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The functional characteristics of Partial acylglycerols (PAGs) have attracted the attention of researchers in designing PAGs for food applications as a potential substitute for conventional fats/oils. Designing PA using enzymes has been of great interest due to the greater specificity of enzymes, giving high-quality products for food applications. The utilization of PA in fat-based products, such as bakery, dairy, and emulsion foods, exhibits superior functionalities and health-friendly characteristics. The PA can also be used for cooking/frying applications. However, exposure of PA to a higher temperature for a longer time shows inferior characteristics. The functional characteristics of PA, such as solid fat content, rheology, microstructure, crystal formation, and thermal behavior, make it a potential replacement for conventional fat. The present review focuses on a comparative assessment of synthetic routes, the functional characteristics of PA, food applications, and technological drawbacks in commercializing PA-based products. Furthermore, the future prospect focuses on supporting future research that will facilitate the incorporation of PA in food products at an industrial scale.

Dairy and plant-based proteins are widely utilized in various food applications. Several techniques have been employed to improve the techno-functional properties of these proteins. Among them, pulsed electric field (PEF) technology has recently attracted considerable attention as a green technology to enhance the functional properties of food proteins. In this review, we briefly explain the fundamentals of PEF devices, their components, and pulse generation and discuss the impacts of PEF treatment on the structure of dairy and plant proteins. In addition, we cover the PEF-induced changes in the techno-functional properties of proteins (including solubility, gelling, emulsifying, and foaming properties). In this work, we also discuss the main challenges and the possible future trends of PEF applications in the food proteins industry. PEF treatments at high strengths could change the structure of proteins. The PEF treatment conditions markedly affect the treatment results with respect to proteins’ structure and techno-functional properties. Moreover, increasing the electric field strength could enhance the emulsifying properties of proteins and protein-polysaccharide complexes. However, more research and academia–industry collaboration are recommended to build highly effective PEF devices with controlled processing conditions.

The identification of multifunctional peptides derived from marine byproducts represents a significant challenge in the field. In Thailand, the fisheries industry exports salted jellyfish, which results in low-value byproducts primarily employed for animal feed. Previous studies have indicated the bioactivities of jellyfish protein hydrolysates from Lobonema smitthii ; however, the multifunctional properties of Rhopilema hispidum remain largely unexplored. This research aimed to characterize synthetic bioactive peptides sourced from the byproducts of salted jellyfish ( R. hispidum ), with a specific emphasis on their antioxidant, angiotensin-I-converting enzyme (ACE) inhibitory, and anti-inflammatory activities. The hydrolysate obtained from the umbrella portion, subjected to pepsin treatment at a 3:20 enzyme-to-substrate ratio for 48 h at 37 °C, demonstrated the highest levels of antioxidant activity (DPPH =  1.85 ± 0.05 mM TE/mg protein, ABTS =  7.28 ± 0.03 mM TE/mg protein, FRAP =  3.04 ± 0.12 mM FeSO 4 /mg protein). Following purification, 18 novel peptides exhibiting high antioxidant scores (FRS+CHEL >  0.48) were identified and synthesized. Notably, the peptide MVVACVLPEA exhibited significant antioxidant (DPPH =  56.07 mM TE/mg protein), ACE inhibitory (91.69%), and anti-inflammatory activities (NO release =  34.59 µ M) without cytotoxic effects, although it is important to note that two other peptides did demonstrate cytotoxicity. This investigation reports a total of 16 synthesized peptides that possess triple functional activities—antioxidant, ACE inhibitory, and anti-inflammatory—without cytotoxicity, thus highlighting their potential applications in health-related fields.

Achieving sustainability in the agro-food sector can only be possible with the valorization of food industry waste and side streams, products with an extremely high intrinsic value but often discarded because they are unfit for further processing that meets consumer expectations [...]

This study explored how combining supercritical fluid extraction (SFE) and enzymatic hydrolysis influences the structure and functionality of peptides recovered from filter-pressed shrimp waste. Freeze-dried press cake (PC) was defatted via SFE and hydrolyzed using Alcalase (ALC) and trypsin (TRYP). ALC-treated PC achieved the highest protein recovery (63.49%), extraction yield (24.73%), and hydrolysis degree (18.10%) (p < 0.05). SFE-treated hydrolysates showed higher zeta potential (−47.23 to −49.93 mV) than non-SFE samples (−25.15 to −38.62 mV) but had larger droplet sizes, indicating lower emulsion stability. SC-ALC displayed reduced fluorescence intensity and a red shift in maximum wavelength. TRYP hydrolysates reduced interfacial tension (20 mN/m), similar to sodium caseinate (Na-Cas, 13 mN/m), but with lesser effects. Dilatational rheology showed TRYP hydrolysates formed stronger, solid-like structures. These results emphasize protease efficacy over SFE for extracting functional compounds, enhancing shrimp waste valorization.

Portable single-sided nuclear magnetic resonance (NMR) magnets used for nondestructive studies of large samples are believed to generate inherently inhomogeneous magnetic fields. We demonstrated experimentally that the field of an open magnet can be shimmed to high homogeneity in a large volume external to the sensor. This technique allowed us to measure localized high-resolution proton spectra outside a portable open magnet with a spectral resolution of 0.25 part per million. The generation of these experimental conditions also simplifies the implementation of such powerful methodologies as multidimensional NMR spectroscopy and imaging.

This study investigated the synergistic effects of three protein concentrates from legumes (pea, lentil, and lima bean) as emulsifiers and stabilizers of oil-in-water (O/W) emulsions using a simplex-centroid mixture design. The aim was to check whether proteins combined in different proportions have better emulsifying properties than isolated proteins. During this study, each protein concentrate was characterized by different evaluated parameters: emulsifying activity, emulsion stability, accelerated stability test, thermal coagulation time, stability to coalescence, and others. After statistical analysis mixture optimization, it was found that the best formulation for stabilizing O/W emulsion under the tested conditions (2% total protein; 3% sunflower oil) was the protein blend containing 21.21% pea, 32.78% lentil, and 46.01% fava bean. This blend exhibited better emulsification properties compared to the individual proteins.

Pereskia aculeata Miller is an edible plant species belonging to the Cactaceae family. It has the potential to be used in the food and pharmaceutical industries due to its nutritional characteristics, bioactive compounds, and mucilage content. Pereskia aculeata Miller is native to the Neotropical region, where it is traditionally employed as food in rural communities, being popularly known as ‘ora-pro-nobis’ (OPN) or the Barbados gooseberry. The leaves of OPN are distinguished by their nontoxicity and nutritional richness, including, on a dry basis, 23% proteins, 31% carbohydrates, 14% minerals, 8% lipids, and 4% soluble dietary fibers, besides vitamins A, C, and E, and phenolic, carotenoid, and flavonoid compounds. The OPN leaves and fruits also contain mucilage composed of arabinogalactan biopolymer that presents technofunctional properties such as thickener, gelling, and emulsifier agent. Moreover, OPN is generally used for pharmacological purposes in Brazilian folk medicine, which has been attributed to its bioactive molecules with metabolic, anti-inflammatory, antioxidant, and antimicrobial properties. Therefore, in the face of the growing research and industrial interests in OPN as a novel food source, the present work reviews its botanical, nutritional, bioactive, and technofunctional properties, which are relevant for the development of healthy and innovative food products and ingredients.

Due to its excellent biocompatibility and ease of biodegradation, jellyfish gelatin has gained attention as a hydrogel. However, hydrogel produced from jellyfish gelatin has not yet been sufficiently characterized. Therefore, this research aims to produce a jellyfish gelatin-based hydrogel. The gelatin produced from desalted jellyfish by-products varied with the part of the specimen and extraction time. Hydrogels with gelatin: glutaraldehyde ratios of 10:0.25, 10:0.50, and 10:1.00 (v/v) were characterized, and their cefazolin release ability was determined. The optimal conditions for gelatin extraction and chosen for the development of jellyfish hydrogels (JGel) included the use of the umbrella part of desalted jellyfish by-products extracted for 24 h (WU24), which yielded the highest gel strength (460.02 g), viscosity (24.45 cP), gelling temperature (12.70 °C), and melting temperature (22.48 °C). The quantities of collagen alpha−1(XXVIII) chain A, collagen alpha−1(XXI) chain, and collagen alpha−2(IX) chain in WU24 may influence its gel properties. Increasing the glutaraldehyde content in JGel increased the gel fraction by decreasing the space between the protein chains and gel swelling, as glutaraldehyde binds with lateral amino acid residues and produces a stronger network. At 8 h, more than 80% of the cefazolin in JGel (10:0.25) was released, which was higher than that released from bovine hydrogel (52.81%) and fish hydrogel (54.04%). This research is the first report focused on the production of JGel using glutaraldehyde as a cross-linking agent.

This study investigated the extraction and colloidal properties of pea protein isolates (PPIs) from four pea cultivars produced in a southern region in Italy. The control PPIs (C-PPIs) were obtained via an alkaline extraction and isoelectric precipitation method and then subjected to ultrasound treatment (US) to yield US-PPIs. The effects of cultivars and sonication on the physicochemical characteristics and emulsifying property of the PPIs were studied. Fourier-transform infrared (FTIR) spectroscopy, colorimetric measurement, dynamic light scattering (DLS), and confocal laser scanning microscopy (CLSM) were applied to characterize the samples. DLS results showed that C-PPIs displayed smaller particle sizes (8.86–15.9 µm) in comparison to US-PPIs (15.8–66.5 µm). DSC data showed that US-PPIs had improved thermal stability compared to control PPIs. FTIR analysis detected differences in the protein secondary structure of the various cultivars and between the native and US-PPIs. Emulsion stability studies indicated that emulsions stabilized with C-PPIs exhibited lower droplet sizes, implying improved stability in comparison to emulsions stabilized with US-PPIs. In conclusion, PPIs can be successfully extracted from different cultivars and applied as a natural emulsifier.