This study mainly investigated the effect of soy protein isolate (SPI) on the gel quality of silver carp surimi under different storage conditions (storage temperatures of 4 °C, -20 °C, and -40 °C, and storage times of 0, 15, and 30 d). The results found that 10% SPI could inhibit the growth of ice crystals, improve the water distribution, enhance the water holding capacity of the gels, and strengthen the interaction between surimi and proteins. Compared to the control group, the composite silver carp surimi gel exhibited superior quality in texture, chemical interactions, and rheological properties during cold storage. Fourier transform infrared spectroscopy revealed an increasing trend in α-helix and β-turn content and a decreasing trend of β-sheet and random coil content. As storage time increased, the gel deterioration during cold storage inhibitory effect of the treatment group was superior to the control group, with the best results observed at -40 °C storage conditions. Overall, SPI was a good choice for maintaining the quality of silver carp surimi gel during cold storage, which could significantly reduce the changes in the textural properties during cold storage with improved water holding capacity.

In this study, soy protein isolate (SPI) films incorporating quercetin-grafted dialdehyde starch (DAS-QR) and DAS/QR, respectively, were developed. The structural, physical, and functional properties of the composite films were determined. The results suggested that DAS-QR and DAS/QR formed hydrogen bonding with the SPI matrix, which improved the structural properties of the films. The light-blocking capacity, thermal stability, hydrophobicity, tensile strength, elongation at break, and antioxidant and antibacterial abilities of SPI films were improved by DAS-QR and DAS/QR. Notably, SPI films incorporated with DAS-QR exhibited better performance than those with DAS/QR in terms of antioxidant (SPI/DAS-QR: 79.8% of DPPH and 62.1% of ABTS scavenging activity; SPI/DAS/QR: 71.4% of DPPH and 56.0% of ABTS scavenging activity) and antibacterial abilities against S. aureus (inhibition rate: 92.7% for SPI/DAS-QR, 83.4% for SPI/DAS/QR). The composite coating film SPI/DAS-QR effectively maintained appearance quality, delayed the loss of weight and total soluble solids, postponed malondialdehyde accumulation, and decreased peroxidase activity and microbial contamination in fresh-cut potatoes. These good performances highlight SPI/DAS-QR as a promising active packaging material for fresh-cut product preservation.

The present study aimed to investigate the properties of calcium-rich soy protein isolate (SPI) gels (14% SPI; 100 mM CaCl2), the effects of incorporating different concentrations locust bean gum (LBG) (0.1-0.3%, w/v) to the systems and the stability of the obtained gels. Also, the incorporation of solid lipid microparticles (SLMs) was tested as an alternative strategy to improve the system\'s stability and, therefore, potential to be applied as a product prototype. The gels were evaluated regarding their visual aspect, rheological properties, water-holding capacities (WHCs) and microstructural organizations. The CaCl2-induced gels were self-supported but presented low WHC (40.0% ± 2.2) which was improved by LBG incorporation. The obtained mixed system, however, presented low stability, with high syneresis after 10 days of storage, due to microstructural compaction. The gels\' stability was improved by SLM incorporation, which decreased the gelled matrices\' compaction and syneresis for more than 20 days. Even though the rheological properties of the emulsion-filled gels (EFGs) were very altered due to the ageing process (which may affect the sensory perception of a future food originated from this EFG), the incorporation of SLMs increased the systems potential to be applied as a calcium-rich product prototype.

In this study, an active biofilm was developed by incorporating red dragon fruit peel (RDF) extract into soy protein isolate (SPI) film matrix for sustainable food packaging. The addition of betalain-rich-RDF extract (1-7 wt%) significantly improved UV-blocking and antioxidant properties of the film compared to the control film. As wt% of RDF-extract increased, water vapor permeability, water solubility, and elongation at break decreased by 1.06 × 10-10 g m m-2 s-1 Pa-1, 34.25%, and 133.25%, respectively. On the other hand, Tensile strength increased significantly (P < 0.05) by 78.76%. FTIR results confirmed the intermolecular interaction between RDF extract and SPI through hydrogen bonding, while XRD result showed a decrease in the crystallinity degree of the film with RDF extract addition. However, no significant change in the TGA curve between extract-incorporated SPI films was observed. SEM analysis revealed that SPI B and SPI D films had a more compact and denser structure than the control film, while AFM analysis showed an increase in Ra and Rq values representing higher surface roughness of SPI D film. SPI D film also significantly (P < 0.05) decreased the weight loss and increased total soluble solids of freshly cut apples over 7-day storage period.
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UNASSIGNED: The online version contains supplementary material available at 10.1007/s13197-024-05940-2.

This study aimed to modify plant protein mixture to improve their functionality and digestibility by limited hydrolysis. Soy protein isolate and corn zein were mixed at the ratio of 5:1 (w/w), followed by limited hydrolysis using papain from 15 to 30 min. The structural characteristics, in vitro digestibility, and functional properties were evaluated. Also, DPPH radical scavenging activity was determined. The results indicated that the molecular weight of different modified samples was largely reduced by limited hydrolysis, and the proportion of random coil was significantly increased. Furthermore, the solubility, foaming, emulsifying and water-holding capacity of hydrolyzed protein mixture were significantly improved, which were close to those of whey protein isolate. In vitro digestibility after 30-min limited hydrolysis was remarkably elevated. In addition, the hydrolyzed protein mixture exhibited a higher antioxidant activity than those of untreated proteins. Overall, limited hydrolysis of protein mixture led to improved digestibility, functionality and antioxidant activity.

This study aimed to investigate the effects of ultrasonic treatment at different powers on the physicochemical properties, microstructure and quercetin delivery capacity of fermentation-induced soy protein isolate emulsion gel (FSEG). The FSEG was prepared by subjecting soy protein isolate (SPI) emulsion to ultrasonic treatment at various powers (0, 100, 200, 300, and 400 W), followed by lactic acid bacteria fermentation. Compared with the control group (0 W), the FSEG treated with ultrasound had higher hardness, water holding capacity (WHC) and rheological parameters. Particularly, at an ultrasonic power of 300 W, the FSEG had the highest hardness (101.69 ± 4.67 g) and WHC (75.20 ± 1.07%) (p < 0.05). Analysis of frequency sweep and strain scanning revealed that the storage modulus (G\') and yield strains of FSEG increased after 300 W ultrasonic treatment. Additionally, the recovery rate after creep recovery test significantly increased from 18.70 ± 0.49% (0 W) to 58.05 ± 0.54% (300 W) (p < 0.05). Ultrasound treatment also resulted in an increased β-sheet content and the formation of a more compact micro-network structure. This led to a more uniform distribution of oil droplets and reduced mobility of water within the gel. Moreover, ultrasonic treatment significantly enhanced the encapsulation efficiency of quercetin in FSEG from 81.25 ± 0.62 % (0 W) to 90.04 ± 1.54% (300 W). The bioaccessibility of quercetin also increased significantly from 28.90 ± 0.40% (0 W) to 42.58 ± 1.60% (300 W) (p < 0.05). This study enriches the induction method of soy protein emulsion gels and provides some references for the preparation of fermented emulsion gels loaded with active substances.

Oil bodies (OBs) are naturally occurring pre-emulsified oil droplets that have broad application prospects in emulsions and gels. The main purpose of this research was to examine the impact of the OB content on the structure and functional aspects of acid-mediated soy protein isolate (SPI) gel filled with OBs. The results indicated that the peanut oil body (POBs) content significantly affected the water holding capacity of the gel. The rheological and textural analyses showed that POBs reduced the gel strength and hardness. The scanning electron and confocal laser scanning microscopy analyses revealed that POBs aggregated during gel formation and reduced the gel network density. The Fourier transform infrared spectrum (FTIR) analysis demonstrated that POBs participated in protein gels through hydrogen bonds, steric hindrance and hydrophobic interactions. Therefore, OBs served as inactive filler in the acid-mediated protein gel, replaced traditional oils and provided alternative ingredients for the development of new emulsion-filled gels.

In this study, a novel and simple strategy is proposed based on 3D network formed by easily blending polysaccharide carrageenan (Car) and fucoidan (Fuc) without a crosslinker. The Fuc/Car dual coating effectively assists the self-assembly of soy protein-isolated (SPI)/curcumin (Cur, C) composite microcapsules (SPI/C) and achieves an excellent curcumin encapsulation efficiency (EE) up to 95.28% with a 4.16% loading capacity (LC) under optimal conditions. The resulting nanocomposites achieved a satisfying redispersibility in aqueous solution and enhanced the water solubility with a lower size dispersity index (PDI) of 0.12 and a larger zeta potential of -29.67 mV. The Fuc/Car double-layer network not only dramatically improved its thermal stability and photostability, but also provided controlled release and enhanced antioxidant activity in in vitro conditions. The underlying mechanism of the self-assembly of the curcumin-loaded nanoparticles was also addressed. The results proved the feasibility of the encapsulation of unstable hydrophobic bioactive substances (curcumin) with the dual anionic polysaccharide Fuc/Car co-stabilized SPI nanoparticles. This study paves the way for an alternative way of developing novel curcumin delivery systems and will have broad prospects in the pharmaceutical industries.

Using parameters of optimal conditions from laboratory experiments often results in the loss of significant time and resources when trying to scale up the process. In this study, the comparison of results of laboratory and semi-industrial experiments of enzymatic hydrolysis of soy protein isolate is considered. The kinetics of peptides accumulation was investigated by colorimetric method in both microtube (volume reaction is 0.7 ml, 7.14 mg/ml of substrate, incubation in solid state thermostat) and industrial homogenizer (volume reaction is 4,000 ml, 100 mg/ml of substrate, rotor-stator type mixer). The enzyme preparation Protosubtilin G3x (main component is subtilisin) was used as an analogue of the Alcalase preparation, which is already widely used in the food industry. It was found that the pH and the number of proteolytic units in the reaction mixture of both scales had slightly different results of the kinetics, while the temperature showed significantly one. The laboratory scale of the reaction had a wide range of optimal temperature (40-60  ∘ C, 30  ∘ C showed slowest rate of kinetics reaction), whereas the semi-industrial scale had 50  ∘ C of optimal temperature (30, 40, 60  ∘ C had the same kinetics). It also was found that maintaining the pH value of the reaction mixture was not mandatory. The obtained results indicate the need to refine the process conditions using semi-industrial experiments before attracting industrial-scale resources. In the case of selection of conditions for the hydrolysis of soy protein isolate in production, it is necessary first of all to take into account the reaction temperature as the most irreproducible parameter when scaling.

The present study aimed to investigate the functional properties of soybean protein isolate (SPI) treated with alkaline protease and high-speed shearing homogenization. Alkaline protease-hydrolyzed SPIs that were characterized by varying degrees of hydrolysis between 0 and 6% were treated with high-speed shearing homogenization to obtain different micro-particulate proteins. The results showed that this combined treatment could significantly reduce the particle size of SPI by markedly degrading the structure of both the 7S and 11S subunits, thereby resulting in a significantly reduced content of β-sheet and β-turn structures. The surface hydrophobicity increased considerably for samples with hydrolysis below the threshold of 2% and then declined gradually above this threshold. Furthermore, the combination of hydrolysis and homogenization significantly improved the emulsion stability of SPI hydrolysates. It also significantly improved the foaming properties of SPI. These results demonstrated that alkaline protease hydrolysis combined with high-speed shearing homogenization represents a promising approach for improving the functional and structural properties of SPI.