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.

This research presents a novel approach to protein extraction from cauliflower (CL) and broccoli (BL) waste leaves by using enzymatic pretreatment, demonstrating its effectiveness on protein yield. Enzymatic pretreatment (pH 4.5, 10 h, t = 35 °C), was performed using commercial enzyme preparations, Viscozyme^® L and Vinozyme^®, in three different enzyme-to-substrate ratios E/S (0.2%, 2.5%, and 4.8%) of each enzyme. Leaf proteins (LPs) were obtained with alkaline extraction at pH 10–11 and their isoelectric precipitation at pH 4, following the control sample (extraction without enzymes). Protein yield (%), which was used as a parameter to monitor enzymatic efficiency, demonstrated a direct correlation with the enzyme-to-substrate (E/S) ratio. The highest protein yields were obtained at an enzyme concentration of 4.8% for both cellulolytic and pectolytic enzyme preparations, yielding 14.90 ± 0.12% for CL and 29.88 ± 0.86% for BL. The obtained proteins were characterized by FTIR spectroscopy and SDS-PAGE electrophoresis, and these methods confirmed the enzymatic efficiency of protein isolation. Isolated LPs showed high protein content for CLP 4.8% (77.27 ± 0.14%) and BPL 4.8% (84.66 ± 0.51%), and an increase in total amino acids, while the content of essential amino acids was over 40%. Protein solubility was assessed, revealing significant improvements (p < 0.05) in LPs derived from CL and BL at the highest E/S ratio of 4.8%, compared to the control sample C0%. Specifically, the solubility of CLP reached 29.4 mg/mL at pH 11, while BLP achieved 36.4 mg/mL at pH 10. As a result, these leaf proteins not only meet nutritional demands but also open innovative avenues of research in food science and biotechnology.

Biopolymers have gained significant attention due to their environmental advantages, with insects emerging as a promising but underutilized source of chitin and chitosan. In this study, chitosan was extracted from the larval exuviae of Tenebrio molitor through sequential demineralization, deproteinization, and deacetylation steps. For selected analyses, the extracted chitosan was further purified via reprecipitation from an acid solution using a basic precipitant (1 M NaOH). Chitosan was then characterized using chemical and instrumental methods. The results indicated that the chitosan had a medium degree of deacetylation (72.27%) and viscosity-average molecular weight (612 kDa), along with minimal ash (0.33%) and amino acid (0.14%) content, suggesting high product quality. FTIR analysis identified characteristic functional groups present, and SEM analysis highlighted a fibrous and porous microstructure in the purified chitosan. The prepared films exhibited favorable properties, including low thickness (0.0197 mm), high swelling degree (335.07%), moderate water solubility (46.99%), and moisture content of 32.39%, supporting their practical applicability. T. molitor exuviae thus represents a sustainable and environmentally friendly source of high-quality chitosan, with beneficial structural and functional properties, supporting its use in a wide array of value-added applications.

Consumer requirements for confectionery products have changed significantly over the past decade. These changes are evident in the growing demand for products that are high in protein but lower in energy content and, as a result, the market for these types of products is expanding. This study compared the chemical composition and functional properties of pork meat protein (MP) and blood plasma protein (BP) and evaluated their incorporation into cocoa cream formulations. Functional properties, such as water-holding capacity (WHC) and oil-holding capacity (OHC), were determined. Essential amino acid profiles were determined using HPLC analysis, and protein digestibility was evaluated both in the native form and after incorporation into the cocoa cream matrix via in vitro enzymatic digestion assays. Additionally, antioxidant activity of the enriched cocoa creams was assessed using the established ABTS assay. Results showed that BP contained a higher proportion of essential amino acids (26.44% of total amino acids), meeting the FAO/WHO recommendations, and exhibited superior digestibility compared to MP. Both proteins demonstrated high WHC and OHC values. The antioxidant potential of BP-enriched cocoa cream further supported its functional benefits. These findings indicate that blood plasma protein is a promising ingredient for enhancing the nutritional and functional quality of cocoa cream products.

Sunflower meal (SFM), a byproduct of sunflower oil extraction, is a relatively inexpensive protein source with high potential for feed formulations. Dry fractionation methodologies are emerging as ‘green’ and affordable technologies with the potential to additionally enhance the nutritional quality of plant-based raw materials for animal feed, including sunflower meal. Following the optimization of a dry fractionation process in a previous study of the authors, this research aims to validate the defined parameters through the processing of three sunflower meals (SFM1, SFM2, and SFM3) with different characteristics. The dry fractionation process includes two-stage grinding using hammer mill and roll mill and fractionation of sunflower meal by sieving. The process successfully increased the protein content of sunflower meals in the range of 17.5% to 31.2%, reaching levels high enough to be categorized as “high protein” sunflower meals of first quality (42% as is). Exceptionally high fraction yields (76.5–78.9%) were obtained for all three sunflower meals. The lowest energy consumption was recorded for SFM1 (8.44 Wh/kg), while slightly higher values were observed during the processing of SFM2 and SFM3 (9.30 and 9.93 Wh/kg, respectively). Relative amino acid enrichments ranging from 13.35% to 26.64% were achieved, with lysine enrichment ranging from 18.9% to 36% and methionine from 30.6% to 44.1%.

This study investigated the isolation and bioactive characterization of proteins obtained from insect flours of Tenebrio molitor, Zophobas morio, and Acheta domesticus. Protein isolates were produced from defatted insect flours using a modified alkaline extraction procedure, including extraction at pH 11, isoelectric precipitation at pH 4, and an additional purification step aimed at improving protein purity and isolate quality. The obtained protein isolates were characterized in terms of chemical composition, electrophoretic profile, solubility, water- and oil-holding capacities, amino acid composition, and antioxidant activity. All isolates exhibited notable antioxidant potential in the 2,2-azino-bis-3-ethylbenzothiazoline-6-sulfonic acid (ABTS) assay, indicating their ability to act as natural radical-scavenging compounds. In order to further evaluate their bioactive potential, the protein isolates were subjected to enzymatic hydrolysis using Alcalase. The obtained protein hydrolysates exhibited antimicrobial activity against both Escherichia coli and Staphylococcus epidermidis, whereas the corresponding protein isolates showed no antimicrobial activity under the applied conditions. Among the investigated samples, Zophobas morio hydrolysate showed the highest antioxidant potential and degree of hydrolysis, whereas Acheta domesticus hydrolysate demonstrated the strongest antibacterial activity. These findings highlight the potential of edible insect-derived proteins as sustainable sources of natural antioxidant and antimicrobial ingredients for future applications in the food, feed, pharmaceutical, and cosmetic industries.