“…The amide I and amide II peaks of glycated MPs exhibited an increasing trend, which was attributed to the glycation reaction, because this process involves the formation of new compounds (C N, C O, C—N) [22] . A new peak (2933 cm −1 ) corresponding to C—H stretching appeared in the spectra of glycated MPs, consistent with the formation of glycation products and confirmed by previous reports [20] . In addition, the absorption peak of the free hydroxyl groups was observed in the 3700–3200 cm −1 region.…”
Section: Resultssupporting
confidence: 91%
“…Consequently, we speculate that the cavitation effect of ultrasound provided an intense physical force to expose more reactive groups for the grafting of MPs and DX [25] . However, the grafting degree of glycated MPs pretreated by 500 W ultrasound decreased significantly ( P < 0.05), presumably because excessive power caused protein molecules to agglomerate through internal thermal effects, which in turn reduced the amount of exposed free amino groups in MPs and suppressed the glycation reaction [20] . Fig.…”
Section: Resultsmentioning
confidence: 99%
“…The degree of MP conjugation was determined by measuring the decrease in free amino group content in the treated MP samples using the o -phthaldialdehyde (OPA) method [20] . The OPA solution was freshly prepared by mixing 80 mg of OPA reagent, 50 mL of 0.1 M sodium tetraborate buffer (pH 9.3), 5.0 mL of 20 % (w/w) SDS, and 200 μL of β-mercaptoethanol, followed by dilution to a final volume of 100 mL with distilled water.…”
“…The amide I and amide II peaks of glycated MPs exhibited an increasing trend, which was attributed to the glycation reaction, because this process involves the formation of new compounds (C N, C O, C—N) [22] . A new peak (2933 cm −1 ) corresponding to C—H stretching appeared in the spectra of glycated MPs, consistent with the formation of glycation products and confirmed by previous reports [20] . In addition, the absorption peak of the free hydroxyl groups was observed in the 3700–3200 cm −1 region.…”
Section: Resultssupporting
confidence: 91%
“…Consequently, we speculate that the cavitation effect of ultrasound provided an intense physical force to expose more reactive groups for the grafting of MPs and DX [25] . However, the grafting degree of glycated MPs pretreated by 500 W ultrasound decreased significantly ( P < 0.05), presumably because excessive power caused protein molecules to agglomerate through internal thermal effects, which in turn reduced the amount of exposed free amino groups in MPs and suppressed the glycation reaction [20] . Fig.…”
Section: Resultsmentioning
confidence: 99%
“…The degree of MP conjugation was determined by measuring the decrease in free amino group content in the treated MP samples using the o -phthaldialdehyde (OPA) method [20] . The OPA solution was freshly prepared by mixing 80 mg of OPA reagent, 50 mL of 0.1 M sodium tetraborate buffer (pH 9.3), 5.0 mL of 20 % (w/w) SDS, and 200 μL of β-mercaptoethanol, followed by dilution to a final volume of 100 mL with distilled water.…”
“…The thermal denaturation temperature of the SPI nanofibrils after ultrasound pretreatment were lower than SPIN, and the denaturation temperature of 60SPIN and 80SPIN decreased more significantly, which were 62.322 °C and 64.679 °C, respectively. This indicated that the molecular environment of proteins was altered by high amplitude ultrasound, thereby reducing their conformational stability and thermal denaturation temperature [43] .…”
“…The secondary structure of the protein was assessed using circular dichroism (CD) spectroscopy according to the method described by [ 24 ], with some modifications. The CD measurements were performed using the J-815 spectropolarimeter (Jasco Corp., Tokyo, Japan) using a quartz cell with a path length of 1.0 mm and a temperature of 25 °C to scan the protein solutions (1% w / v ) from 190 to 260 nm.…”
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.
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