The synergistic interaction and gelling kinetics between xanthan gum (XG) and locust bean gum (LBG) at different mass ratios (XG/LBG 9:1, 7:3, 5:5, 3:7, 1:9) were investigated using a rheometer. The results showed that the mixtures of XG and LBG induced gel formation, and the strongest gel structure was found for the mixture of XG/LBG 3:7 according to the yield stress, storage modulus (G′), and power law parameters. Temperature ramp studies indicated that heating destroyed the gels at 55~60 °C, while cooling induced the sol–gel transition at around 52 °C for all mixtures. Structure developing rate (SDR) curves showed that XG/LBG 3:7 exhibited the highest SDR during the cooling ramp among all the samples. Non-isothermal kinetic analysis demonstrated that the gelation process of XG/LBG mixtures during cooling included two steps: a high-temperature region (55~39 °C) needing higher activation energy (Ea, 111.97 to 199.20 kJ/mol for different mixtures) and a low-temperature region (39~20 °C) needing lower Ea (74.33 to 85.31 kJ/mol), which indicated higher energy barriers to overcome at the initial stage of gel formation. The lowest Ea of 74.33 kJ/mol was found for XG/LBG 3:7 in the low-temperature region. Scanning electron microscopy (SEM) showed that the gel of XG/LBG 3:7 presented the densest entanglements. These results indicated the strongest synergism interaction occurred in XG/LBG 3:7 to form gel network structures. This study will help promote the application of XG-LBG blends to design novel food structures.

Peach gum polysaccharide (PGP), a natural biopolymer extracted from the resin of the peach tree, holds significant potential for applications in food, cosmetics, and pharmaceutical industries. However, detailed analysis and exploration of its physical and chemical properties remain limited. This study investigates the physicochemical properties, rheological behavior and emulsion stability of PGPs extracted using thermal (TPGP) and enzymatic (EPGP) methods. The results indicate that both polysaccharide fractions exhibit similar arabinogalactan (AG) structures, with high contents of arabinose and xylose, as evidenced by FTIR spectra and monosaccharide composition. However, high-performance size-exclusion chromatography (HPSEC) revealed differences in molecular weights and chain conformations, leading to distinct rheological behaviors. PGP solutions exhibited pseudoplastic flow behavior, with TPGP demonstrating higher viscosity due to its larger molecular weight (1.295 × 10⁷ g mol⁻¹). As the PGP concentration increased, gel strength and emulsion stability improved significantly. This study provides more insight into the rheological and emulsifying characteristics of PGPs extracted by varied methods, facilitating their potential applications in food industries.

Bovine lactoferrin (bLf) is a multifunctional glycoprotein and a good candidate for producing diverse bioactive peptides, which are easily lost during over-digestion. Accordingly, the effects of laccase-mediated pectin–ferulic acid conjugate (PF) and transglutaminase (TG) on improving the production of bLf active peptides by in vitro gastrointestinal digestion were investigated. Using ultra-high-performance liquid chromatography tandem mass spectroscopy (UPLC-MS-MS), the digests of bLf alone, PF-encapsulated bLf complex (LfPF), and TG-treated LfPF complex (LfPFTG) produced by conditioned in vitro gastric digestion (2000 U/mL pepsin, pH 3.0, 37 °C, 2 h) were identified with seven groups of active peptide-related fragments, including three common peptides (VFEAGRDPYKLRPVAAE, FENLPEKADRDQYEL, and VLRPTEGYL) and four differential peptides (GILRPYLSWTE, ARSVDGKEDLIWKL, YLGSRYLT, and FKSETKNLL). The gastric digest of LfPF contained more diverse and abundant detectable peptides of longer lengths than those of bLf and LfPFTG. After further in vitro intestinal digestion, two active peptide-related fragments (FEAGRDPYK and FENLPEKADRDQYE) remained in the final digest of LfPFTG; one (EAGRDPYKLRPVA) remained in that of bLf alone, but none remained in that of LfPF. Conclusively, PF encapsulation enhanced the production of bLf active peptide fragments under the in vitro gastric digestion applied. TG treatment facilitated active peptide FENLPEKADRDQYE being kept in the final gastrointestinal digest.