Structural and physicochemical properties of soya bean protein isolate/maltodextrin mixture and glycosylation conjugates

Abstract

The effect of mixture and conjugation with maltodextrin (MD) in aqueous solution on the structural and physicochemical properties of soya bean protein isolate (SPI) was investigated. Although the mixing of MD would not change the distribution of secondary structure and tertiary conformation of SPI, the protein aggregation was promoted through hydrophobic interaction, which resulted in the decrease in solubility and the improvement of gel strength and water holding capacity (WHC) of SPI/MD mixture. However, glycosylation decreased a-helix and increased b-structure. The bathochromic shift of the fluorescence emission maximum wavelength for SPI/MD conjugates was promoted, resulting in less compact tertiary conformation. These structural modifications might be the reason for the changes in the physicochemical properties of conjugates. After glycosylation, the surface hydrophobicity and solubility were increased, the average particle size was decreased, and the gelation properties were weakened including gel strength and WHC.

Effect of ultrasonic treatment on peanut protein isolate‐oat dietary fibre mixture gels induced by transglutaminase

“…The percentage of each secondary structure was obtained by Gaussian peaks fitting of amide I band in FTIR of proteins. The band assignments of each secondary structure type were as follows: 1610-1640 cm -1 , 1640-1650 cm -1 , 1650-1660 cm -1 and 1660-1700 cm -1 corresponded to b-sheet, random coil, a-helix and b-turn, respectively (Zhao et al, 2020).…”

Gellan gum conjugation with soy protein via Maillard-driven molecular interactions and subsequent clustering lead to conjugates with tuned technological functionality

“…3 ). This could be attributed to the shielding effect of polysaccharide chain which hinders ANS binding to hydrophobic residues, so H 0 reduces ( Zhao et al, 2020 ). Moreover, the highest H 0 value in SPI-0.1LAGG might be due to their higher available protein concentration than other systems, probably leading to a greater ANS fluorescence intensity ( Uruakpa & Arntfield, 2006 ).…”

Effects of Different Amounts of Corn Silk Polysaccharide on the Structure and Function of Peanut Protein Isolate Glycosylation Products

“…The amide I band pattern was fitted using the PeakFit v4.12 software(Origin Lab Corp., Waltham, MA, USA) to obtain the percentage of each secondary structure. The frequency bands for each secondary structure were assigned as follows: 1610–1640 cm −1 , 1640–1650 cm −1 , 1650–1660 cm −1 , and 1660–1700 cm −1 corresponding to β -sheet, random coil, α -Helix, and β -turns, respectively [ 45 ]. The results are shown in Table 2 .…”