BACKGROUND: Gluten-free bread (GFB) has technical bottlenecks such as hard texture, rough taste and low nutrition in practical production. In order to solve these problems, this study used germinated brown rice starch as the main raw material, and investigated the effects of soybean isolate protein (SPI) on the multiscale structure of germinated brown rice starch and bread quality.
RESULTS: A gluten-free rice bread process simulation system was established, and the interaction between SPI and starch in the simulation system was characterized. The result shows that the interaction forces between SPI and germinated brown rice starch were mainly represented by hydrogen bonds, and with the addition of SPI, the crystallinity of starch showed a downward trend. At the same time, when the amount of SPI was 3%, the appearance quality was the best and the specific volume of bread was 1.08 mL g-1. When the amount of SPI was 6%, the texture quality was the best. Compared with the bread without SPI, the hardness of the bread with 6% SPI was reduced by 0.13 times, the springiness was increased by 0.03 times, the color was the most vibrant, the L* value being 1.02 times the original, and the baking loss was reduced to 0.98 times the original.
CONCLUSIONS: The interaction force between SPI and germinated brown rice starch and its effect on bread quality were clarified, and these results inform choices about providing a theoretical basis for the subsequent development of higher-quality GFB. © 2024 Society of Chemical Industry.

This study assessed the effect of konjac glucomannan (KGM) on the aggregation of soy protein isolate (SPI) and its gel-related structure and properties. Raman results showed that KGM promoted the rearrangement of SPI to form more β-sheets, contributing to the formation of an ordered structure. Atomic force microscopy, confocal laser scanning microscopy, and small-angle X-ray scattering results indicated that KGM reduced the size of SPI particles, narrowed their size distribution, and loosened the large aggregates formed by the stacking of SPI particles, improving the uniformity of gel system. As the hydrogen bonding between the KGM and SPI molecules enhanced, a well-developed network structure was obtained, further reducing the immobilized water\'s content (T22) and increasing the water-holding capacity (WHC) of SPI gel. Furthermore, this gel structure showed improved gel hardness and resistance to both small and large deformations. These findings facilitate the design and production of SPI-based gels with desired performance.

In recent years, oleogel as a viscoelastic semi-solid to replace trans fatty acids and reduce saturated fatty acids in food has received more and more attention. Herein, an emulsion template method was used to produce soybean oil-based oleogels with seven different ester emulsifiers and soy protein isolate as oleogelators. The chemical and physical characteristics of oleogels produced via various crosslinking factors were comparatively examined. Results revealed that all oleogels generated β-type needle crystals and exhibited high oil-holding capacity (>80 %), among which glycerol monolaurate G2 and diacetyl tartaric acid ester of mono-diglycerides G6 exhibited the strongest oil-holding capacity (96.6 % and 96.2 %, respectively). Furthermore, all oleogels exhibited strong thixotropic recovery, high thermal stability, as well as high gel strength (G\' > G\'\'). Of these, G2 and G6 exhibited the highest thixotropic recovery rates at 74.54 % and 78.19 %, respectively. Additionally, in accelerated oxidation trials, the peroxide value and thiobarbituric acid reactive substances of all oleogels had low oxidation rates, indicating high oxidative stability. These results contribute to a better understanding of oleogels for formulating trans-free and low-saturated foodstuffs with desired physical and functional properties.

This study was conducted to formulate a conjugate of soy protein isolate (SPI) and peach gum (PG) with improved functional properties, interacting at mass ratios of 1:1, 1:2, 1:3, 2:1, and 2:3 by Maillard reaction via wet heating method. Conjugation efficiency was confirmed by grafting degree (DG) and browning index (BI). Results indicated that DG increased with increasing concentration of PG, and decreased with increasing pH, whereas no remarkable change was observed with increasing reaction time. The conjugates were optimized at a ratio of 1:3. SDS-PAGE confirmed conjugate formation, Fourier transform infrared spectroscopy (FTIR) and circular dichroism (CD) verified conjugate secondary structural changes, and scanning electron microscopy (SEM) indicated significant overall structural changes. The functional properties, solubility, emulsifying stability, water holding, foaming, and antioxidant activity were significantly improved. This study revealed the wet heating method as an effective approach to improve the functional properties of soy protein.

This study aimed to prepare soy protein isolate-xanthan gum complexes (SPI-XG) at pH 7.0 and as emulsifiers to prepare Pickering emulsions for delivering quercetin (Que). The results showed that SPI-XG exhibited a gel network structure in which protein particles were embedded. Fourier transform infrared spectroscopy (FTIR) and molecular docking elucidated that SPI-XG formed through hydrogen bonding, hydrophobic, and electrostatic interactions. Three-phase contact angle (θo/w) of SPI-XG approached 90° with biphasic wettability. SPI-XG adsorbed at the oil-water interface to form an interfacial layer with a gel network structure, which prevented droplet aggregation. Following in vitro simulated digestion, Que displayed higher bioaccessibility in SPI-XG stabilized Pickering emulsions (SPI-XG PEs) than SPI stabilized Pickering emulsions. In conclusion, SPI-XG PEs were a promising system for Que delivery.

This study primarily investigated the improvement of high-dose Epigallocatechin-3-Gallate (EGCG)-induced deterioration of MP gel by soy protein isolate (SPI) addition. The results showed that EGCG could interact with MP, SPI, and HSPI (heated), indicating the competitive ability of SPI/HSPI against EGCG with MP. EGCG was encapsulated by SPI/HSPI with high encapsulation efficiency and antioxidation, with antioxidant activities of 78.5% ∼ 79.2%. FTIR and molecular docking results revealed that MP, SPI, and HSPI interacted with EGCG through hydrogen bonding and hydrophobic interactions. SPI/HSPI competed with MP for EGCG, leading to the restoration of MHC and Actin bands, alleviating the aggregation caused by EGCG and oxidation. Additionally, SPI/HSPI-E significantly reduced the high cooking loss (23.71 and 26.65%) and gel strength (13.60 and 17.02%) induced by EGCG. Hence, SPI competed with MP for EGCG binding site to ameliorate MP gel properties, thereby alleviating the detrimental changes in MP caused by high-dose EGCG and oxidation.

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.

With an increasing emphasis on health and environmental consciousness, there is a growing inclination toward plant protein-based meat substitutes as viable alternatives to animal meat. In the pursuit of creating diverse and functional plant protein-based substitutes, innovative plant proteins have been introduced in conjunction with soy protein isolate (SPI), encompassing pea protein isolate (PPI), rice bran protein (RBP), fava bean protein isolate (FPI), and spirulina protein isolate (SPPI). Notably, SPI-WG extrudates and SPI-PPI extrudates exhibited superior fiber structures (fiber degrees were 1.72 and 1.88, respectively), with coarse fibers in SPI-WG extrudates and fine, dense fibers in SPI-PPI extrudates. The addition of RBP, FPI and SPPI had minimal effect on fiber structure. Fresh SPI-FPI displayed the slowest rate of water loss, losing about 7.11% of their total weight in 5 h. Different plant proteins can be selected for the preparation of plant protein-based meat substitutes according to practical needs.

With the increasing demand for food foaming, how to enhance the foaming properties of protein has gradually become the research focus. This work studied the effect of synephrine (SY) on foaming properties, structure properties, and physicochemical properties of soybean protein isolate (SPI). When the mass ratio of SY to SPI was 1:2, compared with SPI alone, the foam capacity and foam stability of the SY-SPI complex were significantly enhanced. Optical microscopy and confocal laser scanning microscope showed that the improvement in foaming performance was mainly due to the reduction of bubble size and uniform protein distribution. Circular dichroism spectrum and fluorescence spectra indicated that the hydrogen bond of SPI was destroyed and blue shifted with the addition of SY. What\'s more, the absolute value of Zeta potential, solubility, and hydrophobicity all increased, while the particle size decreased. As a result of molecular docking, surface hydrogen bonds, Van der Waals forces and hydrophobic interactions are the main driving forces. The addition of SY and SPI improved the specific volume and texture of angel cake. This study shows that SY has the potential to be developed into a new type of blowing agent.

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.