Optimal heat treatment of the soymilks is important to the production of tofu. In this study, soymilk with protein concentration of 40 mg/mL were heated at different temperatures for the fixed 50 s and were characterized by surface hydrophobicity, disulfide linked protein species determined by non-reducing SDS-PAGE and protein structural elements determined by the circular dichroism (CD). Tofu gels were prepared by acidifying the heated soymilks at 60 ℃ and 80 ℃ respectively and gelation time, gel mechanical properties as well as gel viscoelastic properties were determined by rheological analysis. The results showed that most soymilks' properties except surface hydrophobicity changed rapidly when heating temperature was higher than 80 ℃. Gelation time, storage modulus (G') at the end of acidifying and cooling processes as well as retardation time (λ) and recovery rate of tofu gels were affected by the heat treatments of soymilks. The distances between the standardized data describing heated soymilks and tofu gels respectively were calculated and compared. It was found that gelation time, G' and λ were most closely related to disulfide bond linked polymer, [CD] and surface hydrophobicity respectively. This study will provide useful information to the improvement of tofu processing.
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http://dx.doi.org/10.1016/j.foodres.2022.111912 | DOI Listing |
Food Res Int
February 2025
College of Food Science, Northeast Agricultural University, Harbin, Heilongjiang 150030, China.
A soybean protein isolate (SPI)-based hydrogel with controllable properties was prepared under mild conditions using a simple mixing method with dialdehyde sodium alginate (DSA) as an eco-friendly macromolecular crosslinker. DSA was successfully synthesized via periodate oxidation. Analysis of the structure of the SPI/DSA hydrogel indicated that a 3D network was formed between SPI and DSA through dynamic imine and hydrogen bonds.
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December 2024
College of Food Science, Fujian Agriculture and Forestry University, Fuzhou 350002, China.
Soy protein isolate (SPI) possesses potential gelling properties, making it suitable for gel-based applications. However, the gel network stability and mechanical properties of SPI are relatively poor and can be improved through modifications or by combining it with other polymers, such as Konjac Glucomannan (KGM). Combining SPI with KGM can overcome the poor gel network stability and mechanical properties of SPI, but it reduces the water-absorbing capacity of the gel network after drying, which affects the quality characteristics of plant-based protein rehydrated foods and limits the economic feasibility of soy protein foods.
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March 2025
Jilin Provincial Key Laboratory of Nutrition and Functional Food and College of Food Science and Engineering, Jilin University, Changchun 130062, China. Electronic address:
This study investigated the effects of formulation and ultrasound on the processing properties and nutrient digestion of soy protein isolate (SPI)-egg white protein (EWP) emulsion gels. The incorporation of EWP significantly improved the texture properties and freeze-thaw stability through disulfide bonds and homogeneous networks in comparison to SPI emulsion gels. However, swelling ratio of emulsion gels at SPI:EWP ratios of 3:1 and 2:1 decreased due to disruption of SPI network continuity.
View Article and Find Full Text PDFFood Chem
March 2025
Laboratory of Food Proteins and Colloids, School of Food Science and Engineering, Guangdong Province Key Laboratory for Green Processing of Natural Products and Product Safety, South China University of Technology, Guangzhou 510640, PR China. Electronic address:
The aim of this study was to explore the effects of environmental factors (salt ions and pH) on the thermal gelation process of deamidated soy protein isolate (DSPI). The results indicated that with increasing salt ion concentration, DSPI assembled into larger aggregates, which were more prone to aggregation in thermal reactions, ultimately forming a gel network with higher viscoelasticity. The strength enhancement of ion-induced gel networks followed the order from highest to lowest: Ca > Mg > Na.
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March 2025
Chongqing Key Laboratory of Speciality Food Co-Built by Sichuan and Chongqing, College of Food Science, Southwest University, Chongqing 400715, China. Electronic address:
Enhancement mechanism of ι-carrageenan on the network structure and gel-related properties of soy protein isolate (SPI)/λ-carrageenan system was investigated. Adding ι-carrageenan decreased SPI particles' size in nano-scale, reduced hydrophobic interactions by suppressing exposure of hydrophobic groups, and increased the disulfide bonds in SPI. With rising ι-carrageenan content (< 0.
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