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PubMed2004

A quantitative in silico analysis calculates the angiotensin I converting enzyme (ACE) inhibitory activity in pea and whey protein digests.

Angiotensin I converting enzyme (ACE) inhibitory peptides can induce antihypertensive effects after oral administration. By means of an ACE inhibitory peptide database, containing about 500 reported sequences and their IC(50) values, the different proteins in pea and whey were quantitatively evaluated as precursors for ACE inhibitory peptides. This analysis was combined with experimental data from the evolution in ACE inhibitory activity and protein degradation during in vitro gastrointestinal digestion. Pea proteins produced similar in silico scores and were degraded early in the in vitro digestion. High ACE inhibitory activity was observed after the simulated stomach phase and augmented slightly in the simulated small intestine phase. The major whey protein beta-lactoglobulin obtained the highest in silico scores, which corresponded with the fact that degradation of this protein in vitro only occurred from the simulated small intestine phase on and resulted in a 10-fold increase in the ACE inhibitory activity. Whey protein obtained total in silico scores of about 124 ml/mg, compared to 46 ml/mg for pea protein, indicating that whey protein would be a richer source of ACE inhibitory peptides than pea protein. Although beta-lactoglobulin is only partially digested, a higher ACE inhibitory activity was indeed found in the whey (IC(50) = 0.048 mg/ml) compared to the pea digest (IC(50) = 0.076 mg/ml). In silico gastrointestinal digestion of the highest scoring proteins in pea and whey, vicilin and albumin PA2, and beta-lactoglobulin, respectively, directly released a number of potent ACE inhibitory peptides. Several other ACE inhibitory sequences resisted in silico digestion by gastrointestinal proteases. Briefly, the quantitative in silico analysis will facilitate the study of precursor proteins on a large scale and the specific release of bioactive peptides.

Amino Acid Sequence↗

PubMedDate not supplied

ABO blood groups, grass pea preparation, and neurolathyrism in Ethiopia.

An exploratory study was conducted in the rural Estie district of Ethiopia in 1997 to identify the role of ABO blood group, rhesus factor, and type of grass pea (Lathyrus sativus) diet in the susceptibility to neurolathyrism. Five-hundred study subjects (250 cases and 250 controls) were examined and interviewed, and had their ABO and rhesus blood groups determined. The majority (86%) of the cases were males. Blood group O was the most common in the patients and controls followed by groups A, B, and AB. The vast majority of the study subjects were rhesus-positive. The gravy (Shiro) grass pea preparation was consumed by 91.6% of the study population, boiled (Nifiro) by 86%, and roasted (Kollo) by 56.4%. Almost half (48%) of the cases had consumed grass pea for > 4 months compared to 8% of controls (P < 0.001). There was a significant association between the risk for neurolathyrism and the consumption of boiled (adjusted odds ratio [AOR] = 98.4) and roasted (AOR = 55.62) forms of grass pea. There was no risk of paralysis associated with consumption of the gravy form of grass pea (AOR = 0.40, 95% confidence interval 0.1-2.0). Blood group O remained significantly associated with the disease after adjusting for age, type of grass pea preparation consumed, and duration of consumption (AOR = 2.90).

ABO Blood-Group System↗

PubMedDate not supplied

Occupational asthma caused by grass pea used in the industrial processing of parquet.

BACKGROUND: although grass pea belongs to the leguminoseae family, allergic reactions to its flour have rarely been described. Clinical and immunological studies were performed to confirm a type I hypersensitivity mechanism in a case of occupational asthma to grass pea flour exposure, used in the industrial processing of parquet. METHODS: occupational asthma was diagnosed according to patient history, PEFR monitoring and a specific bronchial challenge test. Skin prick test with an aqueous grass pea flour extract, specific IgE determinations (CAP assay) and IgE immunoblot tests were performed. RESULTS: skin prick test with the extract showed a positive immediate response, and negative response in controls. Specific IgE to grass pea was positive (9.57 KU/l). Immunoblotting demonstrated the presence of specific serum IgE that recognized 3 proteins in the extract (MW 46, 32 and 28 kDa). PEFR monitoring showed positive results. Bronchial challenge test with the extract elicited an isolated immediate response. CONCLUSIONS: as far as we know this is the first time that IgE mediated occupational asthma caused by grass pea is reported and it is also the first time that its allergens are characterized. Grass pea flour might constitute a relevant occupational allergen in this unreported source of exposure in parquet manufacturers.

Adhesives↗

PubMed2000

Nutritional assessment in vitro and in vivo of raw and extruded peas (Pisum sativum L.).

The effects of extrusion cooking on the nutritional properties of Pisum sativum L. have been evaluated in vitro and in vivo. The treatment greatly elevated protein and starch digestibility in vitro. Also, the amounts of intact starch diminished while total free sugars increased. In addition, the levels of antinutritional factors, such as protease inhibitors and lectins, were greatly decreased. Concentrations of methionine and cystine were low in raw peas and were further reduced by extrusion treatment. The nutritional performance of rats fed extruded pea diets for 15 days was no better than that of rats given raw pea diet. This was due to the overriding effects of amino acid deficiencies in the diets. Weight gains by rats fed extruded pea diets supplemented with amino acids were, however, much higher than those achieved by rats fed supplemented raw pea diets. Food transformation index and protein efficiency ratio values were also greatly improved. Extrusion treatment did therefore significantly improve the nutritional quality of peas.

Animal Nutritional Physiological Phenomena↗

PubMed2003

Functional properties of purified vicilins from cowpea (Vigna unguiculata) and pea (Pisum sativum) and cowpea protein isolate.

The major storage globulins (vicilins) of cowpea (Vigna unguiculata) and pea (Pisum sativum) seeds were purified by ammonium sulfate precipitation, and a semipurified cowpea protein isolate (CPI) was prepared by isoelectric precipitation. Some of the functional properties of these proteins, including solubility, foaming, and emulsifying capacities, were investigated and compared. The solubility of purified cowpea vicilin was reduced at pH 5.0, increasing markedly below and above this value. Pea vicilin exhibited poor solubility between pH 5.0 and pH 6.0, and CPI was little soluble in the pH range from 4.0 to 6.0. At neutral pH, the emulsifying activity indexes (EAI) of purified pea vicilin and CPI were 194 and 291 m(2)/g, respectively, which compare quite favorably to EAIs of 110 and 133 m(2)/g for casein and albumin, respectively. Remarkably, purified cowpea vicilin exhibited an EAI of 490 m(2)/g, indicating a very high emulsifying activity. Purified cowpea and pea vicilins exhibited lower foaming capacities and foam stablity indexes (FSI) than CPI. FSI values of 80 and 260 min were obtained for purified pea and cowpea vicilin, respectively, whereas a FSI value of 380 min was obtained for CPI. These results are discussed in terms of the possible utilization of purified vicilins or protein isolates from pea and cowpea in the food processing industry.

Amino Acids↗

PubMed2006

Genetic variation in pea seed globulin composition.

A quantitative characterization of seeds from 59 pea (Pisum sativum L.) lines and relative taxa with various external characteristics and wide geographical origin was performed to explore the genetic variation of pea concerning its starch and protein contents and globulin composition. Pea lines, which produce round, wrinkled, flat, and round-dimpled seeds, have starch as the major reserve, with an average content of 46%. Protein content varied from 13.7 to 30.7% of the seed dry matter, with an overall average of 22.3%. Densitometric quantification of the individual globulins (legumin, vicilin, convicilin, and globulin-related proteins) based on SDS-PAGE gels showed no lines lacking any particular globulin. Among the lines tested, variation was shown in both their total globulins content and their globulin composition. The total globulin content ranged from 49.2 to 81.8% of the total pea protein extract (TPPE). Legumin content varied between 5.9 and 24.5% of the TPPE. Vicilin was the most abundant protein of pea, and its content varied between 26.3 and 52.0% of the TPPE. Both processed and nonprocessed vicilins occurred. The processed vicilin was the predominant one, with values between 17.8 and 40.8%, whereas the nonprocessed ones constituted between 3.1 and 13.5% of the TPPE. Convicilin was the least abundant globulin, and its content ranged from 3.9 to 8.3%. Finally, the globulin-related proteins were present in amounts ranging from 2.8 to 17.3%. They were less abundant in comparison with legumin and vicilin, but they showed the largest relative variation of the four globulin classes. Correlations between the different external characteristics and globulin composition were determined. Comparison with soybean showed that pea lines show more variety in the abundance of globulin proteins, enabling a wider range of food application.

Electrophoresis, Polyacrylamide Gel↗

PubMed1999

Influence of genotype and processing on the in vitro rate of starch hydrolysis and resistant starch formation in peas (Pisum sativum L.).

The formation of resistant starch (RS) and the rate of starch hydrolysis were evaluated in vitro in a wild type of green-seeded pea genotype RRRbRb BC3 (33-Am) with 32.7% amylose content and in two mutants RRrbrb BC3 (23-Am) and rrRbRb BC3 (65-Am) with amylose contents of 23.3 and 65.1%, respectively. Pea samples were intact or homogenized and subjected either to autoclaving or to boiling at atmospheric pressure. The amount of RS (total starch basis) varied from 6.2 to 12.9% in the 23-Am products and from 31.2 to 33.4% in the 65-Am products. The RS level of the 33-Am product with a regular amylose content was 11.0%. Both the 23-Am and the 65-Am products were abundant sources of dietary fiber (39 and 34%, dry matter basis, respectively) versus 23% in the regular pea product. The amylose/amylopectin ratio was an important determinant of the rate of starch hydrolysis. The hydrolysis indices (HI) and predicted glycemic indices were lowest in the 65-Am peas (HI range = 42-59) as compared to the 23-Am peas (HI range = 53-84). It is concluded that the pea genotypes covered a wide range in starch availability, which is likely to affect nutritional parameters such as glycemic responses and colonic delivery of starch.

Amylose↗

PubMed1998

Cloning, expression and characterization of a gene which encodes a topoisomerase I with positive supercoiling activity in pea.

We have isolated and sequenced the full length cDNA for topoisomerase I. Using degenerate primers, based on the conserved amino acid sequences of five eukaryotic topoisomerase I, a 386 bp fragment was PCR amplified using pea cDNA as template. This fragment was used as a probe to screen a pea cDNA library. Two partial cDNA clones were isolated which were truncated at the 5' end. RACE-PCR was employed to isolate the remaining portion of the gene. The total size of the gene was 3055 bp with an open reading frame of 2676 bp. The deduced structure of pea topoisomerase I contain 892 amino acids with a calculated molecular weight of 100 kDa and an estimated pI of 9.3. A comparison of the deduced amino acid sequences of the pea topo I with the other eukaryotic topoisomerases clearly suggested that they are all related. Pea topoisomerase I has been overexpressed in E. coli system and the recombinant topoisomerase purified to homogeneity. The purified protein relaxes both positive and negative supercoiled DNA in the absence of divalent cation Mg2+. In the presence of Mg2+ ions the purified enzyme introduces positive supercoils a unique property not reported in any other organism except in archaebacterial topoisomerase I. Polyclonal antibodies were raised against recombinant topoisomerase I and western blotting with sub-cellular fractions indicated the localization of this topoisomerase in pea nuclei.

Amino Acid Sequence↗

PubMed1995

Cellular expression, developmental regulation, and phylogenic conservation of PEA-15, the astrocytic major phosphoprotein and protein kinase C substrate.

PEA-15 has recently been identified as a major phosphoprotein in astrocytes and an endogenous substrate for protein kinase C. This 15-kDa protein exists under three molecular forms, an unphosphorylated form, N, and two phosphorylated forms, Pa and Pb. Antisera were raised against synthetic peptides corresponding to the internal sequences of the mouse protein containing the two specific phosphorylation sites and affinity-purified antibodies were used for immunoblotting. PEA-15 was found mainly in the cytosol, but its protein kinase C-phosphorylated form, Pb, was also detectable in association with the membrane and remained with the fraction that contains stabilized microtubules. Abundant in astrocytes, particularly in the hippocampus, PEA-15 was also detected in all cultured brain cell types examined, indicating a more ubiquitous distribution of the protein, further demonstrated by its detection in the eye and in the lung. Parallel to the increase in expression levels, phosphorylation of PEA-15 also increased during development. This paralleled results obtained in primary cultures, whereas PEA-15 levels increase with cell maturation. Finally, physiological importance of PEA-15 phosphorylation was illustrated by immunoreactivity observed in brain homogenates of different mammals, birds, amphibians, and fish.

Animals↗

PubMed1994

The effect of heat on amino acids for growing pigs. 3. The availability of lysine from heat-treated field peas (Pisum sativum cultivar Dundale) determined using the slope-ratio assay.

The effect of heat on the availability of lysine in field peas (Pisum sativum cultivar Dundale) was determined using the slope-ratio assay with growing pigs. The field peas were heated to 110 degrees, 135 degrees, 150 degrees, or 165 degrees for 15 min using a forced-air dehydrator. Lysine availability was significantly depressed (P < 0.05) with the application of heat, even at mild temperatures of 110 degrees. Lysine availability values of 0.96, 0.71, 0.77, 0.56, and 0.47 were determined for the raw peas and peas heated to 110 degrees, 135 degrees, 150 degrees or 165 degrees respectively. The effect of dietary protein level on the ileal digestibility of lysine in raw field peas was determined in a second experiment to estimate true ileal digestibility. Five diets were formulated to contain 85, 105, 125, 145 and 165 g protein/kg. Increasing dietary protein from 85 to 105 g/kg resulted in a significant increase in the estimate of apparent ileal digestibility from 0.84 to 0.93. Comparisons were then able to be drawn between the ileal digestibility, availability and utilization of lysine from raw and heat-treated field peas. The results indicate that unlike ileal digestibility values, estimates of lysine availability are sensitive to heat treatment and are a close reflection of lysine utilization in heated protein concentrates. Thus, lysine availability values would be more suitable for use in diet formulations than ileal digestibility estimates when dealing with heat-processed protein concentrates.

Amino Acids↗

PubMed2003

Supplementation of diets containing pea meal with exogenous enzymes: effects on weight gain, feed conversion, nutrient digestibility and gross morphology of the gastrointestinal tract of growing broiler chicks.

1. The potential for the nutritional improvement of pea-based diets by supplementation with a cocktail of exogenous carbohydrases was investigated using growing broiler chicks. 2. Pea meals (grown in the UK) were included in wheat-based diets at 300 g/kg as a partial replacement for an approximately isonitrogenous mixture of wheat and soybean meal. A wheat/soybean meal diet served as a control and each diet was supplemented with a cocktail of alpha-amylase, pectinase and cellulase. The diets were fed to 1-d-old broiler chicks for a period of 21 d. Weight gain and feed conversion were monitored weekly and excreta were collected during the final week in order to determine nutrient digestibility coefficients and metabolisable energy. On d 21, the gastrointestinal (GI) tract was excised and gross morphology measured. 3. Inclusion of pea meal reduced weight gain, feed conversion, nutrient digestibility and also increased the relative sizes of the distal sections of the GI tract. 4. Enzyme addition partially ameliorated the detrimental effects of pea meal inclusion although similar improvements were also noted for birds fed on the control diet. 5. It is concluded that the nutritive value of pea-meal-based diets can be improved by the addition of carbohydrases, and that some pea cultivars show considerable potential as vegetable protein sources for broiler chicks.

Animal Feed↗

PubMed2004

Food intake, growth rate, food conversion and food choice in broilers fed on diets high in rapeseed meal and pea meal, with observations on sensory evaluation of the resulting poultry meat.

1. Experiments were done to measure the effects of 100 and 200 g/kg of either pea meal or low glucosinolate, low erucic acid rapeseed meal on food intake and growth, food choice and meat organoleptic quality in broiler chickens. 2. The test diets were formulated to be iso-energetic and iso-nitrogenous with a soy-wheat control diet. In all diets, lysine was fixed at 11.0 g/kg and all other indispensable amino acids were present in excess of requirements. 3. Food intake was little affected by the inclusion of 100 g/kg of pea meal in the diet but 200 g/kg of peas caused a decrease. Rapeseed produced a decrease in food intake at both dietary concentrations. 4. Weight gain was similarly affected, but food conversion from d 0 to d 42 was little affected by the inclusion of either peas or rapeseed. 5. Absolute breast muscle weight was affected by diet but there was no significant difference in breast weight as a proportion of total body weight. 6. From d 7 onwards, selection against the pea-containing diet approached statistical significance. Between d 7 and d 14, birds ate almost twice as much of the control as of the pea-containing diet. Birds offered a rapeseed meal diet ate similar amounts of that and the control diet. 7. The breast meat from birds given 200 g rapeseed/kg was the only meat identified as different but no strong aversion was expressed by the tasting panel.

Animal Feed↗

PubMed2001

Saponin content and trypsin inhibitor activity in processed and cooked pigeon pea cultivars.

Four high-yielding varieties of pigeon pea namely UPAS-120, Manak, JCPL-151. ICPL-87 had considerable amounts of antinutrients i.e. saponins and trypsin inhibitors. Saponin content of these unprocessed cultivars ranged from 2164 to 3494 mg/100 g. There were significant varietal variations in trypsin inhibitor activity (1007-1082 TIU/g) of these pigeon pea cultivars. Some simple, inexpensive and easy-to-use domestic processing and cooking methods, namely, soaking (6, 12, 18 h), soaking (12 h)-dehulling, ordinary cooking, pressure cooking and germination (24, 36, 48 h) were found to be quite effective in lowering the level of saponins and trypsin inhibitors in all the pigeon pea cultivars. Pressure cooking of soaked and dehulled seeds lowered the content of saponins to a maximum extent (28 to 38%) followed by ordinary cooking of soaked and dehulled seeds (28 to 35%), soaked dehulled raw seeds (22 to 27%) and 48 h germinated seeds (15 to 19%). Loss of TIA was marginal due to soaking but ordinary as well as pressure cooking of unsoaked and soaked-dehulled pigeon pea seeds reduced the TIA drastically. Pressure cooking of pigeon pea seeds completely destroyed the TIA while it was reduced to the extent of 86-88% against the control in 48 h pigeon pea sprouts.

Analysis of Variance↗

PubMed1990

[The effect of different high doses of field peas on the digestibility of their crude nutrients in colostomized laying hens].

Five groups of five colostomized laying hens each received 0 g, 15 g, 30 g, 45 g and 60 g peas of the variety Grapis per animal and day with Triticum rations. The apparent digestibility of the crude nutrients of the rations and the peas was determined, ascertained according to the difference method in dependence on their quotas in the rations. The digestibility of the N-free extracts of the peas increases by 3 digestion units each under the influence of the increasing intake of peas, so that the digestibility of the organic matter of the peas increases with the growing quota. On an average of the 20 individual values the following digestion values for the pea variety Grapis are indicated: organic matter 66.9%, crude protein 78.5%, crude fat 48.7%, N-free extracts 70.3%. Energy concentration amounts to 572 EFU-hen/kg dry matter.

Animal Feed↗

PubMed1993

Gibberellin (GA3) enhances cell wall invertase activity and mRNA levels in elongating dwarf pea (Pisum sativum) shoots.

The invertase (EC 3.2.1.26) purified from cell walls of dwarf pea stems to homogeneity has a molecular mass of 64 kilodaltons (kD). Poly(A)+RNA was isolated from shoots of dwarf pea plants, and a cDNA library was constructed using lambda gt11 as an expression vector. The expression cDNA library was screened with polyclonal antibodies against pea cell wall invertase. One invertase cDNA clone was characterized as a full-length cDNA with 1,863 base pairs. Compared with other known invertases, one homologous region in the amino acid sequence was found. The conserved motif, Asn-Asp-Pro-Asn-Gly, is located near the N-terminal end of invertase. Northern blot analysis showed that the amount of invertase mRNA (1.86 kb) was rapidly induced to a maximal level 4 h after GA3 treatment, then gradually decreased to the control level. The mRNA level at 4 h in GA3-treated peas was fivefold higher than that of the control group. The maximal increase in activity of pea cell wall invertase elicited by GA3 occcured at 8 h after GA3 treatment. This invertase isoform was shown immunocytochemically to be localized in the cell walls, where a 10-fold higher accumulation occurred in GA3-treated tissue compared with control tissue. This study indicates that the expression of the pea shoot cell-wall invertase gene could be regulated by GA3 at transcriptional and/or translational levels.

Amino Acid Sequence↗

PubMed2026

Identification and characterization of PsFwC9 conferring Fusarium wilt resistance in pea.

Pea (Pisum sativum L.) is one of the most important edible legumes in China, with both planting area and total yield ranking among the highest in the world. Fusarium wilt, caused by Fusarium oxysporum f. sp. pisi (Fop), is a severe factor limiting pea production. The deployment of resistant pea cultivars is the most effective and sustainable strategy for controlling this disease. In the present study, a novel resistance gene PsFwC9, conferring resistance to Fop race 5, was identified in the resistant pure line Chengwan 9-8 (CW9-8), and its candidate gene Psat4g213640 was characterized and functionally validated to be associated with disease resistance. Genetic analysis of the F₂ population derived from the cross between the resistant parent CW9-8 and the susceptible parent Chengwan 9-1 (CW9-1) revealed that PsFwC9 was controlled by a single dominant gene. Based on whole-genome resequencing, bulked segregant analysis sequencing (BSA-seq) and fine mapping, PsFwC9 was localized to an 817.06-kb region on chromosome 4 (i.e. linkage group IV, chr4LG4), flanked by KASP markers A016508 and A016511, and co-segregated with four markers. Haplotype analysis revealed that only the marker A016615 was significantly associated with Fusarium wilt resistance, and this marker was designated as a diagnostic marker for PsFwC9. Marker A016615 was located at 425 699 725 bp on chr4LG4, corresponding to the 277 bp within Psat4g213640, where a 'A/G' single-nucleotide polymorphism caused an amino acid substitution leading to an alteration in protein structure; therefore, Psat4g213640 was identified as the PsFwC9 candidate gene. Quantitative real-time PCR analysis showed no significant difference in the expression levels of Psat4g213640 between CW9-8 and CW9-1. Overexpression of the candidate gene Psat4g213640CW9-8 in the hairy root system significantly enhanced the resistance of CW9-1 to Fusarium wilt, whereas RNA interference-mediated silencing of Psat4g213640CW9-8 reduced the resistance of CW9-8, indicating that Psat4g213640CW9-8 played a crucial role in pea resistance to Fusarium wilt. In addition, subcellular localization showed that the protein encoded by Psat4g213640 was targeted to the endoplasmic reticulum. Collectively, these findings not only enriched the gene resources for disease resistance in pea and provided an important foundation for elucidating the molecular mechanism of PsFwC9-mediated resistance, but also provided important technical support for the practical application of molecular breeding for disease resistance in pea.

Journal Article↗

PubMed2004

Protein-enriched pea flour extract protects stored milled rice against the rice weevil, Sitophilus oryzae.

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.

Animals↗

PubMed1994

Pea fiber lowers fasting and postprandial blood triglyceride concentrations in humans.

The effect of a pea cell wall fiber preparation with a high content of soluble fiber on fasting and postprandial blood lipids was investigated in young healthy subjects. Inclusion of 33 g pea fiber product/10 MJ (20 g dietary fiber) in a low fiber diet was tested in five men and six women (mean age 23 y) in a strictly controlled randomized cross-over intervention study over 2 wk separated by a 2-wk period of habitual diet consumption. No significant differences in fasting concentrations of total cholesterol, LDL cholesterol or HDL cholesterol were observed, whereas total and VLDL triglyceride concentrations were lower when subjects consumed the pea fiber diet compared with the low fiber diet (P < 0.05). Postprandial response to pea fiber was studied in eight men. Addition of 12 g pea fiber product/ 10 MJ to a breakfast meal and 15 g/10 MJ to the following lunch meal resulted in significantly lower total triglyceride (P = 0.01), chylomicron triglyceride (P = 0.03) and insulin (P = 0.003) concentrations after the lunch meal compared with results following the same meal without pea fiber. No differences were observed in glycemic response. In conclusion, this source of dietary fiber lowered fasting and postprandial triglyceride concentrations but did not change fasting cholesterol concentrations.

Adult↗