Intermolecular interaction in the hybrid gel of scallop (Patinopecten yessoensis) male gonad hydrolysates and κ‐carrageenan

Abstract

Various bond disrupting agents including NaCl, GuHCl, urea, and SDS were introduced to investigate the intermolecular interactions between scallop (Patinopecten yessoensis) male gonad hydrolysates (SMGHs) and κ‐carrageenan (κ‐C), which were monitored by changes in rheological property, water distribution, conformation characterization and microstructure by using rheometer, low field‐NMR relaxometry, Fourier transform infrared (FTIR) spectroscopy, cryo‐scanning electron microscopy (cryo‐SEM), and confocal laser scanning microscopy. The results showed that the bond disrupting agents deteriorated the rheological property of SMGHs/κ‐C in a dose‐dependent manner. Indeed, at the same concentration of 2 M, NaCl deteriorated the SMGHs/κ‐C more obviously than GuHCl and urea. In addition, SMGHs/κ‐C with bond disrupting agents possessed higher relaxation times including T21 and T23, indicating the migration to free water direction of bound and free water. Moreover, the FITR results showed the red‐shift in water regions (amide A and B bands), amide I and II bands, and indicated the breakdown of hydrogen bonds and electrostatic interactions, indicating a disordered structure in SMGHs/κ‐C by various bond disrupting agents. Furthermore, cryo‐SEM results showed the change of SMGHs/κ‐C from a homogeneous network to a looser and ruptured one with larger void spaces, and indicated the disrupted and tattered microstructure of SMGHs/κ‐C by various bond disrupting agents. Additionally, SMGHs/κ‐C as well showed less aggregates stained by RITC by bond disrupting agents. These results suggest that electrostatic interactions would be mainly involved in the maintenance of SMGHs/κ‐C gel network. This study could provide theoretical and methodological basis for hydrogel products with modified gel strength and microstructure by understanding the intermolecular interactions in gel system. Practical Application Scallop (Patinopecten yessoensis) male gonads as a high‐protein part of scallop, is usually discarded during processing despite its edibility. In recent years, scallop male gonads are regarded as good sources to develop protein matrices due to their high protein content and numerous nutrients. In this study, scallop male gonad hydrolysates (SMGHs) were obtained by trypsin‐treated process. The considerable gelation behavior of SMGHs indicated that the SMGHs could be potentially utilized as a novel thickener and additive in production of kamaboko gels, can, sausage and spread with marine flavor.

Complex characterization and formation mechanism of scallop (Patinopecten yessoensis) protein hydrolysates/κ‐carrageenan/konjac gum composite gels

“…As regards to SMGHs/KC, NaCl mostly decreased the rheological behaviors with the transformation from solid to slimy condition and relative G′ and G″ reducing to 14.72% and 18.92%, respectively (Figure 6b). This observation was consistent with the data reported by Yan, Du, et al (2021) that electrostatic interactions primarily govern the gel formation of SMGHs/KC.…”

“…This observation was consistent with the data reported by Yan, Du, et al. (2021) that electrostatic interactions primarily govern the gel formation of SMGHs/KC.…”

“…Different from Figure 6b, GuHCl and SDS as well strongly destructed the SMGHs/KGM/KC and revealed analogously effect, with corresponding relative G ′ and G ″ responses of 15.67%, 7.68% and 17.69%, 10.41%, respectively (Figure 6c), suggesting the involvement of hydrophobic interactions to gel development. Typically, hydrogen bonds are prone to be destroyed by urea, in which less hydrogen bonds could be retained upon urea treatment (Yan, Du, et al., 2021). In this study, the relative G′ responses of ternary gels was 62.36%, while only 45.72% in SMGHs/KC gels upon urea treatment (Figure 6b,c).…”

“…According to Yan, Du et al (2021), NaCl (1 mol/L), GuHCl (1 mol/L), urea (4 mol/L), and SDS (2%) were dissolved in deionized water before SMGHs, KC, or KGM (0.28%) addition. After sufficient dissolution, powder samples were soaked into corresponding solution at 4 • C for 16 h for sufficient hydration and gel formation.…”

“…The participant of intermolecular interactions in polysaccharide or protein gels could be deducted from the intervention of NaCl, urea, GuHCl, and SDS (Yan, Du, et al, 2021;Yu et al, 2017). Generally, NaCl primarily interferes electrostatic interactions through shielding the charged reactive patches in biopolymers; GuHCl and urea prevailingly have negative impact on hydrogen bonds and hydrophobic interactions, and SDS chiefly influences hydrophobic and electrostatic interactions (Sun & Arntfield, 2010;Yu et al, 2017).…”