Fusheng Chen

BACKGROUND: Soybean glycinin is considered a major allergenic protein, and glycation is widely used to reduce the allergenic potential of present allergens. Glycation of soybean glycinin with xylose at 55 °C for different lengths of time was investigated. The extent of Maillard reaction was reflected through the content changing of free amino groups, color analysis and sodium dodecyl sulfate–polyacrylamide gel electrophoresis. Alteration in the structural properties of glycinin was characterized by Fourier transform infrared spectroscopy, and antigenicity was evaluated by indirect competitive enzyme‐linked immunosorbent assay.RESULTS: The changes in the color of glycinin–xylose samples and the reduction of free amino group content in proteins indicated that the Maillard reaction occurred. The degree of glycation increased in glycated samples with the increase in reaction time. Glycation induced the changes in the secondary structure of glycinin and the ordered structure of proteins increased during the glycation reaction. The antigenicity of glycinin was reduced with the increase in reaction time. After glycation for 12 h, the antigenicity of glycinin declined about 18% compared with native glycinin.CONCLUSION: The application of glycation may be an efficient method to reduce the antigenicity of soybean glycinin. © 2016 Society of Chemical Industry

Five different extruded soy protein isolates (ESPIs) were obtained by extrusion and denoted by IVD1, IVD2, IVD3, IVD4, and IVD5. Then the SDS-PAGE results showed that the subunits of SPI decreased after extrusion, especially the subunits of 90.8, 32.8, and 31.3 kDa, whereas no isopeptide bond was formed. Although SPI improved both the development time (DT) and stability (S) of dough, ESPIs increased S but the DT decreased from 4.3 min to 1.8–2.0 min. Texture profile analysis (TPA) results showed that the hardness and chewiness of Chinese steamed bread (CSB) decreased in the order wheat flour Five different extruded soy protein isolates (ESPIs) were obtained by extrusion and denoted by IVD1, IVD2, IVD3, IVD4, and IVD5. Then the SDS-PAGE results showed that the subunits of SPI decreased after extrusion, especially the subunits of 90.8, 32.8, and 31.3 kDa, whereas no isopeptide bond was formed. Although SPI improved both the development time (DT) and stability (S) of dough, ESPIs increased S but the DT decreased from 4.3 min to 1.8–2.0 min. Texture profile analysis (TPA) results showed that the hardness and chewiness of Chinese steamed bread (CSB) decreased in the order wheat flour

Sodium bis (2-ethylhexyl) sulfosuccinate (AOT)-sodium dodecyl sulfate (SDS)/isooctane-octanol reverse micelle extraction was tested an efficient and effective approach to separate peanut protein from full-fat peanut powder. Here, important kinetic factors including pH, ion strength, and temperature were studied during reverse micelle backward extraction. The extraction conditions were obtained by response surface experiments as follows: pH 7.5, ion concentration 1.1 mol/L at temperature 35°C. Under these optimum extraction conditions, the extraction rate of protein reached 79.03%. A model on the kinetic partitioning of peanut protein was also developed. The backward extraction in this reverse micelle system was controlled by interfacial resistance instead of diffusion resistance in reverse micelle and aqueous phase with the total mass transfer rate of 0.8×10⁻⁵ m³·s⁻¹. A two-film theory may be the mechanism for flat interface. Results of mass transfer process are helpful for creating an reverse micelle extraction process, and used for purification of peanut proteins, promoting the development of food industry.

Cationic Surfactant-assisted Microwave-NaOH Pretreatment for Enhancing Enzymatic Hydrolysis and Fermentable Sugar Yield from Peanut Shells