Seed production determines the entrance to dormancy of the inflorescence meristem of Pisum sativum and the end of the flowering period.

Flowering plants adjust their reproductive period to maximize the success of the offspring. Monocarpic plants, those with a single reproductive cycle that precedes plant senescence and death, tightly regulate both flowering initiation and flowering cessation. The end of the flowering period involves the arrest of the inflorescence meristem activity, known as proliferative arrest, in what has been interpreted as an evolutionary adaptation to maximize the allocation of resources to seed production and the viability of the progeny. Factors influencing proliferative arrest were described for several monocarpic plant species many decades ago, but only in the last few years studies performed in Arabidopsis have allowed to approach proliferative arrest regulation in a comprehensive manner by studying the physiology, hormone dynamics, and genetic factors involved in its regulation. However, these studies remain restricted to Arabidopsis and there is a need to expand our knowledge to other monocarpic species to propose general mechanisms controlling the process. In this work, we have characterized proliferative arrest in Pisum sativum, trying to parallel available studies in Arabidopsis to maximize this comparative framework. We have assessed quantitatively the role of fruits/seeds in the process, the influence of the positional effect of these fruits/seeds in the behavior of the inflorescence meristem, and the transcriptomic changes in the inflorescence associated with the arrested state of the meristem. Our results support a high conservation of the factors triggering arrest in pea and Arabidopsis, but also reveal differences reinforcing the need to perform similar studies in other species.

The Long-Distance Transport of Jasmonates in Salt-Treated Pea Plants and Involvement of Lipid Transfer Proteins in the Process.

The adaption of plants to stressful environments depends on long-distance responses in plant organs, which themselves are remote from sites of perception of external stimuli. Jasmonic acid (JA) and its derivatives are known to be involved in plants' adaptation to salinity. However, to our knowledge, the transport of JAs from roots to shoots has not been studied in relation to the responses of shoots to root salt treatment. We detected a salt-induced increase in the content of JAs in the roots, xylem sap, and leaves of pea plants related to changes in transpiration. Similarities between the localization of JA and lipid transfer proteins (LTPs) around vascular tissues were detected with immunohistochemistry, while immunoblotting revealed the presence of LTPs in the xylem sap of pea plants and its increase with salinity. Furthermore, we compared the effects of exogenous MeJA and salt treatment on the accumulation of JAs in leaves and their impact on transpiration. Our results indicate that salt-induced changes in JA concentrations in roots and xylem sap are the source of accumulation of these hormones in leaves leading to associated changes in transpiration. Furthermore, they suggest the possible involvement of LTPs in the loading/unloading of JAs into/from the xylem and its xylem transport.

Sensoproteomic Characterization of Lactobacillus Johnsonii-Fermented Pea Protein-Based Beverage: A Promising Strategy for Enhancing Umami and Kokumi Sensations while Mitigating Bitterness.

This study investigated the mechanism underlying the flavor improvement observed during fermentation of a pea protein-based beverage using Lactobacillus johnsonii NCC533. A combination of sensomics and sensoproteomics approach revealed that the fermentation process enriched or generated well-known basic taste ingredients, such as amino acids, nucleotides, organic acids, and dipeptides, besides six new taste-active peptide sequences that enhance kokumi and umami notes. The six new umami and kokumi enhancing peptides, with human recognition thresholds ranging from 0.046 to 0.555 mM, are produced through the degradation of Pisum sativum's storage protein. Our findings suggest that compounds derived from fermentation enhance umami and kokumi sensations and reduce bitterness, thus improving the overall flavor perception of pea proteins. In addition, the analysis of intraspecific variations in the proteolytic activity of L. johnsonii and the genome-peptidome correlation analysis performed in this study point at cell-wall-bound proteinases such as PrtP and PrtM as the key genes necessary to initiate the flavor improving proteolytic cascade. This study provides valuable insights into the molecular mechanisms underlying the flavor improvement of pea protein during fermentation and identifies potential future research directions. The results highlight the importance of combining fermentation and senso(proteo)mics techniques in developing tastier and more palatable plant-based protein products.

Effective population size in field pea.

BACKGROUND: Effective population size (Ne) is a pivotal parameter in population genetics as it can provide information on the rate of inbreeding and the contemporary status of genetic diversity in breeding populations. The population with smaller Ne can lead to faster inbreeding, with little potential for genetic gain making selections ineffective. The importance of Ne has become increasingly recognized in plant breeding, which can help breeders monitor and enhance the genetic variability or redesign their selection protocols. Here, we present the first Ne estimates based on linkage disequilibrium (LD) in the pea genome. RESULTS: We calculated and compared Ne using SNP markers from North Dakota State University (NDSU) modern breeding lines and United States Department of Agriculture (USDA) diversity panel. The extent of LD was highly variable not only between populations but also among different regions and chromosomes of the genome. Overall, NDSU had a higher and longer-range LD than the USDA that could extend up to 500 Kb, with a genome-wide average r2 of 0.57 (vs 0.34), likely due to its lower recombination rates and the selection background. The estimated Ne for the USDA was nearly three-fold higher (Ne = 174) than NDSU (Ne = 64), which can be confounded by a high degree of population structure due to the selfing nature of pea. CONCLUSIONS: Our results provided insights into the genetic diversity of the germplasm studied, which can guide plant breeders to actively monitor Ne in successive cycles of breeding to sustain viability of the breeding efforts in the long term.

Screening of a Microbial Culture Collection: Empowering Selection of Starters for Enhanced Sensory Attributes of Pea-Protein-Based Beverages.

Pea-protein-based ingredients are gaining attention in the food industry due to their nutritional benefits and versatility, but their bitter, astringent, green, and beany off-flavors pose challenges. This study applied fermentation using microbial cultures to enhance the sensory qualities of pea-protein-based beverages. Using UHPLC-TOF-MS analyses along with sensory profile comparisons, microbial species such as Limosilactobacillus fermentum, Lactococcus lactis, Lactobacillus johnsonii, Lacticaseibacillus rhamnosus, and Bifidobacterium longum were preselected from an entire culture collection and found to be effective in improving the overall flavor impression by reducing bitter off-notes and enhancing aroma profiles. Notably, L. johnsonii NCC533 and L. fermentum NCC660 exhibited controlled proteolytic activities after 48 h of fermentation, enriching the matrix with taste-active amino acids, nucleotides, and peptides and improving umami and salty flavors while mitigating bitterness. This study has extended traditional volatile analyses, including nonvolatile metabolomic, proteomic, and sensory analyses and offering a detailed view of fermentation-induced biotransformations in pea-protein-based food. The results highlight the importance of combining comprehensive screening approaches and sensoproteomic techniques in developing tastier and more palatable plant-based protein products.

Solubility, (micro)structure, and in vitro digestion of pea protein dispersions as affected by high pressure homogenization and environmental conditions.

In this work, dispersions were prepared with commercial pea protein isolate (PPI) and subjected to different (i) high pressure homogenization (HPH) intensities (0 - 200 MPa) (room temperature, pH 7) or (ii) environmental conditions (60 °C, pH 7 or pH 12) to generate dispersions with distinct protein molecular and microstructural characteristics, impacting protein solubility. Besides, protein digestion was analyzed following the static INFOGEST in vitro digestion protocol. Generally, increasing pressure of the homogenization treatment was linked with decreasing particle sizes and enhanced protein digestion. More specifically, the dispersion that did not undergo HPH (0 MPa) as well as the dispersion treated at 60 °C, pH 7, had highly similar microstructures, consisting of large irregular particles (10 - 500 µm) with shell-like structures, and exhibited low solubility (around 15 % and 28 %, respectively), which resulted in limited proteolysis (35 % and 42 %, respectively). In contrast, the dispersion subjected to HPH at 100 MPa and the dispersion treated at 60 °C, pH 12 also had similar microstructures with small and homogeneous particles (<1 µm), and exhibited relatively good solubility (54 % and 31 %, respectively), which led to enhanced protein digestion levels (87 % and 74 %, respectively). This study highlights the potential of food processing on macronutrient (micro)structure and further gastrointestinal stability and functionality.

Enhancing the usability of pea protein in emulsion applications through modification by various approaches: A comparative study.

The extensive utilization in food industry of pea protein is often impeded by its low water solubility, resulting in poor functional properties. Various methods, including pH-shifting (PS), ultrasonication (US), high-pressure micro-fluidization (MF), pH-shifting combined with ultrasonication (PS-US), and pH-shifting with micro-fluidization (PS-MF), were utilized to modify pea protein isolate (PPI) in order to enhance its functionality in emulsion formulation. The physicochemical properties and structural changes of the protein were investigated by assessing solubility, particle size, surface charge, protein profile, surface hydrophobicity, free sulfhydryl groups, and secondary structure content. The extent of modification induced by each treatment method on PPI-stabilized emulsions was compared based on parameters such as adsorbed interfacial protein concentration, particle size, zeta potential, and microstructure of the prepared emulsions. All modification increased the solubility of pea protein in the sequence of PS (4-fold) < MF (7-fold) < US (11-fold) < PS-US (13-fold) < PS-MF (14-fold). For single treatments, proteins dissolved more readily under US, resulting in the most uniform emulsions with small particle. The combined processes of PS-US and PS-MF further improved solubility, decreased emulsions particle size, promoted uniformity of emulsions. PS-US-stabilized emulsions displayed more smaller droplet size, narrower size distribution, and slightly higher stability than those prepared by PS-MF. The relatively higher emulsifying capacity of PPI treated by PS-US than those by PS-MF may be attributed to its higher surface hydrophobicity.

Thermal stability, antioxidant activity and bioavailability of pea protein-naringin Pickering emulsion for enhanced delivery applications.

After successfully addressing to mitigate bitterness of naringin through construction Pickering emulsion using pea protein (PP) and naringin (NG) in our previous study, we now probed thermal stability, antioxidant efficacy, and bioavailability. FTIR analysis and UV-vis spectroscopy indicated predominant interactions between PP and NG were hydrogen and hydrophobic bonds. TGA and DSC analyses demonstrated that PP-NG complexes exhibited superior heat-resistance compared to pure PP and NG. Thermal stability assessments indicated a significant retention of NG in the PP-NG Pickering emulsion than the control NG across varied temperatures (4 °C, 25 °C, 37 °C, and 65 °C). Moreover, the antioxidant activity of PP-NG emulsion was dependent on the concentration of NG, as evidenced by DPPH and ABTS free radicals scavenging abilities, ferric reducing power, and lipid peroxidation resistance. Additionally, PP-NG Pickering emulsion exhibited substantially high bioavailability (92.01 ± 3.91%). These results suggest a promising avenue for the application of NG with improved characteristics.

Effect of limited proteolysis and CaCl2 on the rheology, microstructure and in vitro digestibility of pea protein-carboxymethyl cellulose mixed gel.

Limited proteolysis, CaCl2 and carboxymethyl cellulose (CMC) have individually demonstrated ability to increase the gel strength of laboratory-extracted plant proteins. However, the syneresis effects of their combination on the gelling capacity of commercial plant protein remains unclear. This was investigated by measuring the rheological property, microstructure and protein-protein interactions of gels formed from Alcalase hydrolyzed or intact pea proteins in the presence of 0.1 % CMC and 0-25 mM CaCl2. Sodium dodecyl-sulfate polyacrylamide gel electrophoresis (SDS-PAGE) showed the molecular weight of pea protein in the mixture were < 15 kDa after hydrolysis. The hydrolysates showed higher intrinsic fluorescence intensity and lower surface hydrophobicity than the intact proteins. Rheology showed that the storage modulus (G') of hydrolyzed pea protein (PPH)-based gels sightly decreased compared to those of native proteins. 5-15 mM CaCl2 increased the G' for both PP and PPH-based gels and decreased the strain in the creep-recovery test. Scanning electron microscopy (SEM) showed the presence of smaller protein aggregates in the PPH-based gels compared to PP gels and the gel network became denser, and more compact and heterogenous in the presence of 15 and 25 mM CaCl2. The gel dissociation assay revealed that hydrophobic interactions and hydrogen bonds were the dominant forces to maintain the gel structure. In vitro digestion showed that the soluble protein content in PPH-based gels was 10 âˆ¼ 30 % higher compared to those of the PP counterpart. CaCl2 addition reduced protein digestibility with a concentration dependent behavior. The results obtained show contrasting effects of limited proteolysis and CaCl2 on the gelling capacity and digestibility of commercial pea proteins. These findings offer practical guidelines for developing pea protein-based food products with a balanced texture and protein nutrition through formulation and enzymatic pre-treatment.

Effects of Pea (Pisum sativum) Prebiotics on Intestinal Iron-Related Proteins and Microbial Populations In Vivo (Gallus gallus).

Iron deficiency remains a public health challenge globally. Prebiotics have the potential to improve iron bioavailability by modulating intestinal bacterial population, increasing SCFA production, and stimulating expression of brush border membrane (BBM) iron transport proteins among iron-deficient populations. This study intended to investigate the potential effects of soluble extracts from the cotyledon and seed coat of three pea (Pisum sativum) varieties (CDC Striker, CDC Dakota, and CDC Meadow) on the expression of BBM iron-related proteins (DCYTB and DMT1) and populations of beneficial intestinal bacteria in vivo using the Gallus gallus model by oral gavage (one day old chicks) with 1 mL of 50 mg/mL pea soluble extract solutions. The seed coat treatment groups increased the relative abundance of Bifidobacterium compared to the cotyledon treatment groups, with CDC Dakota seed coat (dark brown pigmented) recording the highest relative abundance of Bifidobacterium. In contrast, CDC Striker Cotyledon (dark-green-pigmented) significantly increased the relative abundance of Lactobacillus (p < 0.05). Subsequently, the two dark-pigmented treatment groups (CDC Striker Cotyledon and CDC Dakota seed coats) recorded the highest expression of DCYTB. Our study suggests that soluble extracts from the pea seed coat and dark-pigmented pea cotyledon may improve iron bioavailability by affecting intestinal bacterial populations.

Cadmium Alters the Metabolism and Perception of Abscisic Acid in Pisum sativum Leaves in a Developmentally Specific Manner.

Abscisic acid (ABA) plays a crucial role in plant defense mechanisms under adverse environmental conditions, but its metabolism and perception in response to heavy metals are largely unknown. In Pisum sativum exposed to CdCl2, an accumulation of free ABA was detected in leaves at different developmental stages (A, youngest, unexpanded; B1, youngest, fully expanded; B2, mature; C, old), with the highest content found in A and B1 leaves. In turn, the content of ABA conjugates, which was highest in B2 and C leaves under control conditions, increased only in A leaves and decreased in leaves of later developmental stages after Cd treatment. Based on the expression of PsNCED2, PsNCED3 (9-cis-epoxycarotenoid dioxygenase), PsAO3 (aldehyde oxidase) and PsABAUGT1 (ABA-UDP-glucosyltransferase), and the activity of PsAOγ, B2 and C leaves were found to be the main sites of Cd-induced de novo synthesis of ABA from carotenoids and ABA conjugation with glucose. In turn, ß-glucosidase activity and the expression of genes encoding ABA receptors (PsPYL2, PsPYL4, PsPYL8, PsPYL9) suggest that in A and B1 leaves, Cd-induced release of ABA from inactive ABA-glucosyl esters and enhanced ABA perception comes to the forefront when dealing with Cd toxicity. The distinct role of leaves at different developmental stages in defense against the harmful effects of Cd is discussed.

The influence of biological products and growth regulators on the yield and quality indicators of pea seeds of various varieties.

Peas are an important agricultural crop of great importance in human and animal nutrition. Peas, being a legume crop, help replenish nitrogen reserves in the soil. In field studies of the Federal State Budgetary Scientific Institution of the Federal Scientific Center of Legumes and Goat Crops (Oryol region), the influence of various growth regulators and biological products on the yield and quality indicators of pea seeds of the Nord and Multik varieties was studied. Pea plants are grown on dark gray forest, medium loamy soil of average cultivation. Before sowing, pea seeds were treated with solutions of Kornevin, Albit and Epin-extra by soaking for 5 hours. Solutions of the drugs were used at a concentration of 10-6 M, then dried and treated with Rizotorfin before sowing. Growth rates during the growing season and the yield of pea plants were determined. The content of protein, starch and amylose in starch was determined in the seeds. Research results have shown that the yield of pea plants depends on weather conditions. Under favorable weather conditions, the highest yield was obtained from the pea variety Nord (42.2 c/ha) in the variant with seed treatment with Kornevin, and in the Multik variety (43.0 c/ha) when treated with Rizotorfin. In arid conditions, the highest yield of peas of the Nord variety was obtained using the preparations Epin-extra and Kornevin. The highest yield of peas of the Multik variety was obtained using the preparations Rizotorfin, Kornevin and Epin-Extra. The research results, confirmed by statistical evaluation, showed that bioregulators and growth regulators help stimulate the amount of nitrogen supplied to plants, as well as the synthetic processes of protein synthesis. This contributed to improving the quality of seeds and green mass.

Artificial and biological supports are different for pea plants.

Previous studies on the kinematics of pea plants' ascent and attach behavior have demonstrated that the signature of their movement varies depending on the kind of support. So far, these studies have been confined to artificial supports (e.g. wooden sticks). Little is known regarding the conditions under which pea plants could rely on biological supports (e.g. neighboring plants) for climbing toward the light. In this study, we capitalize on the 3D kinematic analysis of movement to ascertain whether pea plants scale their kinematics differently depending on whether they aim for artificial or biological support. Results suggest that biological support determines a smoother and more accurate behavior than that elicited by the artificial one. These results shed light on pea plants' ability to detect and classify the properties of objects and implement a movement plan attuned to the very nature of the support. We contend that such differences depend on the augmented multisensory experience elicited by the biological support.

Deciphering genotype-by-environment interaction of grass pea genotypes under rain-fed conditions and emphasizing the role of monthly rainfall.

Rainfed regions have inconsistent spatial and temporal rainfall. So, these regions could face water deficiency during critical stages of crop growth. In this regard, multi-environment trials could play a key role in introducing stable genotypes with good performance across several rainfed regions. Grass pea, as a potential forage crop, is a resilient plant that could grow in unsuitable circumstances. In this study, agro-morphological attributes of 16 grass pea genotypes were examined in four semi-warm rain-fed regions during the years 2018-2021. The MLM analysis of variance showed a significant genotype-by-environment interaction (GEI) for dry yield, seed yield, days to maturity, days to flowering, and plant height of grass pea. The PLS (partial least squares) regression revealed that rainfall in the grass pea establishment stage (October and November) is meaningful. For grass pea cultivation, monthly rainfall during plant growth is important, especially in May, with an aim for seed yield. Regarding dry yield, G5, G10, G11, G12, G13, and G15 were selected as good performers and stable genotypes using DY × WAASB biplots, while SY × WAASB biplot manifested G2, G3, G12, and G13 as superior genotypes with stable seed yield. Considering equal weights for yield as well as the WAASB stability index (50/50), G13 was selected as the best one. Among test environments, E2 and E11 played a prominent role in distinguishing the above genotypes from other ones. In this study, MTSI (multi-trait stability index) analysis was applied to select a stable genotype, considering all measured agro-morphological traits simultaneously. Henceforth, the G5 and G15 grass pea genotypes were discerningly chosen due to their commendable performance in the WAASBY plot. In this context, G13 did not emerge as the winner based on MTSI; however, it exhibited an MTSI value in close proximity to the outer boundary of the circle. Consequently, upon comprehensive consideration of all traits, it is deduced that G5, G13, and G15 can be appraised as promising superior genotypes with stability across diverse environmental conditions.

Understanding Stabilization of Oil-in-Water Emulsions with Pea Protein─Studies of Structure and Properties.

This study investigates the stability and structure of oil-in-water emulsions stabilized by pea protein. Of the wide range of emulsion compositions explored, a region of stability at a minimum of 5% w/v pea protein and 30-50% v/v oil was determined. This pea protein concentration is more than what is needed to form a layer covering the interface. X-ray scattering revealed a thick, dense protein layer at the interface as well as hydrated protein dispersed in the continuous phase. Shear-thinning behavior was observed, and the high viscosity in combination with the thick protein layer at the interface creates a good stability against creaming and coalescence. Emulsions in a pH range from acidic to neutral were studied, and the overall stability was observed to be broadly similar independently of pH. Size measurements revealed polydisperse protein particles. The emulsion droplets are also very polydisperse. Apart from understanding pea protein-stabilized emulsions in particular, insights are gained about protein stabilization in general. Knowledge of the location and the role of the different components in the pea protein material suggests that properties such as viscosity and stability can be tailored for various applications, including food and nutraceutical products.

In situ interaction of pea peptides and bile salts under in vitro digestion: Potential impact on lipolysis.

The present work evaluated how a native pea protein isolate (PPI) affects the key roles carried out by bile salts (BS) in lipid digestion by means of the in vitro static INFOGEST protocol. Two gastric residence times were evaluated (10 and 60 min), and then the peptides obtained (GPPP) were mixed with BS at physiological concentration in simulated intestinal fluid to understand how they interact with BS both at the bulk and at the interface. Both GPPP give rise to a film with a predominant viscous character that does not constitute a barrier to the penetration of BS, but interact with BS in the bulk duodenal fluid. When the peptides flushing from the stomach after the different gastric residence times undergo duodenal digestion, it was found that for the longer gastric residence time the percentage of soluble fraction in the duodenal phase, that perform synergistically with BS micelles, was twice that of the lower residence time, leading to an increase in the solubilization of oleic acid. These results finally lead to a greater extent of lipolysis of olive oil emulsions. This work demonstrates the usefulness of in vitro models as a starting point to study the influence of gastric residence time of pea protein on its interaction with BS, affecting lipolysis. Pea proteins were shown to be effective emulsifiers that synergistically perform with BS improving the release and bioaccessibility of bioactive lipids as olive oil.

afila, the origin and nature of a major innovation in the history of pea breeding.

The afila (af) mutation causes the replacement of leaflets by a branched mass of tendrils in the compound leaves of pea - Pisum sativum L. This mutation was first described in 1953, and several reports of spontaneous af mutations and induced mutants with a similar phenotype exist. Despite widespread introgression into breeding material, the nature of af and the origin of the alleles used remain unknown. Here, we combine comparative genomics with reverse genetic approaches to elucidate the genetic determinants of af. We also investigate haplotype diversity using a set of AfAf and afaf cultivars and breeding lines and molecular markers linked to seven consecutive genes. Our results show that deletion of two tandemly arranged genes encoding Q-type Cys(2)His(2) zinc finger transcription factors, PsPALM1a and PsPALM1b, is responsible for the af phenotype in pea. Eight haplotypes were identified in the af-harbouring genomic region on chromosome 2. These haplotypes differ in the size of the deletion, covering more or less genes. Diversity at the af locus is valuable for crop improvement and sheds light on the history of pea breeding for improved standing ability. The results will be used to understand the function of PsPALM1a/b and to transfer the knowledge for innovation in related crops.

Identification of volatile and odor-active compounds in pea protein fractions obtained by a modified extraction method using fermentation.

This study investigates the aromatic composition of pea albumin and globulin fractions obtained through either fermentation or conventional acidification using hydrochloric acid (control) toward the isoelectric point of pea globulins. Different lactic acid bacteria were used including S. thermophilus (ST), L. plantarum (LP), and their coculture (STLP). The volatile compounds were extracted by solvent-assisted flavor evaporation technique and quantified by gas chromatography-mass spectrometry (GC-MS). Odor-active compounds (OAC) were further characterized by gas chromatography-olfactometry (GC-O). In total, 96 volatile and 36 OACs were identified by GC-MS and GC-O, respectively. The results indicated that the protein fractions obtained by conventional acidification were mainly described by green notes for the presence of different volatile compounds such as hexanal. However, the samples obtained by fermentation had a lower content of these volatile compounds. Moreover, protein fractions obtained by coculture fermentation were described by volatile compounds associated with fruity, floral, and lactic notes. PRACTICAL APPLICATION: The insights from this study on pea protein aroma could find practical use in the food industry to enhance the sensory qualities of plant-based products. By utilizing fermentation methods and specific lactic acid bacteria combinations, manufacturers may produce pea protein with reduced undesirable green notes, offering consumers food options with improved flavors. This research may contribute to the development of plant-based foods that not only provide nutritional benefits but also meet consumer preferences for a more appealing taste profile.

The interplay of muscle and pea proteins in low-salt gels: An insight into in situ structure formation in hybrid meat alternatives.

The present study investigated thermal gelation of mixed sarcoplasmic (Sarc), myofibrillar (Myof), and pea proteins corresponding to partial meat replacements (0, 25, and 50%) by pea protein isolate (PPI) at reducing salt levels (0.6 â†’ 0.1 M NaCl) to understand in situ (simulated) structure-forming properties of hybrid meat analogues. The amount of soluble proteins in hybrids generally increased with salt concentrations and PPI substitution. While muscle proteins (mixed Sarc and Myof) had the strongest gelling capacity, hybrid proteins also exhibited moderate aggregation and gelling activity based on the sol→gel rheological transition and gel hardness testing. Sarc and pea 7S/11S globulins collectively compensated for the attenuated gelling capacity of mixed proteins due to diminishing Myof in the hybrids. Immobilized water within hybrid protein gels was tightly bonded (T2 from nuclear magnetic resonance), consistent with the dense and uniform microstructure observed. These findings offer a new knowledge base for developing reduced-salt hybrid meat analogues.

Fine mapping and identification of a Fusarium wilt resistance gene FwS1 in pea.

KEY MESSAGE: A Fusarium wilt resistance gene FwS1 on pea chromosome 6 was identified and mapped to a 91.4 kb region by a comprehensive genomic-based approach, and the gene Psat6g003960 harboring NB-ARC domain was identified as the putative candidate gene. Pea Fusarium wilt, incited by Fusarium oxysporum f. sp. pisi (Fop), has always been a devastating disease that causes severe yield losses and economic damage in pea-growing regions worldwide. The utilization of pea cultivars carrying resistance gene is the most efficient approach for managing this disease. In order to finely map resistance gene, F2 populations were established through the cross between Shijiadacaiwan 1 (resistant) and Y4 (susceptible). The resistance genetic analysis indicated that the Fop resistance in Shijiadacaiwan 1 was governed by a single dominant gene, named FwS1. Based on the bulked segregant analysis sequencing analyses, the gene FwS1 was initially detected on chromosome 6 (i.e., linking group II, chr6LG2), and subsequent linkage mapping with 589 F2 individuals fine-mapped the gene FwS1 into a 91.4 kb region. The further functional annotation and haplotype analysis confirmed that the gene Psat6g003960, characterized by a NB-ARC (nucleotide-binding adaptor shared by APAF-1, R proteins, and CED-4) domain, was considered as the most promising candidate gene. The encoding amino acids were altered by a "T/C" single-nucleotide polymorphism (SNP) in the first exon of the Psat6g003960, and based on this SNP locus, the molecular marker A016180 was determined to be a diagnostic marker for FwS1 by validating its specificity in both pea accessions and genetic populations with different genetic backgrounds. The FwS1 with diagnostic KASP marker A016180 could facilitate marker-assisted selection in resistance pea breeding in pea. In addition, a comparison of the candidate gene Psat6g003960 in 74SN3B and SJ1 revealed the same sequences. This finding indicated that 74SN3B carried the candidate gene for FwS1, suggesting that FwS1 and Fwf may be closely linked or an identical resistant gene against Fusarium wilt.