RESUMO
This study evaluated the effects of different drying techniques on the physicochemical properties of Pleurotus citrinopileatus Singer (P. citrinopileatus), focusing on the ergothioneine (EGT) contents. The P. citrinopileatus was subjected to natural ventilation drying (ND), freeze-drying (FD), and hot-air drying (HD). EGT was extracted using high-hydrostatic-pressure extraction (HHPE), and response surface methodology (RSM) was employed with four variables to optimize the extraction parameters. The crude EGT extract was purified by ultrafiltration and anion resin purification, and its antioxidant activity was investigated. The results showed that the ND method effectively disrupted mushroom tissues, promoting amino acid anabolism, thereby increasing the EGT content of mushrooms. Based on RSM, the optimum extracting conditions were pressure of 250 MPa, extraction time of 52 min, distilled water (dH2O) as the extraction solvent, and a 1:10 liquid-solid ratio, which yielded the highest EGT content of 4.03 ± 0.01 mg/g d.w. UPLC-Q-TOF-MSE was performed to assess the purity of the samples (purity: 86.34 ± 3.52%), and MS2 information of the main peak showed primary ions (m/z 230.1) and secondary cations (m/z 186.1050, m/z 127.0323) consistent with standard products. In addition, compared with ascorbic acid (VC), EGT showed strong free radical scavenging ability, especially for hydroxyl and ATBS radicals, at more than 5 mmol/L. These findings indicate that the extraction and purification methods used were optimal and suggest a possible synthetic path of EGT in P. citrinopileatus, which will help better explore the application of EGT.
RESUMO
This study explored the Maillard reaction process during the glycation of soy protein isolate (SPI) with galacto-oligosaccharides (GOSs) under high-pressure homogenization (HPH) and its effects on the emulsifying properties of SPI. SPI-GOS glycation under moderate pressure (80 MPa) significantly inhibited the occurrence and extent of the Maillard reaction (p < 0.05), but homogenization pressures in the range of 80−140 MPa gradually promoted this reaction. HPH caused a decrease in the surface hydrophobicity of the glycated protein, an increase in the abundance of free sulfhydryl groups, unfolding of the protein molecular structure, and the formation of new covalent bonds (C=O, C=N). Additionally, the particle size of emulsions created with SPI-GOS conjugates was reduced under HPH, thus improving the emulsifying properties of SPI. A reduction in particle size (117 nm), enhanced zeta potential (−23 mV), and uniform droplet size were observed for the emulsion created with the SPI-GOS conjugate prepared at 120 MPa. The conformational changes in the glycated protein supported the improved emulsification function. All results were significantly different (p < 0.05). The study findings indicate that HPH provides a potential method for controlling glycation and improving the emulsifying properties of SPI.
