Search Results (25)

Fusarium spp. are active producers of mycotoxins that enter the food chain and pose risks to human health. Identifying pathogenic agents is a key step in developing disease management strategies. For the first time in Bulgaria, we identified eight Fusarium species in wheat, harvest 2024–2025, through the application of DNA barcoding. For a genetic marker and construction of phylogenetic tree, the protein-coding gene β-tub was chosen. Among 26 identified isolates, F. sporotrichioides (42.3%) dominated, followed by F. proliferatum (23.1%), F. avenaceum (7.7%), F. armeniacum (7.7%), and F. poae (7.7%). F. tricinctum (3.8%), F. oxysporum (3.8%), and F. equiaseti (3.9%) were weakly expressed. Phylogenetic analysis classified the isolates into five species complexes: FSAMSC, FFSC, FTSC, FIESC, and FOSC and highlighted the genetic distances between them. Molecular genetic analysis showed that 84.6% of the wheat samples contained only one species of Fusarium, and in 15.4% the co-presence of two species was established. The largest share was in samples with a low infestation of 2–4%, which represented 35% (n = 32) of all positives. No statistically significant difference was found between varieties and contamination level, but a statistically significant positive correlation was demonstrated by the preceding crop (rapeseed, sunflower, and maize). Full article

Aquaporins are key membrane proteins that mediate water transport in plants and are indispensable for maintaining cellular water homeostasis and normal physiological processes. This study investigated the function of SbPIP1-3, an aquaporin gene isolated from drought-tolerant Sorghum bicolor. Bioinformatics analysis, subcellular localization, and heterologous expression of SbPIP1-3 were performed in Saccharomyces cerevisiae, Arabidopsis thaliana, and rapeseed. Sequence analysis revealed that SbPIP1-3 encodes a basic hydrophobic protein targeted to the plasma membrane, a finding further corroborated by subcellular localization assays. In yeast expression assays, SbPIP1-3-transformed strains retained viability under osmotic stress induced by 1.2 M mannitol, whereas non-transgenic control strains failed to survive. In Arabidopsis and rapeseed experiments, the SbPIP1-3 overexpression enhanced drought tolerance (improved germination, root growth, antioxidant enzyme activity, proline content, PSII repair capacity, and survival after drought–rewatering) and reduced intracellular H₂O₂ accumulation. Transcriptome profiling of drought-stressed transgenic Arabidopsis and control plants demonstrated significant upregulation of mostly stress-responsive pathways (e.g., MAPK signaling pathway and hormone signaling pathways) and key drought-tolerance genes (e.g., SNRK2-2, SOD1, APX3, GPX3, P5CS1). Collectively, these findings suggest that SbPIP1-3 enhances plant drought tolerance through the following mechanisms: improving transmembrane water transport efficiency to sustain cellular osmotic balance; activating the antioxidant defense system to increase enzyme activity and mitigate reactive oxygen species (ROS) accumulation; optimizing photosynthetic protection mechanisms to preserve the structural and functional integrity of PSII; and regulating the expression of stress-responsive signaling pathways and associated functional genes. Full article

Cottonseed meal (CSM) is a cost-effective protein source, but its application is limited by the toxicity of free gossypol. Traditional physical and chemical detoxification methods are costly, energy-intensive, and cause nutrient loss, while microbial fermentation-based biological detoxification is considered more sustainable than chemical or physical approaches. This study reports an alkaline protease from the marine strain Bacillus safensis DL12 isolated from Yellow Sea sediments. Following cloning of its encoding gene and heterologous expression, enzymatic characterization of the purified enzyme revealed optimal activity at pH 8.0 and 50 °C, with Fe²⁺, Cu²⁺, Ni²⁺, and dithiothreitol (DTT) significantly enhancing its activity. Substrate hydrolysis analysis using the purified enzyme on soybean meal, peanut meal, rapeseed meal, and cottonseed meal demonstrated that, compared to the control group, cottonseed meal hydrolysates exhibited a 55.6% relative increase in peptide content and a 41.5% relative improvement in the degree of hydrolysis (DH), indicating higher hydrolysis efficiency among the four substrates. Notably, when hydrolyzing cottonseed meal with purified enzyme versus crude enzyme preparation at equivalent activity, the purified enzyme effectively reduced free gossypol content by 70% compared to the control, achieving more efficient detoxification than the crude enzyme preparation and most reported microbial treatments. These results highlight the potential of B. safensis DL12 protease as a marine-derived enzyme, offering promising prospects for enhancing protein digestibility and addressing the long-standing challenge of gossypol toxicity in cottonseed meal utilization. Full article

Background/Objectives: Oleosomes, plant-derived lipid nanostructures comprising a triacylglycerol core surrounded by a phospholipid monolayer and interfacial proteins, provide sustainable alternatives to synthetic lipid vesicles. This study compares solvent-free aqueous extractions of oleosomes from five nuts (almond, macadamia, walnut, hazelnut, pine) and five seeds (flaxseed, sunflower, hemp, sesame, canola/rapeseed) to understand how botanical origin influences composition and physicochemical behavior. Methods: Oleosomes were isolated using solvent-free aqueous extraction. Extraction yield, lipid content, protein content, particle size, polydispersity, and zeta potential were determined using standard analytical assays and dynamic light scattering techniques. SDS–PAGE was performed to evaluate interfacial protein profiles and oleosin abundance. Results: Extraction yields ranged from 8.4% (flaxseed) to 59.5% (walnut). Oleosome diameters spanned 424 nm to 3.9 µm, and all oleosome dispersions exhibited negative zeta potentials (–26 to –57 mV). SDS–PAGE revealed abundant 15–25 kDa oleosins in seed oleosomes but relatively sparse proteins in nut oleosomes. Seed oleosomes were smaller and exhibited stronger electrostatic stabilization, while nut oleosomes formed larger droplets stabilized primarily through steric interactions due to lower oleosin content. Conclusions: Variation in oleosin abundance and interfacial composition leads to distinct stabilization mechanisms in nut and seed oleosomes. These findings establish a predictive basis for tailoring oleosome size, stability, and functionality, and highlight their potential as natural nanocarriers for food, cosmetic, and pharmaceutical formulations. Full article

This study investigated the potential of rapeseed protein isolate (RPI) as a sustainable alternative to soy protein isolate (SPI) in chicken pâtés, considering the combined effects of protein (SPI or RPI) and oil (sunflower or rapeseed) sources. The proximate composition, pH, water activity (a_w), and colour of the RPI-based formulations were largely comparable to their SPI counterparts and remained stable over 60 days of refrigerated storage. However, at day 0, the RPI-based samples exhibited lower pH values (approx. 6.09 vs. 6.41), slightly lower lightness (L* approx. 68.9 vs. 72.5), higher redness (a* approx. 4.72 vs. 3.58), and higher yellowness (b* approx. 23.3 vs. 9.38), indicating some initial formulation-dependent differences. Furthermore, RPI-based formulations exhibited enhanced textural properties and improved oxidative stability, likely due to synergistic effects between rapeseed protein and oil. The substitution of sunflower oil with rapeseed oil significantly improved the fatty acid profile (p < 0.05), notably increasing α-linolenic acid (C18:3n-3) and achieving a favourable n-6/n-3 ratio (approx. 2.8). Sensory evaluation revealed that the formulation combining both rapeseed ingredients provided a stable and highly acceptable profile. These results collectively demonstrate that RPI is a viable and functional replacer for SPI, enabling the production of nutritious, high-quality, and sustainable chicken pâtés. Full article

Rapeseed proteins, due to their quality and wide availability, have great potential for application in human nutrition. However, their high content of antinutritional compounds poses significant economic and environmental challenges for food industry applications. To overcome these obstacles, various extraction and modification techniques, including enzymatic and ultrasound-assisted methods, were used to enhance protein functionality and improve both nutritional and sensory properties. In this study, the effects of dephenolization on the structural, physicochemical, and functional properties of rapeseed protein isolate obtained from defatted rapeseed cake were investigated through four different protocols. All obtained protein isolates (PIs) exhibited high protein purity (above 65%), with a notable difference in extraction yield. Furthermore, the extraction process was optimized using an artificial neural network (ANN) model, which demonstrated high predictive performance. The optimal extraction conditions for the dephenolization of rapeseed oil cake were 84% ethanol concentration, a solid-to-liquid ratio of 1/60 w/v, and 15 min of ultrasound treatment, resulting in an impressive protein purity of 90.68% with a yield of 29.17%. The obtained proteins were further characterized and compared in terms of protein profile (FTIR and SDS-PAGE), amino acid composition, solubility, and digestibility. The protein isolate (PI) obtained under optimized conditions displayed superior functional properties, underscoring the relevance and necessity of a data-driven, mathematical approach for scale-up and industrial implementation. Full article

Sinapine adsorption was studied on four weak cation exchanges at pHs ranging from 2 to 8. The best adsorption rate was observed with C106 resin at pH 4 (95.25%). The adsorption kinetics followed a pseudo-second-order model while the isotherm data better fitted the Langmuir model. The ΔG°, ΔH°, and ΔS° values (−25.834 kJ·mol⁻¹, −24.428 kJ·mol⁻¹, and 0.004 kJ·mol⁻¹·K⁻¹) revealed that the adsorption process was spontaneous and exothermic. Acidified ethanol showed a better desorption rate (75.41%), while virtually no (3.32%) or low (31.14%) sinapine desorption was observed with 50% ethanol and 0.1 M HCl solution, respectively. This indicated that sinapine adsorption took place throughout both ionic and hydrophobic interactions. Very close sinapine adsorption performances were observed with an effluent of the patented rapeseed protein isolate process. Two-step desorption using 50% ethanol, then acidified ethanol, yielded a highly purified neutral sinapine-derivative phenol fraction (75.23%) in the first elution fraction and sinapine (98.85%) in the second one. Full article

This study investigates the production of protein hydrolysates with dipeptidyl peptidase-IV (DPP-IV) inhibitory activity from agro-industrial by-products, namely olive seed, sunflower seed, rapeseed, and lupin meals, as well as from two plant protein isolates such as pea and potato. Furthermore, the effect of simulated gastrointestinal digestion on the DPP-IV inhibitory activity of all the hydrolysates was evaluated. Overall, the lowest values of IC₅₀ (1.02 ± 0.09 – 1.24 ± 0.19 mg protein/mL) were observed for the hydrolysates with a high proportion of short-chain [< 1 kDa] peptides (i.e., olive seed, sunflower seed, and lupin) or high content of proline (i.e., rapeseed). Contrarily, the IC₅₀ of the pea and potato hydrolysates was significantly higher (1.50 ± 0.13 – 1.93 ± 0.13 mg protein/mL). In vitro digestion led to an increase in peptides <1 kDa for almost all hydrolysates (except olive and sunflower seed meals), which was noticeable for rapeseed, pea, and potato hydrolysates. Digestion did not significantly modify the DPP-IV inhibitory activity of olive, sunflower, rapeseed, and potato hydrolysates, whereas a significant decrease in IC₅₀ value was obtained for pea hydrolysate and a significant increase in IC₅₀ was obtained for lupin hydrolysate. Thus, this work shows the potential of agro-industrial by-products for the production of protein hydrolysates exhibiting DPP-IV inhibition. Full article

Aphids are a serious threat to rapeseed (Brassica napus L.) production, and cause unmanageable loss. Therefore, effective prevention and management strategies are urgently required to avoid losses. Bacillus amyloliquefaciens AK-12 isolated from a dead aphid with aphicidal activity was tagged with a green fluorescent protein through a natural transformation. The transformed strains were checked for stability and growth, and the best-performing strain was tested for its colonization inside and outside the rapeseed plant. The stability of AK-12-GFP reached more than 95%, and the growth curve was consistent with that of AK-12. After 30 days of treatment, the colonization of 1 × 10⁶ CFU/g was recorded in rapeseed leaves. Interestingly, AK-12 reduced the aphid transmission rate compared with the control and improved the growth of the rapeseed seedlings. Meanwhile, the AK-12 strain also exhibited phosphorus, potassium-solubilizing, and nitrogen-fixing activity, and produced 2.61 µg/mL of IAA at 24 h. Regulation in the activity of four enzymes was detected after the AK-12 treatment. Phenylalanine ammonia lyase (PAL) was recorded at a maximum of 86.84 U/g after 36 h, and catalase (CAT) decreased after 48 h; however, peroxidase (POD) and polyphenol oxidase (PPO) reached the maximum within 12 h of AK-12 application. Additionally, important resistance genes related to these enzymes were upregulated, indicating the activation of a defense response in the rapeseed against aphids. In conclusion, defense enzymes and defense-related gene activation could improve the pest resistance in rapeseed, which has good application prospects for the future to be developed into biopesticide. Full article

The fungal secretome is the main interface for interactions between the pathogen and its host. It includes the most important virulence factors and effector proteins. We integrated different bioinformatic approaches and used the newly drafted genome data of P. lingam isolate CAN1 (blackleg of rapeseed fungus) to predict the secretion of 217 proteins, including many cell-wall-degrading enzymes. All secretory proteins were identified; 85 were classified as CAZyme families and 25 were classified as protease families. Moreover, 49 putative effectors were predicted and identified, where 39 of them possessed at least one conserved domain. Some pectin-degrading enzymes were noticeable as a clustering group according to STRING web analysis. The secretome of P. lingam CAN1 was compared to the other two blackleg fungal species (P. lingam JN3 and P. biglobosus CA1) secretomes and their CAZymes and effectors were identified. Orthologue analysis found that P. lingam CAN1 shared 14 CAZy effectors with other related species. The Pathogen-Host Interaction database (PHI base) classified the effector proteins in several categories where most proteins were assigned as reduced virulence and two of them termed as hypervirulence. Nowadays, in silico approaches can solve many ambiguous issues about the mechanism of pathogenicity between fungi and plant host with well-designed bioinformatics tools. Full article

Rapeseed (Brassica napus L.) is an important crop for edible oil, vegetables, and biofuel. Rapeseed growth and development require a minimum temperature of ~1–3 °C. Notably, frost damage occurs during overwintering, posing a serious threat to the productivity and yield of rapeseed. MYB proteins are important transcription factors (TFs) in plants, and have been proven to be involved in the regulation of stress responses. However, the roles of the MYB TFs in rapeseed under cold stress conditions are yet to be fully elucidated. To better understand the molecular mechanisms of one MYB-like 17 gene, BnaMYBL17, in response to low temperature, the present study found that the transcript level of BnaMYBL17 is induced by cold stress. To characterize the gene’s function, the 591 bp coding sequence (CDS) from rapeseed was isolated and stably transformed into rapeseed. The further functional analysis revealed significant sensitivity in BnaMYBL17 overexpression lines (BnaMYBL17-OE) after freezing stress, suggesting its involvement in freezing response. A total of 14,298 differentially expressed genes relative to freezing response were found based on transcriptomic analysis of BnaMYBL17-OE. Overall, 1321 candidate target genes were identified based on differential expression, including Phospholipases C1 (PLC1), FCS-like zinc finger 8 (FLZ8), and Kinase on the inside (KOIN). The qPCR results confirmed that the expression levels of certain genes showed fold changes ranging from two to six when compared between BnaMYBL17-OE and WT lines after exposure to freezing stress. Furthermore, verification indicated that BnaMYBL17 affects the promoter of BnaPLC1, BnaFLZ8, and BnaKOIN genes. In summary, the results suggest that BnaMYBL17 acts as a transcriptional repressor in regulating certain genes related to growth and development during freezing stress. These findings provide valuable genetic and theoretical targets for molecular breeding to enhance freezing tolerance in rapeseed. Full article

Rapeseed meal (RSM), a by-product of rapeseed oil extraction, is currently used for low-value purposes. With a biorefinery approach, rapeseed proteins may be extracted and recovered for high-end uses to fully exploit their nutritional and functional properties. This study reports the application of RSM protein isolate, the main output of a biorefining process aimed at recovering high-value molecules from rapeseed meal, as a supplement to texture-modified (TM) food designed for elderly people with mastication and dysphagia problems. The compositional (macronutrients by Official Methods of Analyses, and mineral and trace element profiles using Inductively Coupled Plasma Optical Emission Spectrometry ICP-OES), nutritional and sensory evaluations of TM chicken breast, carrots and bread formulated without and with RSM protein supplementation (5% w/w) are hereby reported. The results show that the texture modification of food combined with rapeseed protein isolate supplementation has a positive impact on the nutritional and sensory profile of food, meeting the special requirements of seniors. TM chicken breast and bread supplemented with RSM protein isolate showed unaltered or even improved sensory properties and a higher nutrient density, with particular regard to proteins (+20–40%) and minerals (+10–16%). Supplemented TM carrots, in spite of the high nutrient density, showed a limited acceptability, due to poor sensory properties that could be overcome with an adjustment to the formulation. This study highlights the potentialities of RSM as a sustainable novel protein source in the food sector. The application of RSM protein proposed here is in line with the major current challenges of food systems such as the responsible management of natural resources, the valorization of agri-food by-products, and healthy nutrition with focus on elderly people. Full article

Preventing oxidation and microbial spoilage are both major concerns in food industries. In this context, this study aimed to valorize the total rapeseed meal proteins with controlled enzymatic proteolysis to generate potent mineral-chelating peptides from cruciferins while keeping intact the antimicrobial napins. Implementation of proteolysis of total rapeseed protein isolate with the Prolyve^® enzyme highlighted an interesting selective hydrolysis of the cruciferins. Hence, the mechanism of this particular hydrolysis was investigated through a Design of Experiments method to obtain a model for the prediction of kinetics (cruciferin degradation and napin purity) according to the operating conditions applied. Then, multicriteria optimization was implemented to maximize the napin purity and yield while minimizing both enzymatic cost and reaction time. Antioxidant assays of the peptide fraction obtained under the optimal conditions proved the high metal-chelating activity preservation (EC₅₀ = 247 ± 27 µg) for more than three times faster production. This fraction might counteract lipid oxidation or serve as preventing agents for micronutrient deficiencies, and the resulting purified napins may have applications in food safety against microbial contamination. These results can greatly help the development of rapeseed meal applications in food industries. Full article

Rapeseed meal is a by-product of the oil-producing industry with a currently underestimated application. Two protein isolates, PI_2.5–8.5 or PI_10.5–2.5, were obtained from industrial rapeseed meal after treatment with an aqueous ethanol solution. The alkaline-extracted proteins were sequentially precipitated by two different modes, from pH 10.5 to 2.5, and vice versa, from 2.5 to 8.5, with a step of 1 pH unit. The preparation approach influenced both the functional and antioxidant properties of the isolates. The PI_10.5–2.5 exhibited higher water and oil absorption capacities than PI_2.5–8.5, reaching 2.68 g H₂O/g sample and 2.36 g oil/g sample, respectively. The emulsion stability of the PI_2.5–8.5, evaluated after heating at 80 °C, was either 100% or close to 100% for all pH values studied (from 2 to 10), except for pH 6 where it reached 93.87%. For the PI_10.5–2.5, decreases in the emulsion stability were observed at pH 8 (85.71%) and pH 10 (53.15%). In the entire concentration range, the PI_10.5–2.5 exhibited a higher scavenging ability on 2,2-diphenyl-1-picryl hydrazyl (DPPH) and hydroxyl radicals than PI_2.5–8.5 as evaluated by DPPH and 2-deoxyribose assays, respectively. At the highest concentration studied, 1.0%, the neutralization of DPPH radicals by PI_10.5–2 reached half of that exhibited by synthetic antioxidant butylhydroxytoluene (82.65%). At the same concentration, the inhibition of hydroxyl radicals by PI_10.5–2 (71.25%) was close to that achieved by mannitol (75.62%), which was used as a positive control. Established antioxidant capacities add value to the protein isolates that can thus be used as both emulsifiers and antioxidants. Full article

Rapeseed protein is not currently utilized for food applications, although it has excellent physicochemical, functional, and nutritional properties similar to soy protein. Thus, the goal of this study was to create new plant-based extrudates for application as high-moisture meat analogs from a 50:50 blend of rapeseed protein concentrate (RPC) and yellow pea isolate (YPI) using high-moisture-extrusion (HME) cooking with a twin-screw extruder to gain a better understanding of the properties of the protein powders and resulting extrudates. The effects of extrusion processing parameters such as moisture content (60%, 63%, 65%, 70%), screw speed (500, 700, and 900 rpm), and a barrel temperature profile of 40–80–130–150 °C on the extrudates’ characteristics were studied. When compared to the effect of varying screw speeds, targeted moisture content had a larger impact on textural characteristics. The extrudates had a greater hardness at the same moisture content when the screw speed was reduced. The specific mechanical energy (SME) increased as the screw speed increased, while increased moisture content resulted in a small reduction in SME. The lightness (L*) of most samples was found to increase as the target moisture content increased from 60% to 70%. The RPC:YPI blend was equivalent to proteins produced from other sources and comparable to the FAO/WHO standard requirements. Full article