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The gel properties and microstructure of scallop male gonad hydrolysates (SMGHs) were investigated by combing with κ‐carrageenan (κ‐C) and locust bean gum (LBG). It was shown that the initial elastic module of SMGHs/κ‐C 0.1 Hz got marked improvement from 202.3 Pa to 326.7 Pa and the melting temperature also increased 6°C with the addition of LBG. According to the data of low‐field nuclear magnetic resonance, the relaxation time T23 markedly reduced in SMGHs/κ‐C/LBG, representing the migration of water might result in a strong bind among SMGHs, κ‐C, and LBG. Fourier transform infrared spectroscopy showed the existence of hydrogen bonding between LBG and SMGHs/κ‐C. Low‐temperature scanning electron microscopy showed that the SMGHs/κ‐C/LBG ternary complexes possessed smaller voids and more dense network structures. These results could provide more possibilities for the application of SMGHs and polysaccharide complexes in functional hydrogel development. Novelty impact statement: We evaluated the gel and microstructure properties of ternary composite gel consisted of protein hydrolysates from male gonad of scallop (Patinopecten yessoensis) (SMGHs), κ‐carrageenan (κ‐C), and locust bean gum (LBG). The results showed that the addition of κ‐C and LBG significantly improved the gel properties of SMGHs. [ABSTRACT FROM AUTHOR]

• Low-acyl gellan gum had effect on gelation of scallop male gonad hydrolysates (SMGHs). • Gel strength of SMGHs was increased with increasing of low-acyl gellan gum (GG) dose. • The thermal stability of SMGHs gel was improved by the addition of GG. • The promoting effect of GG on SMGHs gel was related to the water migration. • The SMGHs/GG composite gels showed a regular and homogenous network. This study aimed to examine the gelation and microstructural properties of scallop male gonad hydrolysates (SMGHs) in the presence of low-acyl gellan gum (GG) at different mass ratios. The rheological results showed that both elastic modulus and thermal stability of SMGHs were significantly improved by the addition of GG. Meanwhile, the relaxation time T 23 was significantly reduced in SMGHs/GG by low-field nuclear magnetic resonance, indicating a strong interaction between SMGHs and GG. Fourier transform infrared spectroscopy indicated the blueshift of amide I and II peaks in SMGHs/GG further demonstrated the electrostatic interaction between SMGHs and GG. The network structure of SMGHs/GG binary complexes was more compact and the surface was smoother than that of SMGHs by cryo-scanning electron microscopy. Furthermore, increasing the content of GG in the SMGHs/GG binary complex significantly reinforced the gel strength and promoted the gelation process. [ABSTRACT FROM AUTHOR]

Studying the noncovalent interactions between proteins and polysaccharides is quite important mainly due to the wide number of applications such as developing pH-responsive complexes. Scallop Patinopecten yessoensis male gonad hydrolysates‑sodium alginate (SMGHs-SA) was investigated as noncovalent complexes at pH from 1 to 10. The critical pH values pH C (around 6) and pHφ (around 4) were independent of the SMGHs-SA ratio, indicating the formation of soluble and insoluble complexes. The pH response of SMGHs-SA complexes was evaluated by investigating the rheological behavior, moisture distribution, functional group change and microstructure. Compared to the co-soluble and soluble complexes phases, the SMGHs-SA complexes had a higher storage modulus and viscosity as well as a lower relaxation time (T 23) in the insoluble complexes phase (pHφ>3). Additionally, the amide I band and COO− stretching vibration peaks were redshifted and the amide A band vibration peaks were blueshifted by acidification. Electrostatic interactions and intermolecular/intramolecular hydrogen bonding led to SMGHs-SA agglomeration at pH 3, forming a uniform and dense gel network structure with strong gel strength and water-retention capacity. This study provides a theoretical and methodological basis for the design of novel pH-responsive complexes by studying SMGHs-SA complex coacervation. • Scallop gonad hydrolysates (SMGHs) and sodium alginate (SA) could coacervate. • Acidification promoted the formation of SMGHs-SA coacervations. • Electrostatic interactions were the main force for the SMGHs-SA complex at pH 3. • Hydrogen bonding also drove the interaction of SMGHs and SA. [ABSTRACT FROM AUTHOR]

Studying the noncovalent interactions between proteins and polysaccharides is quite important mainly due to the wide number of applications such as developing pH-responsive complexes. Scallop Patinopecten yessoensis male gonad hydrolysates‑sodium alginate (SMGHs-SA) was investigated as noncovalent complexes at pH from 1 to 10. The critical pH values pH C (around 6) and pHφ (around 4) were independent of the SMGHs-SA ratio, indicating the formation of soluble and insoluble complexes. The pH response of SMGHs-SA complexes was evaluated by investigating the rheological behavior, moisture distribution, functional group change and microstructure. Compared to the co-soluble and soluble complexes phases, the SMGHs-SA complexes had a higher storage modulus and viscosity as well as a lower relaxation time (T 23) in the insoluble complexes phase (pHφ>3). Additionally, the amide I band and COO− stretching vibration peaks were redshifted and the amide A band vibration peaks were blueshifted by acidification. Electrostatic interactions and intermolecular/intramolecular hydrogen bonding led to SMGHs-SA agglomeration at pH 3, forming a uniform and dense gel network structure with strong gel strength and water-retention capacity. This study provides a theoretical and methodological basis for the design of novel pH-responsive complexes by studying SMGHs-SA complex coacervation. • Scallop gonad hydrolysates (SMGHs) and sodium alginate (SA) could coacervate. • Acidification promoted the formation of SMGHs-SA coacervations. • Electrostatic interactions were the main force for the SMGHs-SA complex at pH 3. • Hydrogen bonding also drove the interaction of SMGHs and SA. [ABSTRACT FROM AUTHOR]

A composite hydrogel composed of scallop (Patinopecten yessoensis) male gonad hydrolysates (SMGHs) and κ -carrageenan (KC) was fabricated with a designed microstructure to preserve curcumin (Cur) during the upper gastrointestinal tract (GIT). The presence of KC obviously increased the initial elastic moduli (8.2–761.8 Pa), shortened the relaxation time T 23 (517.37–420.10 ms) as well as caused the blue shift of the emission peak and quenched the intrinsic fluorescence of Cur in SMGHs/KC-Cur system, signifying the solid combination within SMGHs and KC. In addition, the red shift in O–H stretching bands and blue shift in amide I bands in SMGHs/KC-Cur further accentuated the involvement of hydrogen bonds and electrostatic interactions within SMGHs, KC and Cur. The disappearance of crystalline structures suggested the successful embedment of Cur in the hydrophobic core of SMGHs. Moreover, the microstructure of the hydrogels varied from heterogeneous with tattered large pore cavities and scattered patches to homogeneous distribution with dense mesh and solid network wall. These scenarios caused a more compact network of SMGHs/KC-Cur than SMGHs-Cur to protect Cur from releasing in simulated intestinal and simulated colonic phases with slower released rate, both of which had the final extent of Cur release exceeding 90%. Furthermore, cryo-SEM showed that the significant release of Cur from hydrogels in the simulated intestinal phase was due to SMGHs matrix erosion with even larger pore sizes, tattered network and thinner network wall. Therefore, it is suggested that SMGHs/KC hydrogels with biocompatibility and good tolerance to acid environment could be reliable and desirable soft materials to embed and deliver Cur to the colon, having potential applications in functional foods and biological therapeutic purposes. [Display omitted] - Enhancement of gel elasticity in SMGHs/KC confirmed a feasible Cur-loaded carrier. - Migration of water in SMGHs/KC to bound water direction supported the Cur embedment. - Compact and dense porous networks of SMGHs/KC contributed to the Cur embedment. - Better sustained release of Cur in SMGHs/KC promised the delivery of Cur in colon. [ABSTRACT FROM AUTHOR]