Advances in synthesis and applications of epitope-imprinted polymers (EIPs) for protein recognition and separation.

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 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.

Barley malt residue (BMR) was subjected to microwave-assisted enzymatic hydrolysis to evaluate its potential as a raw material to produce xylooligosaccharides (XOS) suitable for use as a prebiotic. The influent factors on XOS production, microwave power, exposure time, and xylanase dosage were ascertained with response surface methodology based on Box–Behnken design (BBD). The fitted models of XOS and xylose yields were in good agreement with the experimental results. Using a microwave power of 1235.1 W, a 6 min exposure time, and a xylanase concentration of 89.12 U/g substrate gave the highest yield of XOS: 208.05 mg/g substrate at 4 h of enzyme incubation time. Based on the product composition, BMR-XOS purification by Saccharomyces cerevisiae treatment was superior to the process of activated carbon adsorption and ethanol precipitation treatment and was selected for further experiments. Thin-Layer Chromatography (TLC) and high-performance liquid chromatography (HPLC) clearly elucidated the oligosaccharide compositions, and the result of Fourier Transform Infrared Spectroscopy (FTIR) confirms the molecular structure and sugar components of achieved BMR-XOS. In vitro fermentation of BMR-XOS obtained from this study by the selected probiotics, Lactococcus lactis TISTR 1401, Levicaseibacillus brevis FS 2.1, Lactobacillus casei TISTR 1463, showed similar prebiotic activity compared with the commercial XOS, galactooligosaccharides (GOS), xylose, and glucose (control). In conclusion, the present study was successful in establishing the use of barley malt residue for the extraction of xylan and XOS, which could be further used as a prebiotic.

This study evaluated the effectiveness of photodynamic treatment (PDT) using riboflavin (Rbf) and blue light-emitting diode (BL) irradiation for microbial inactivation and quality preservation in fresh betel leaves (Piper betle L.). Non-pathogenic surrogates Escherichia coli K-12 and Listeria innocua were used to model Gram-negative and Gram-positive bacteria. The combined Rbf-BL treatment significantly reduced microbial populations by up to 5.3 log CFU/g for E. coli and 6.2 log CFU/g for L. innocua on leaf surfaces (p < 0.05) and 1.3–1.5 log CFU/mL in broth cultures. Treated samples showed significantly higher total soluble solids (12.0 ± 0.0 °Brix), total phenolic content (0.17 ± 0.02 mmol GAE/g, p < 0.05), and antioxidant activity (62.0 ± 3.1% DPPH inhibition, p < 0.05), with minimal color alteration after treatment (ΔE = 4.68). The total fluence measured at the leaf surface was approximately 11.72 J/cm². As a mild thermal treatment utilizing a GRAS photosensitizer, riboflavin-assisted PDT presents a promising strategy for enhancing microbial safety and promoting phytochemical quality in betel leaves.