The pulsed electric field (PEF) was applied to improve the extraction yield and properties of rice bran proteins from two rice varieties (“Kum Chao Mor Chor 107” and “Kum Doi Saket”). As compared to the conventional alkaline extraction, PEF treatment at 2.3 kV for 25 min increased the protein extraction efficiency by 20.71–22.8% (p < 0.05). The molecular weight distribution detected by SDS-PAGE and amino acid profiles of extracted rice bran proteins was likely unchanged. The PEF treatment influenced changes in the secondary structures of rice bran proteins, especially from the β-turn to the β-sheet structure. Functional properties of rice bran protein including oil holding capacity and emulsifying properties were significantly improved by PEF treatments by about 20.29–22.64% and 3.3–12.0% (p < 0.05), respectively. Foaming ability and foam stability increased by 1.8- to 2.9-fold. Moreover, the in vitro digestibility of protein was also enhanced, which was consistent with the increment of DPPH and ABTS radical-scavenging activities of peptides generated under in vitro gastrointestinal digestion (37.84–40.45% and 28.46–37.86%, respectively). In conclusion, the PEF process could be a novel technique for assisting the extraction and modification of the protein’s digestibility and functional properties.

Crickets contain high protein content that can be used to improve nutrition but are less exploited. This study was conducted to isolate different Cricket Protein Fractions including albumin, globulin, glutelin, and prolamin. All fractions were characterized and hydrolyzed by commercial enzymes. The results showed that the glutelin fractions had the highest extraction yields with 53.9 ± 2.12% (p < 0.05). Moreover, glutelin hydrolysate fraction prepared by Alcalase with a 16.35 ±0.29% hydrolysis degree was selected for further purification because of their high antioxidant activities, including ABTS radical-scavenging activity (0.44–0.55 µmol Trolox eq./g) and metal chelating activity (1721.99–1751.71 µmol EDTA eq./g). Two active fractions, GA-1 (<3 kDa) and GA-2 (<3 kDa), were collected from the consecutive purification of glutelin hydrolysates, which included processes such as membrane ultrafiltration and gel filtration. The fractions were analyzed by LC-MS/MS to obtain 10 peptides with 3–13 amino acids identified as TEAPLNPK, EVGA, KLL, TGNLPGAAHPLLL, AHLLT, LSPLYE, AGVL, VAAV, VAGL, and QLL with a molecular weight range of 359.23–721.37 Da in the two fractions. The amino acid sequence shows a prevalence of hydrophobic amino acids (50–100%) such as valine and leucine in the peptide chains, accounting for its high antioxidant activity. In conclusion, cricket glutelin hydrolysate prepared by Alcalase can serve as an alternative source of potent edible bioactive peptides in functional food products.

The global plant-based protein demand is rapidly expanding in line with the increase in the world’s population. In this study, ultrasonic-assisted extraction (UAE) was applied to extract protein from Wolffia globosa as an alternative source. Enzymatic hydrolysis was used to modify the protein properties for extended use as a functional ingredient. The successful optimal conditions for protein extraction included a liquid to solid ratio of 30 mL/g, 25 min of extraction time, and a 78% sonication amplitude, providing a higher protein extraction yield than alkaline extraction by about 2.17-fold. The derived protein was rich in essential amino acids, including leucine, valine, and phenylalanine. Protamex and Alcalase were used to prepare protein hydrolysates with different degrees of hydrolysis, producing protein fragments with molecular weights ranging between <10 and 61.5 kDa. Enzymatic hydrolysis caused the secondary structural transformations of proteins from β-sheets and random coils to α-helix and β-turn structures. Moreover, it influenced the protein functional properties, particularly enhancing the protein solubility and emulsifying activity. Partial hydrolysis (DH3%) improved the foaming properties of proteins; meanwhile, an excess hydrolysis degree reduced the emulsifying stability and oil-binding capacity. The produced protein hydrolysates showed potential as anti-cancer peptides on human ovarian cancer cell lines.

Moringa oleifera seeds are rich in protein, yet their potential as plant-based protein in food remains underutilized. This study evaluated the extraction efficiency, composition, and techno-functional properties of moringa seed protein isolate (MSPI) using enzyme-assisted (EAE), ultrasonic-assisted (UAE), and microwave-assisted extraction (MAE) methods, compared to conventional alkaline extraction (CE). EAE was performed with viscozyme (2%, pH 8, 50 °C, 2 h) and papain (1%, pH 7, 50 °C, 1 h), UAE at 40% amplitude (20 kHz, 20 min), and MAE at 800 W (50 °C, 90 s). All methods significantly improved extraction yield (14.60–30.08%), protein content (80.47–86.61%), solubility (40.78–60.09% at pH 10), and techno-functional properties over CE. However, MAE slightly reduced solubility. Phytates (0.83–0.49 g/100 g) and trypsin inhibitor activity significantly decreased (4.48–1.92 U/mg). In vitro protein digestibility improved (p < 0.05) across all samples (88.11–93.81%), with hydrolysis patterns supporting the enhanced digestibility. Structural modifications were indicated by altered surface hydrophobicity and thermal properties. SDS-PAGE showed consistent major protein bands at 17, 25, and 48–63 kDa, with EAE showing reduced intensity at ~63 kDa. While UAE and MAE achieved high protein yield and purity, EAE offered the best balance of functionality and digestibility, making it the most promising method for producing high-quality MSPI. These findings are relevant for guiding the selection of extraction methods for MSPI recovery for food applications.

The rising protein demand has driven intensified research into alternative protein sources and extraction technologies. Brewer’s spent grain (BSG), which is rich in protein, remains mostly underutilized. This study aimed to optimize BSG protein extraction conditions using pulsed electric field (PEF) by assessing the influence of pulse numbers (5000–9000), electric field strength (8–10 kV/cm), and frequency (8–10 Hz) on protein recovery and purity. The optimized conditions (5386 pulses, 10 kV/cm field strength, and 10 Hz frequency) provided a higher extraction yield with a significant improvement of approximately 90% (p < 0.05). Essential amino acids in proteins extracted via PEF were significantly increased (60,864.84 mg/100 g), particularly phenylalanine, threonine, and valine; furthermore, amino acid score (AAS) and protein digestibility-corrected amino acid score (PDCAAS) were found to be superior to those of protein obtained through alkaline extraction. The PEF treatment resulted in the modification of the secondary structures of proteins from α-helices and β-turns to β-sheets, as well as the enhancement of the hydrophobic−hydrophilic amino acid balance. The functional properties of the proteins, particularly their foaming properties and solubility, were significantly affected by PEF (p < 0.05). In conclusion, PEF-assisted extraction produces high-quality BSG protein concentrates efficiently while rendering the process environmentally sustainable.

To obtain oil from bee brood, which was dried using a tray drying method, this study used the supercritical CO₂ extraction method. Extraction occurred at temperatures between 40–60 °C and low pressures of 180–220 bar for 1.5 h, with a high pressure of 600 bar for 1 h. The study investigated both the yield and chemical properties of the extracted bee brood oils. Supercritical CO₂ extraction of tray-dried bee brood at 600 bar pressure demonstrated higher oil extraction efficiency compared to lower pressures (180–220 bar). At temperatures of 40–60 °C, total phenolic compounds increased while total flavonoids decreased. The extracted oil exhibited antioxidant activity, primarily due to quercetin. Despite decreased acid, iodine, and saponification values, peroxide value slightly increased but remained below 12 meqO₂/kg of oil. The make-up of the fatty acids changed. At 600 bar, palmitic and oleic acids were the most common, while myristic, linoleic, and docosadienoic acids decreased. At 600 bar, eicosadienoic acid was absent. The defatted bee brood retained significant essential and non-essential amino acids, indicating its potential for further development as a protein source.