Effect of sanxan as novel natural gel modifier on the physicochemical and structural properties of microbial transglutaminase-induced mung bean protein isolate gels

Lactoferrin–Chitosan Composite Hydrogels Induced by Microbial Transglutaminase: Potential Delivery Systems for Thermosensitive Bioactive Substances

“…This finding illustrated that increasing the CS concentration did not correspond to a proportional increase in hydrogel hardness, suggesting that 1.5% CS might represent the optimal concentration for maximizing the gel strength. Additionally, the results also indicated that a higher CS concentration (2%) impeded the formation of a robust gel network, likely due to the steric hindrance effect . Cohesiveness can be utilized to identify the internal bonding strength of a hydrogel structure.…”

“…This spectral region is frequently utilized for analyzing the secondary structure of proteins. Primarily, there are four structural units: α-helix (1646–1664 cm –1 ), β-turn (1664–1681 cm –1 ), β-sheet (1615–1637 cm –1 and 1682–1700 cm –1 ), and random coil (1637–1645 cm –1 ) . To better understand the conformational changes in proteins subjected to varying concentrations of CS and MTG treatments, the second derivative spectrum of the deconvoluted amide I band was analyzed.…”

“…Additionally, the results also indicated that a higher CS concentration (2%) impeded the formation of a robust gel network, likely due to the steric hindrance effect. 23 Cohesiveness can be utilized to identify the internal bonding strength of a hydrogel structure. The strongest cohesiveness was exhibited by the LF 16% − CS 1.5% −MTG 100U hydrogel, indicating that a greater CS concentration improved the structural integrity and cohesiveness of LF−CS−MTG hydrogels (Figure 2b).…”

“…Primarily, there are four structural units: α-helix (1646−1664 cm −1 ), β-turn (1664− 1681 cm −1 ), β-sheet (1615−1637 cm −1 and 1682−1700 cm −1 ), and random coil (1637−1645 cm −1 ). 23 To better understand the conformational changes in proteins subjected to varying concentrations of CS and MTG treatments, the second derivative spectrum of the deconvoluted amide I band was analyzed. This analysis involved fitting the spectrum to determine the relative proportions of the protein's secondary structure.…”