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In this study, soy β-conglycinin (7S) was glycated with dextran of different molecular masses (40, 70, 150, 500 kDa) by the dry-heating method to synthesize soy β-conglycinin-dextran (7S-DEX) conjugates. The curcumin (Cur) loaded nanocomplexes were prepared based on 7S-DEX conjugates by a pH-driven self-assemble strategy to enhance the solubility and thermal stability of curcumin. Results showed that the 7S-150 conjugates (glycated from 7S with dextran (150 kDa)) could remain stable in the pH 3.0–pH 8.0 range and during the heat treatment. The results of fluorescence quenching and FT-IR indicated that glycated 7S were combined with curcumin mainly by hydrogen bonding and hydrophobic interaction, and 7S-150 conjugates had higher binding affinity than natural 7S for curcumin. The loading capacity (μg/mg) and encapsulation efficiency (EE%) of 7S-150-Cur were 16.06 μg/mg and 87.51%, respectively, significantly higher than that of 7S-Cur (12.41 μg/mg, 51.15%). The XRD spectrum showed that curcumin was exhibited in an amorphous state within the 7S-150-Cur nanocomplexes. After heating at 65 °C for 30 min, the curcumin retention of the 7S-150-Cur nanocomplexes was about 1.4 times higher than that of free curcumin. The particle size of 7S-150-Cur nanocomplexes was stable (in the range of 10–100 nm) during the long storage time (21 days).

Gelation properties of myofibrillar protein (MP)/wheat gluten (WG) induced by glutamine transaminase (TGase) were studied. Results showed that the inclusion of transglutaminase increased the gel strength, water‐holding capacity (WHC), and nonfreezable water (Wnf) of MP/WG mixture. Circular dichroism (CD) analysis showed that the β‐sheet and random coil content of the MP/WG treated with TGase addition increased by 12.1% and 3.7%, while the α‐helix and β‐turn content decreased by 14.2% and 1.8%. Rheological measurements showed that TGase induced higher energy storage modulus value during the MP/WG gel heating‐cooling cycle. the hydrogen bond and hydrophobic interaction content of the MP/WG gels increased by 80 and 120 ug/L, and the disulfide bond decreased by 200 ug/L, with TGase addition was increased from 0 to 120 U/g protein. Scanning electron microscope (SEM) showed that MP/WG gel with TGase had uniform and dense network structure. Practical Application The properties of myofibrillar/wheat gluten gel induced by TGase crosslinking was studied. The gel structure and water holding capacity of MP/WG were improved by the cross‐linking of TGase. The study of the gel properties of MP/WG induced by TGase crosslinking also can provide a theoretical basis for analyzing the effect of TGase on the application of gluten protein in complex meat emulsion system.

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