lower than those of other pea types. The unique properties of high protein peas characterized in this study provided useful information to further improve pea quality.