Oriental Green Peas and the possible benefit of this winter crop.
- Basic Botanical Data of Green Peas.
- Green peas Description: Taxonomy, Morphology and Floral Biology.
- History and Origin of Green peas.
- Chemistry of Green peas:Phytochemical and constituents, Nutrients and Facts.
- Uses and Traditional Medicinal Uses of Green peas.
- Safety of Green Peas.
- How to Select and Store Green Peas.
- Tips for Preparing and Cooking Green Peas:A Few Quick Serving Ideas.
- Research Update:Greean Pea or Pisum sativum L.
Research Update:Greean Pea or Pisum sativum L.:
Effect of brassinolide on tyrosine phosphorylation of pea leaf proteins.:Biochemistry (Mosc). 2006 Apr;71(4):423-9. Fedina EO, Karimova FG, Tarchevsky IA.Kazan Institute of Biochemistry and Biophysics, Kazan Scientific Center, Russian Academy of Sciences, 420111 Kazan, Russia. email@example.com
Brassinosteroid-induced phosphorylation of tyrosine residues in proteins was studied. Proteins of crude extract of pea leaves were analyzed by one- and two-dimensional electrophoresis followed by Western blotting with monoclonal antibodies PY20 to phosphotyrosine proteins. One- and two-dimensional electrophoresis revealed 7 and 13 tyrosine-phosphorylated proteins, respectively. Brassinolide increased the phosphorylation level of most of these proteins. With inhibitors of tyrosine protein phosphatases, such as phenylarsine oxide and orthovanadate, the level of tyrosine phosphorylation of these proteins increased.
Protein-enriched pea flour extract protects stored milled rice against the rice weevil, Sitophilus oryzae.:J Insect Sci. 2004;4:26. Epub 2004 Jul 30. Pretheep-Kumar P, Mohan S, Ramaraju K.Department of Entomology, Tamil Nadu Agricultural University, Coimbatore-641003, Tamil Nadu, India. firstname.lastname@example.org
Studies were conducted to evaluate the effect of a protein-enriched pea (Pisum sativum var. Bonneville) flour extract against the rice weevil, Sitophilus oryzae in its repellency, toxicity, effect on fecundity, stability and sensory properties. Milled rice admixed with pea flour extract at 1% concentration significantly repelled S. oryzae. Mortality of S. oryzae was found to increase and fecundity was markedly suppressed, in rice treated with 1% pea flour extract. The toxicity and reproductive effects of the pea protein-enriched rice were found to be stable for a period of 5 months. The sensory characteristics of stored rice when eaten were not affected by the treatment with pea flour extract. This study indicates that the protein-enriched flour extract obtained from the Bonneville pea may be feasible to protect stored milled rice from insect attack.
Isolation and identification of an allelopathic substance in Pisum sativum.:Phytochemistry. 2003 Apr;62(7):1141-4.
The residue of peas (Pisum sativum L.) has allelopathic activity and the putative compound causing this inhibitory effect was isolated from a methanol extract of pea shoots. Chemical structure of this compound was determined by high-resolution MS, IR and 1H NMR spectral data as pisatin. Pisatin inhibited growth of cress (Lepidium sativum L.) and lettuce (Lactuca sativa L.) seedlings at concentrations greater than 10 and 30 microM, respectively. The doses required for 50% growth inhibition of roots and hypocotyls of cress were 61 and 91 microM, respectively, and those of lettuce were 78 and 115 microM, respectively. The concentration of pisatin in the pea shoots was 32.7 nmol x g(-1) fresh weight. The effectiveness of pisatin on growth inhibition in cress and lettuce, and its occurrence in pea shoots suggest that it may contribute to the growth inhibitory effect of pea residue, and may play an important role in pea allelopathy.
Carbohydrate fractions of legumes: uses in human nutrition and potential for health.:Br J Nutr. 2002 Dec;88 Suppl 3:S293-306. Review.Guillon F, Champ MM.URPOI & UFDNH, National Institute for Agronomic Research (INRA), Rue de la Géraudière, BP 71627, 44316 Nantes Cedex, 03, France. email@example.com
Starch and fibre can be extracted, using wet or dry processes, from a variety of grain legumes and used as ingredients for food. alpha-Galactosides can be isolated during wet processes from the soluble extract. Starch isolates or concentrates are mostly produced from peas, whereas dietary fibre fractions from peas and soyabean are commercially available. The physico-chemical characteristics of fibre fractions very much depend on their origin, outer fibres being very cellulosic whereas inner fibres contain a majority of pectic substances. Inner fibres are often used as texturing agents whereas outer fibres find their main uses in bakery and extruded products, where they can be introduced to increase the fibre content of the food. Most investigations on impacts on health have been performed on soyabean fibres. When positive observations were made on lipaemia, glucose tolerance or faecal excretion, they were unfortunately often obtained after non-realistic daily doses of fibres. Legume starches contain a higher amount of amylose than most cereal or tuber starches. This confers these starches a lower bioavailability than that of most starches, when raw or retrograded. Their low glycaemic index can be considered as beneficial for health and especially for the prevention of diseases related to insulin resistance. When partly retrograded, these starches can provide significant amount of butyrate to the colonic epithelium and may help in colon cancer prevention. alpha-Galactosides are usually considered as responsible for flatus but their apparent prebiotic effects may be an opportunity to valorize these oligosaccharides.
Calcium- and magnesium-dependent aggregation of legume seed storage proteins.:J Agric Food Chem. 1999 Aug;47(8):3009-15. Ferreira RB, Franco E, Teixeira AR.Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Portugal. firstname.lastname@example.org
The solubility characteristics and sedimentation behavior of total or individual globulins from legume seeds [Lupinus albus L., Pisum sativum L., and Glycine max (L.) Merr.] were investigated. The typical insolubility of globulins detected during their extraction seems to be due to the presence of a low molecular weight factor(s) in the seed extract. The solubility of the purified globulins decreases with increasing concentrations of calcium and/or magnesium, but not of other cations, showing minimum values at concentrations that vary with the particular globulin considered. Ultracentrifugation analyses revealed that the Ca(2+)- and/or Mg(2+)-induced insolubilization of the globulins involves the formation of high-order aggregates of molecules of the same or of different globulins. These macromolecular structures are dissociated under conditions of high ionic strength, suggesting the involvement of electrostatic interactions in the aggregation process. The degree of association relies heavily on the amount of Ca(2+) and/or Mg(2+) available, on the presence of chelating agents for these divalent cations, and on the ionic strength of the surrounding medium. The possible physiological significance of the findings is discussed.
The xylose-rich pectins from pea hulls.:Int J Biol Macromol. 1997 Aug;21(1-2):155-62.Renard CM, Weightman RM, Thibault JF.Institut National de la Recherche Agronomique, Centre de Recherches Agro-alimentaires, Laboratoire de Biochimie et Technologie des Glucides, Nantes, France.
The hot acid extract of pea hull, HSP, was rich in galacturonic acid, arabinose and xylose. It was fractionated by copper precipitation followed by ion-exchange chromatography. The copper-soluble fraction represented 26% of HSP and was mostly composed of an arabinan with a low degree of branching, some heteroxylans and a glucan, probably starch. The copper-precipitate (74% of HSP) contained pectins and some residual arabinan, xylan, glucan and mannan. One of the pectic fractions was rich in terminal xylose and fucose; it could be partially degraded by endo-polygalacturonase but not by endo-xylanase and seemed to contain xylogalacturonans.
Evidence for channeling of intermediates in the oxidative pentose phosphate pathway by soybean and pea nodule extracts, yeast extracts, and purified yeast enzymes.:Eur J Biochem. 1997 Jun 1;246(2):283-90.Debnam PM, Shearer G, Blackwood L, Kohl DH.Biology Department, Washington University, St Louis, MO 63130, USA.
Evidence is presented that intermediates of the oxidative pentose phosphate pathway (OPPP) are channeled from one pathway enzyme to the next. CO2 produced from [1-14C]glucose in the presence of unlabelled pathway intermediates contained much more radioactivity than predicted by a model in which pathway-produced intermediates are in equilibrium with identical molecules in the bulk phase. This was the case whether glucose 6-phosphate (Glc6P), 6-phosphogluconolactone, or 6-phosphogluconate was added. Assumptions involved in calculating the amount of 14CO2 predicted for free mixing of 14C-labelled and unlabelled intermediates are discussed, together with the following results. (a) 14CO2 production by pea nodules in the presence of 3 mM 6-phosphogluconate was higher than in its absence. (b) Apparent channeling of intermediates was much higher for purified yeast enzymes than for yeast extract. (c) 6-Phosphogluconate and 6-phosphogluconolactone were channeled between yeast Glc6P dehydrogenase and 6-phosphogluconate dehydrogenase despite the absence of 6-phosphogluconolactonase in the purified yeast enzyme mixture. (d) When purified yeast hexokinase was physically separated from Glc6P dehydrogenase and 6-phosphogluconate dehydrogenase by a dialysis membrane, there was no apparent channeling. (e) Poly(ethylene glycol), high salt and detergents had little effect on apparent channeling of OPPP intermediates, which is consistent with a stable complex of enzymes. On the other hand, density gradient centrifugation experiments suggested a more transient interaction between the enzymes. Taken together, the results support channeling of OPPP pathway intermediates.
Large scale procedure for fractionation of albumins and globulins from pea seeds.:Nahrung. 1996 Oct;40(5):237-44.Crévieu I, Bérot S, Guéguen J.INRA, Laboratoire de biochimie et technologie des protéines, Nantes, France.
The buffer extractable proteins of pea, albumins and globulins, were successively extracted in a large amount at a pilot scale. In order to preserve as much as possible the native structure of proteins, a selective solubilization step procedure was performed. Firstly, albumins were extracted with acetate buffer and secondly globulins with phosphate buffer of high ionic strength. Each extract was desalted by diafiltration without protein precipitation. From 15 kg of flour, 380 g of albumin fraction and 1000 g of globulin fraction were obtained with a protein content of 86.0% and 90.7% of dry matter respectively. The characterisation of albumin and globulin fractions by electrophoresis, ultracentrifugation and anion-exchange chromatography, showed that the cross-contamination of these two fractions was minimal.
The isolation and purification of diamine oxidase of pea seedlings and pig liver.:Appl Biochem Biotechnol. 1996 Mar;56(3):235-41.Güvenilir YA, Deveci N.Department of Chemical Engineering, Istanbul Technical University, Turkey.
Enzymes have been extensively used in many industries for the last 20 years. They are becoming more common because of new areas of application. The limitations of applications of enzymes are activity, specificity, stability, and price. Higher enzyme activities and less susceptibility of process conditions are desirable. Therefore, in some cases, purified enzyme extracts are needed. The purpose of this study is the isolation and purification of diamine oxidase (DAO) of pea seedlings and pig liver. The relationship between pea seedlings growth rate and enzyme activity is established. DAO of pea seedlings and pig liver is prepared by way of tissue disruption with homogenization, centrifugation, fractionation with ammonium sulfate, precipitation of inert components, column electrophoresis, and DEAE-cellulose column chromatography. The specific activity of disrupted pea seedlings cells was measured as 0.017 (U/mg protein), and the pig liver DAO activity was measured as 0.00037 (U/mg protein). The specific enzyme activity from pea seedlings was increased to 6.750 (U/mg protein). On the other hand, the specific enzyme activity from pig liver was increased to 0.30 (U/mg protein). The final enzyme extract from pea is 400-fold purer than raw material, and the final enzyme extract from pig liver is 820-fold purer than raw material.
Localization of free and bound biotin in cells from green pea leaves.:Arch Biochem Biophys. 1993 May 15;303(1):67-73.Baldet P, Alban C, Axiotis S, Douce R.Unité mixte C.N.R.S./Rh?ne-Poulenc (Unité Associée au Centre National de la Recherche Scientifique, U.M.R. 41), Lyon, France.
Cytosol and vacuoles from protoplasts, chloroplasts, and mitochondria from green pea (Pisum sativum) leaves were purified and examined for their biotin content. The bulk of free biotin was shown to be exclusively associated with the cytosolic fraction at a concentration of about 4 pmol/mg protein and no bound biotin was detected. The bulk of bound biotin (biotin-containing carboxylases) was associated with the soluble fraction of chloroplasts and mitochondria at a concentration of about 1.2 and 13 microM, respectively. No free biotin was detected in these organelles. Western blot analysis of total, chloroplastic, and mitochondrial polypeptides, using horseradish peroxidase-labeled streptavidin, revealed three biotin-containing polypeptides with molecular mass of 220,000, 76,000 and 34,000. All were detected in the total pea leaf extract, but the M(r) 76,000 and the M(r) 34,000 biotinylated polypeptides were only detected in mitochondria and chloroplasts, respectively. 3-Methylcrotonyl-coenzyme A carboxylase and acetyl-coenzyme A carboxylase activities were measured in these two compartments, respectively. Previously, it has been shown that the M(r) 76,000 polypeptide was the biotinylated subunit of the mitochondrial 3-methylcrotonyl-coenzyme A carboxylase. In this paper, the origin and putative function of free biotin located in cytosol are discussed.
Purification of Multiple Forms of Glutathione Reductase from Pea (Pisum sativum L.) Seedlings and Enzyme Levels in Ozone-Fumigated Pea Leaves.:Plant Physiol. 1992 Sep;100(1):138-145.Madamanchi NR, Anderson JV, Alscher RG, Cramer CL, Hess JL.Department of Plant Pathology, Physiology and Weed Science, Virginia Polytechnic Institute and State University, Blacksburg, Virginia 24061.
Glutathione reductase was purified from pea seedlings using a procedure that included 2',5'-ADP Sepharose, fast protein liquid chromatography (FPLC)-anion exchange, and FPLC-hydrophobic interaction chromatography. The purified glutathione reductase was resolved into six isoforms by chromatofocusing. The isoform eluting with an isoelectric point of 4.9 accounted for 18% of the total activity. The five isoforms with isoelectric points between 4.1 and 4.8 accounted for 82% of the activity. Purified glutathione reductase from isolated, intact chloroplasts also resolved into six isoforms after chromatofocusing. The isoform eluting at pH 4.9 constituted a minor fraction of the total activity. By comparing the chromatofocusing profile of the seedling extract with that of the chloroplast extract, we inferred that the least acidic isoform was extraplastidic and that the five isoforms eluting from pH 4.1 to 4.8 were plastidic. Both the plastidic (five isoforms were pooled) and extraplastidic glutathione reductases had a native molecular mass of 114 kD. The plastidic glutathione reductase is a homodimer with a subunit molecular mass of 55 kD. Both glutathione reductases had optimum activity at pH 7.8. The K(m) for the oxidized form of glutathione (GSSG) was 56.0 and 33.8 mum for plastidic and extraplastidic glutathione reductase, respectively, at 25 degrees C. The K(m) for NADPH was 4.8 and 4.0 mum for plastidic and extraplastidic isoforms, respectively. Antiserum raised against the plastidic glutathione reductase recognized a 55-kD polypeptide from purified antigen on western blots. In addition to the 55-kD polypeptide, another 36-kD polypeptide appeared on western blots of leaf crude extracts and the purified extraplastidic isoform. The lower molecular mass polypeptide might represent GSSG-independent enzyme activity observed on activity-staining gels of crude extracts or a protein that has an epitope similar to that in glutathione reductase. Fumigation with 75 nL L(-1) ozone for 4 h on 2 consecutive days had no significant effect on glutathione reductase activity in peas (Pisum sativum L.). However, immunoblotting showed a greater level of glutathione reductase protein in extracts from ozone-fumigated plants compared with that in control plants at the time when the target concentration was first reached, approximately 40 min from the start of the fumigation, and 4 h on the first day of fumigation.
Further characterization of a low-molecular weight allergen fragment isolated from the green pea.:Clin Exp Immunol. 1976 Jul;25(1):159-64.Malley A, Baecher L, Mackler B, Perlman .
A low molecular weight allergen fragment present in the pea dialysate fraction was purified by ion-exchange chromatography and gel filtration. The highly purified allergen fragment inhibits both antigen-indiced passive cutaneous anaphlaxix reactions in guinea-pigs sensitized with rabbit anti-pea extract sera and Prausnitz-Küstner reactions in non-allergic volunteers sensitized with the sera of patients sensitive to green peas. Preliminary analysis of the purified allergen fragment indicates that it is a glycoprotein with a molecular weight of 1800 +/- 250.
The isolation of allergens from the green pea.:J Allergy Clin Immunol. 1975 Oct;56(4):282-90.Malley A, Baecher L, Mackler B, Perlman F.
The aqueous extract of green peas was separated into 3 fractions (albumin, legumin, and vicilin) by dialysis against distilled water and isoelectric precipitation. The major antigenic and all of the allergenic activity of the pea extract was associated with the albumin fraction. The albumin fraction retains its allergenicity upon heating at 60 degrees C for 30 min or boiling at 100 degrees C for 5 min, but becomes partially inactivated by autoclaving at 120 degrees C for 15 min. The allergenic determinant expressed by the albumin fraction appears to be common to several other members of the legume family. In addition, the pea dialysate fraction was shown to specifically inhibit precipitin and passive cutaneous anaphylaxis (PCA) reactions involving rabbit antipea serum and the pea albumin fraction, and histamine release from passively sensitized monkey lung tissue using the serum of pea-sensitive patients.
Phytosterol, Squalene, Tocopherol Content and Fatty Acid Profile of Selected Seeds, Grains, and Legumes.:Plant Foods Hum Nutr. 2007 Jun 27;Ryan E, Galvin K, O'connor TP, Maguire AR, O'brien NM.Department of Food and Nutritional Sciences, University College, Cork, Ireland, email@example.com.
The unsaponifiable lipid fraction of plant-based foods is a potential source of bioactive components such as phytosterols, squalene, and tocopherols. The objective of the present study was to determine the levels of phytosterols, and squalene, as well as tocopherols (alpha and beta + gamma) in selected grains, seeds, and legumes. The method comprised acid hydrolysis and lipid extraction followed by alkaline saponification, prior to analysis by HPLC. In addition, the fatty acid profile of the foods was determined via total lipid extraction, fatty acid derivitisation and GC analysis. In general, beta-sitosterol was the most prevalent phytosterol, ranging in concentration from 24.9 mg/100 g in pumpkin seed to 191.4 mg/100 g in peas. Squalene identified in all foods examined in this study, was particularly abundant in pumpkin seed (89.0 mg/100 g). The sum of alpha- and beta+ gamma-tocopherols ranged from 0.1 mg/100 g in rye to 15.9 mg/100 g in pumpkin seeds. Total oil content ranged from 0.9% (w/w) in butter beans to 42.3% (w/w) in pumpkin seed and the type of fat, in all foods examined, was predominantly unsaturated. In conclusion, seeds, grains, and legumes are a rich natural source of phytosterols. Additionally, they contain noticeable amounts of squalene and tocopherols, and in general, their fatty acid profile is favorable.
Peas (Pisum sativum L.).:Methods Mol Biol. 2006;343:337-45. Review.Grant J, Cooper P.New Zealand for Crop & Food Research, Ltd., Christchurch, New Zealand.
In this chapter we describe a robust method for transformation of peas that has been successfully used in our laboratory since 1992. Using immature pea seed collected from field- or greenhouse-grown plants, we have produced transgenic lines for over 30 genotypes including named pea cultivars and advanced breeding lines. This method uses immature cotyledons as the explant, and the transformation efficiency is in the range 0.2 to 13.5% of cotyledons producing at least one independently transformed line. Agrobacterium tumefaciens strains AGL1 and KYRT1 are the most successful in our procedure, and kanamycin, phosphinothricin, and hygromycin are reliable selectable markers. Potentially useful genes have been introduced for pest and disease resistance, altering quality traits, and investigating metabolic pathways and are being studied in transgenic pea lines.
Effect of vitamin C and folic acid on seed vigour response and phenolic-linked antioxidant activity.:Bioresour Technol. 2007 May;98(7):1393-404. Epub 2006 Jul 28.Burguieres E, McCue P, Kwon YI, Shetty K.Program in Plant Biology, University of Massachusetts, Amherst, MA 01003, USA.
Folic acid and vitamin C were used in the concentration range of 0-500muM as exogenous growth enhancers to stimulate pea (Pisum sativum) seedling vigour. The results suggest that a concentration of 50muM folic acid and 500muM vitamin C were optimum in maximally enhancing seed vigour and potentially seedling performance according to both agronomic and biochemical seed vigour parameters. Results indicated that germination percentage, shoot weight, shoot height, and root length were enhanced in folic acid and vitamin C treated plants compared to control plants. The levels of enhanced phenolic content in response to folic acid and vitamin C treatments were highest on days 8 and 10. Evaluation of critical biochemical parameters indicated that the average glucose-6-phosphate dehydrogenase (G6PDH) activity and proline content in response to treatments were higher than control and correlated to enhanced phenolic content and DPPH-based antioxidant activity. Key enzymes, guaiacol peroxidase (GPX), superoxide dismutase (SOD), and catalase (CAT) were also higher in response to treatments and correlated to enhanced phenolic content and DPPH-based antioxidant activity. Taken together, these studies support the hypothesis that the proline-linked pentose phosphate pathway stimulates phenolic synthesis and related free-radical scavenging antioxidant activity. Further, this proline-linked pentose phosphate pathway stimulation in response to folic acid and vitamin C was also correlated to antioxidant enzyme response indicated by the stimulation of GPX, SOD, and CAT activities. Therefore, this study indicates the enhancement of seed vigour response by folic acid and vitamin C as reflected in both agronomic and biochemical responses, and this occurred through the stimulation of phenolic-linked antioxidant response that is likely positively modulated through the proline-linked pentose phosphate pathway.
An antifungal protein from the pea Pisum sativum var. arvense Poir.:Peptides. 2006 Jul;27(7):1732-7. Epub 2006 Mar 30.Wang HX, Ng TB.State Key Laboratory for Agrobiotechnology and Department of Microbiology, China Agricultural University, Beijing, China.
An antifungal protein with a molecular mass of 11 kDa and a lysine-rich N-terminal sequence was isolated from the seeds of the pea Pisum sativum var. arvense Poir. The antifungal protein was unadsorbed on DEAE-cellulose but adsorbed on Affi-gel blue gel and CM-cellulose. It exerted antifungal activity against Physalospora piricola with an IC50 of 0.62 microM, and also antifungal activity against Fusarium oxysporum and Mycosphaerella arachidicola. It inhibited human immunodeficiency virus type 1 reverse transcriptase with an IC50 of 4.7 microM.
Polycyclic aromatic hydrocarbons in the beans, peas and broad beans from domestic market, 1999-2002:Rocz Panstw Zakl Hig. 2005;56(1):83-90. Polish.Ba?dyga B, Zbigniew B, Wieczorek J, Dymkowska-Malesa M, Smoczyńtski SS.Instytut Towaroznawstwa i Kszta?towania Jako?ci, Uniwersytet Warmińsko-Mazurski, 10-910 Olsztyn.
Seeds of bean, peas and broad bean, purchased from local seed production plants in the provinces of Mazowieckie and Kujawsko-Pomorskie in the years 1999-2002, were determined for the contents of fifteen polycyclic aromatic hydrocarbons. The hydrocarbons were extracted from the seeds with a hexane-acetone mixture by means of sonification. The obtained extracts were then purified in a silica gel column. Polycyclic aromatic hydrocarbons (PAH) were identified and determined quantitatively with liquid chromatography using a fluorescent detector. The presence (in different concentrations) of PAH was reported in the majority of seeds of the bean, peas and broad bean varieties examined, which indicates that they may be ingested with food and bioaccumulated in the human organism. A considerably higher content of SPAH was observed in the seeds of broad bean, compared to those of bean and peas. The highest SPAH determined reached 2 x 10(2) microg/kg of product. The obtained results were comparable with those reported by other authors for vegetables originating from non-industrial areas. It is worth emphasising that all the seeds examined revealed the presence of PAH with carcinogenic properties.
Nutritional assessment of raw and germinated pea (Pisum sativum L.) protein and carbohydrate by in vitro and in vivo techniques.:Nutrition. 2005 Feb;21(2):230-9.Urbano G, López-Jurado M, Frejnagel S, Gómez-Villalva E, Porres JM, Frías J, Vidal-Valverde C, Aranda P.Departamento de Fisiología, Instituto de Nutrición, Universidad de Granada, Granada, Spain. firstname.lastname@example.org
OBJECTIVE: We assessed the effect of germinating Pisum sativum L. variant Arvense cv. Esla for 3 and 6 d in darkness on the chemical composition and nutritive utilization of protein and carbohydrates. METHODS: Nutritional assessment of protein and carbohydrates was based on chemical analysis of raw and germinated pea flours and in vitro and in vivo rat balance methodologies. RESULTS: Germination caused a notable decrease in alpha-galactoside content and significant increases in sucrose, glucose, and fructose. The ratio of available starch to total starch increased as a consequence of processing. The content of vitamin B2 increased significantly, whereas no significant change was observed in vitamin B1 content in germinated peas. Protein digestibility assessed with an in vivo technique (apparent digestibility coefficient) or as the percentage of dialyzable nitrogen increased significantly as a result of germination in contrast to what was observed with the in vitro pH-drop methodology. Daily food intake, nitrogen absorption and balance, percentage of retained versus absorbed nitrogen, protein efficiency ratio, and the index of available carbohydrates were significantly improved by germination for 3 d and significantly decreased by germination for 6 d. CONCLUSIONS: Germination of pea seeds for 3 d significantly improves palatability of these seeds and the nutritive utilization of protein and carbohydrates.
Physicochemical traits of Dekoko (Pisum sativum var. abyssinicum) seeds.:Plant Foods Hum Nutr. 2003;58(4):275-83.Yemane A, Skjelv?g AO.Agricultural University of Norway, Department of Horticulture and Crop Sciences, PO Box 5022, N-1432 As, Norway. email@example.com
Dekoko (Pisum sativum var. abyssinicum) has high appreciation for its taste and obtains a premium price in local markets compared to Ater (Pisum sativum var. sativum). However, data on the physicochemical traits of Dekoko seeds were lacking. This paper reports on the physicochemical features of Dekoko and compares the results with that of Ater. Seed weight and seed volume were 36 and 30%, respectively, higher in Ater, while water absorption, percent seed swelling, and percent husk were higher in Dekoko. Cooking time was shorter for Dekoko than Ater seeds. Decortication reduced cooking time on average by 39 and 45 min in Dekoko and Ater, respectively. Cotyledon flour of Dekoko contained 251 g crude protein, 19 g fat, 31.7 g total sugars, 370 g starch, and 130 g neutral detergent fiber per kilogram DM. These traits were significantly higher in Dekoko than in Ater, except for starch, which was higher in the latter. Arginine, asparagine, and glutamine occurred in larger proportions, and collectively contributed about 39% to the total amino acids in both varieties. Lysine contributed about 7%, while sulfur containing amino acids constituted about 3.0 and 2.3% of the total amino acids in Dekoko and Ater, respectively. Ca and Mg were higher in Ater, while P was higher in Dekoko. Based on the observations it was concluded that Dekoko is a suitable supplementary protein source for a cereal-based diet.
Seed lectin from pisum arvense: isolation, biochemical characterization and amino acid sequence.:Protein Pept Lett. 2003 Dec;10(6):607-17.Cavada BS, da Silva LI, Ramos MV, Galvani FR, Grangeiro TB, Leite KB, Assreuy AM, Cajazeiras JB, Calvete JJ.Departamento de Bioquímica e Biologia Molecular, Campus do Pici, Caixa Postal 6033, Fortaleza-Ceará. CEP 60451-970, Brazil. firstname.lastname@example.org
A glucose/mannose lectin was purified by affinity chromatography from Pisum arvense seeds (PAL) and the 50 kDa molecular mass in solution determined by size exclusion chromatography. SDS-PAGE and electrospray ionization mass spectrometry showed two distinct polypeptide chains: alpha (Mr. 5591 Da) and beta (19986 Da). The lectin was extensively characterized in terms of its biochemical and biological aspects. The amino acid sequence was established by Edman degradation of overlapping peptides. PAL in solution behaves as a dimer and has its monomeric structure formed by two distinct polypeptide chains named alpha (Mr. 5591 Da) and beta (19986 Da) by Electrospray ionization (ESI) mass spectrometry. PAL possesses identical amino acid sequences to that of pea seed lectin but undoubtedly does not exhibit sequence heterogeneity. It is discussed that P. arvense should be considered as a synonym of P. sativum. Furthermore, like pea lectin, PAL discriminates biantennary fucosylated glycan, determined by surface plasmon resonance.
Identification and differential expression of two thioredoxin h isoforms in germinating seeds from pea.:Plant Physiol. 2003 Jul;132(3):1707-15.Montrichard F, Renard M, Alkhalfioui F, Duval FD, Macherel D.Unité Mixte de Recherche 1191 Physiologie Moléculaire des Semences, Institut National de Recherche Agronomique - Institut National d'Horticulture - Université d'Angers, France. email@example.com
The NADPH/NADP-thioredoxin (Trx) reductase (NTR)/Trx system (NTS) is a redox system that plays a posttranslational regulatory role by reducing protein targets involved in crucial cellular processes in microorganisms and animals. In plants, the system includes several h type Trx isoforms and has been shown to intervene in reserve mobilization during early seedling growth of cereals. To determine whether NTS was operational during germination of legume seeds and which Trx h isoforms could be implicated, Trx h isoforms expression was monitored in germinating pea (Pisum sativum cv Baccara) seeds, together with the amount of NTR and NADPH. Two new isoforms were identified: Trx h3, similar to the two isoforms already described in pea but not expressed in seeds; and the more divergent isoform, Trx h4. Active recombinant proteins were produced in Escherichia coli and used to raise specific antibodies. The expression of new isoforms was analyzed at both mRNA and protein levels. The lack of correlation between mRNA and protein abundances suggests the occurrence of posttranscriptional regulation. Trx h3 protein amount remained constant in both axes and cotyledons of dry and imbibed seeds but then decreased 2 d after radicle protrusion. In contrast, Trx h4 was only expressed in axes of dry and imbibed seeds but not in germinated seeds or in seedlings, therefore appearing as closely linked to germination. The presence of NTR and NADPH in seeds suggests that NTS could be functional during germination. The possible role of Trx h3 and h4 in this context is discussed.
Nutritional value of broad bean seeds. Part 2: Selected biologically active components.:Nahrung. 2003 Apr;47(2):98-101.Borowska J, Giczewska A, Zadernowski R.Chair of Food Plant Chemistry and Processing, University of Warmia and Mazury, Olsztyn, Pl. Cieszyński 1, PL-10-957 Olsztyn, Poland. firstname.lastname@example.org
Selected biologically active non-nutrient components (BANS) were determined in broad bean seeds of fine-size and large-size seed varieties and in pea seeds for comparison. Among the analysed biologically active substances the broad bean seeds of fine-size and large-size seed varieties were differentiated mainly by phenolic compounds (including flavanols and proantocyanidines) which appear in twice as large quantities in large-size seed varieties. It was shown that in comparison to pea, broad bean seeds are characterised by a higher content of phenolic compounds, phytates as well as a higher activity of inhibitors of trypsin and amylases. Moreover, it was found that phenolic compounds accumulate mainly in the dark-colored seed coats of large-size broad bean and this fact is related to higher activity inhibiting-amylases of methanol extracts from this fraction of seeds.
Effect of germination on the carbohydrate composition of the dietary fiber of peas (Pisum sativum L.).:J Agric Food Chem. 2003 Feb 26;51(5):1254-9.Martín-Cabrejas MA, Ariza N, Esteban R, Mollá E, Waldron K, López-Andréu FJ.Departamento de Química Agrícola, Facultad de Ciencias, Universidad Autónoma de Madrid (UAM), Spain. email@example.com
The effect of different conditions of pea germination on dietary fiber (DF) composition was studied. Insoluble dietary fiber (IDF) and soluble dietary fiber (SDF) were subjected to acid hydrolysis, and the resultant neutral sugars, uronic acids, and Klason lignin were quantified. Germinated peas exhibited significantly higher contents of total dietary fiber (TDF) than the raw sample, due to the increases of both DF fractions. Under darkness conditions, germination exhibited the highest contents of IDF and SDF. Decreasing IDF/SDF ratios showed that the carbohydrate changes did not take place to the same extent during germination, the SDF fraction being the most affected. The detailed chemical composition of fiber fractions reveals increases of cellulose in the IDF of germinated samples, whereas SDF exhibits a decrease of pectic polysaccharides and also increases of polysaccharides rich in glucose and mannose. The DF results were corroborated by a comparative examination of the cell wall carbohydrate composition.
Isolation and study of the functional properties of pea proteins.:Nahrung. 2001 Oct;45(6):399-401.T?m?sk?zi S, Lásztity R, Haraszi R, Baticz O.Budapest University of Technology and Economics, Department of Biochemistry and Food Technology, Pf. 91, H-1521 Budapest, Hungary.
Proteins of pea seeds were isolated after defatting with hexane using alkaline (0.1 M sodium hydroxide) extraction and acid (HCl) precipitation. Concentrates were also prepared by hexane extraction and ethanolic extraction (pH = 5). Gross chemical composition amino acid content and functional properties (solubility profile, emulsifying--and foaming properties, water--and oil absorption) were studied. The results were compared with the same parameters of soy and lupin protein products. Although the majority of functional characteristics of isolates were lower in comparison to soy isolates, pea protein concentrate and isolate could be successfully used in bakery products for enrichment in protein and improvement of biological value. Their utilization as meat protein substitute in some Frankfurter type sausages is also possibly.
- 1.Oriental Green Peas and the possible benefit of this winter crop.
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