This study investigated relationship between secondary structure and surface hydrophobicity of soy protein isolate (SPI) subjected to a thermal treatment at 70~90°C. Heat denaturation increased the surface hydrophobicity and surface hydrophobicity decreased as aggregate formed. Heat caused an increase in the relative amount ofα-helix structures and an overall decrease in the amount ofβ-sheet structures when compared with nontreated SPI. The relative amounts of secondary structures varied with time, temperature, and intensity of heat treatment applied. Theβ-sheet structure was most important for its significant role in denaturation of 7S globulin and following formed aggregates and even in denaturation of 11S globulin. The amount ofβ-sheet structure in SPI had an inverse correlation with the surface hydrophobicity when the temperature was kept below 90°C. Besides,β-turn structure increased asβ-7S/B-11S aggregate formated.

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Maillard reaction products (MRPs) of soybean protein isolate (SPI) and sugars (glucose and maltose) were prepared by heating in the aqueous dispersion at 95°C for 15 min with ultrasonic pretreatment (ultrasonic power of 200 W) for 20 min. Effect of ultrasonic pretreatment on physicochemical characteristics and rheological properties of SPI/sugar MRPs was investigated. SPI/sugar MRPs prepared with ultrasonic pretreatment had higher degree of glycation (DG), lower browning and less compact tertiary conformation than that with non-ultrasonic pretreatment. Surface hydrophobicity (H 0 ), particle size and rheological properties were measured by fluorescence spectrophotometry, laser particle size analysis and dynamic oscillatory rheometry, respectively. Glycation reduced H 0 and particle size as well as weaken the gel network formed by the acidification of GDL. However, ultrasound increased H 0 and decreased particle size. This is desirable for the formation of acid-induced gel structure. The ultrasonic pretreatments reduced/eliminate the weakening effect of glycation on the gel network of SPI/sugar MRPs, and even improved the gel properties.

Considering that a series of complex issues such as environmental problems, sustainable development, animal welfare, and human health are on a global scale, the development of vegetable protein‐based meat substitutes provides a potential solution to the disparity between meat consumption demand and supply. The research and development of vegetable protein‐based meat substitutes have become a major commercial activity, and the market is expanding to meet the growing consumer demand. Soy protein isolates (SPI) are often used as a raw material for vegetable meat substitutes because of their potential to form fiber structures. Although significant initial success has been achieved, it is still a challenge to explain how the composition and aggregation of SPI influence gel properties and the mechanism(s) involved. This article reviews the latest research about SPI. The relationship between the composition, aggregation, and gelation properties of SPI is based on a through literature search. It focused on the application of SPI in heat‐ and cold‐induced gels, given the diversified market demands. The research on cold gel has helped expand the market. The methods to improve the properties of SPI gels, including physical, chemical, and biological properties, are reviewed to provide insights on its role in the properties of SPI gels. To achieve environmentally friendly and efficient ways for the food industry to use SPI gel properties, the research prospects and development trends of the gel properties of SPI are summarized. New developments and practical applications in the production technology, such as for ultrasound, microwave and high pressure, are reviewed. The potential and challenges for practical applications of cold plasma technology for SPI gel properties are also discussed. There is a need to transfer the laboratory technology to actual food production efficiently and safely.

The objective of this study was to determine the functional and structural properties of Maillard reaction products of mung bean [Vigna radiate (L.)] protein isolate with dextran obtained under the temperature of 80°C or 90°C with different times (0, 1, 2, 3, 4, 5, and 6 h). The mung bean protein isolate-dextran conjugate had better solubility, emulsifying activity, and emulsifying stability than mung bean protein isolate; however, the protein aggregation decreased the solubility, surface hydrophobicity, emulsifying activity, and emulsifying stability of mung bean protein isolate-dextran conjugate. In general, these functional properties of mung bean protein isolate-dextran conjugate obtained at 80°C with lower degree of glycosylation and browning degree were better than mung bean protein isolatedextran conjugate obtained at 90°C. Both vicilin (8S) and legumin type (11S) globulins both participated in the graft reaction, the subunit with a molecular weight of 21 kDa that contributed to 11S globulin might be the most vulnerable to dextran followed by the 60, 32, and 26 kDa subunits. Maillard reaction between mung bean protein isolate and dextran led to a decreased fluorescence intensity and a bathochromic shift. The fluorescence intensity of mung bean protein isolate-dextran conjugate generally decreased, and λ max of mung bean protein isolate-dextran conjugate first increased and then decreased. The grafted mung bean protein isolates had lower α-helix content but higher β-sheet content. As the Maillard reaction between mung bean protein isolate and dextran proceeded, the α-helix contents of the mung bean protein isolate-dextran conjugates were significantly increased and then decreased, and the β-sheet content generally decreased and then increased. Excessive grafted dextran and more protein aggregation was observed in mung bean protein isolate-dextran conjugate obtained at 90°C, which induced structural changes that might have impaired the functions. Our findings suggest that conjugation of mung bean protein isolate with dextran through the Maillard reaction is an effective way of improving the functional properties of mung bean protein isolate for its application in the food industry. ARTICLE HISTORY

The structure and functionalities of rice bran protein (RBP) oxidized by peroxyl radicals were analyzed in this study. The thermal decomposition of 2,2′-azobis [2-amidinopropane] dihydrochloride (AAPH) was used to generate peroxyl radicals. Increased oxidation of RBP by AAPH gradually generated more carbonyl (COOH) groups, which resulted in a loss of protein sulfhydryl groups. Low oxidization (≤0.2 mmol/L AAPH) could cause structural unfolding with an increase in surface hydrophobicity and emulsion properties but reducing the solubility and disulfide bonding. Moderate and high oxidization (>0.2 mmol/L AAPH) could result in soluble aggregates formed by subunits with molecular weights of 53, 49, and 36 kDa, attributed to globulin, albumin, and glutelin, increasing the solubility and disulfide bonding but decreasing the surface hydrophobicity and emulsion stability. Oxidization by low concentration AAPH induced a more unordered structure and transformation from β-turn to β-sheets, while a more ordered structure increased with aggregation.

Ultrasound treatment and high-pressure homogenization were used to prepare soybean protein (SP)-phosphatidylcholine (PC) nanoemulsions in this study. Nanoemulsions prepared by high-pressure homogenization were more stable. The structural changes of SP and PC under ultrasound treatment and high-pressure homogenization treatment were investigated by Raman spectroscopy. It could be concluded that ultrasound and high-pressure homogenization treatments increased both the content of α-helix and unordered structure but decreased that of β-structures of SP, while the interaction between SP and PC decreased α-helix content and also reduced unordered structure and β-sheet structure. Ultrasound treatment and high-pressure homogenization exposed more tryptophan and tyrosine residues to promote hydrophobic interaction between SP and PC, which was beneficial for stabilizing the nanoemulsion. The SP-PC interaction exerted a more significant effect on side chain structure than those observed under ultrasound treatment and high-pressure homogenization. The dominant g-g-t vibrational mode of the disulfide bond of soybean protein was not appreciably changed by the two preparations. High-pressure homogenization increased the disorder of lipid chains of PC, promoting SP-PC interaction and thereby increasing the stability of the nanoemulsion. The structural change provided a theoretical basis for preparation of two nanoemulsions.