Delaying In vitro gastric digestion of myofibrillar protein gel using carboxymethylated cellulose nanofibrils: Forming a compact and uniform microstructure

Zhang, Kai; Tian, Xiaojing; Shen, Ruixi; Zhao, Kaixuan; Wang, Yang; Zhang, Yafei; Wang, Wenhang

doi:10.1016/j.foodhyd.2023.108661

Cited by 25 publications

(3 citation statements)

References 51 publications

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“…Among these protein delivery systems, SPI exhibited an optimum sustained-release effect. This might be because SPI had the largest molecular weight and highly folded structure, which made it easier to form a dense micronetwork and thus inhibited the destruction of digestive enzymes on core material within carriers. , …”

Section: Resultsmentioning

confidence: 99%

“…This might be because SPI had the largest molecular weight and highly folded structure, which made it easier to form a dense micronetwork and thus inhibited the destruction of digestive enzymes on core material within carriers. 42,43 Thermal Stability. Considering the potential application of protein−Myr hydrogels in functional foods involving heat treatment, the thermal stability of Myr was evaluated.…”

Section: ■ Materials and Methodsmentioning

confidence: 99%

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Comparison of Alternative Protein Hydrogels for Delivering Myricetin: Interaction Mechanism and Stability Evaluation

Wang,

Wu,

et al. 2024

J. Agric. Food Chem.

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Food protein carriers from different sources might have distinct stabilizing and enhancing effects on the same small molecule. To elucidate the molecular mechanism, five different sourced proteins including soy protein isolates (SPIs), whey protein isolates (WPIs), edible dock protein (EDP), Tenebrio molitor protein (TMP), and yeast protein (YP) were used to prepare protein hydrogels for delivering myricetin (Myr). The results suggested that the loading capacity order of Myr in different protein hydrogels was EDP (11.5%) > WPI (9.3%) > TMP (8.9%) > YP (8.0%) > SPI (7.6%), which was consistent with the sequence of binding affinity between Myr and different proteins. Among five protein hydrogels, EDP had an optimum loading ability since it possessed the highest hydrophobic amino acid content (45.52%) and thus provided a broad hydrophobic cavity for loading Myr. In addition, these protein−Myr composite hydrogels displayed the core−shell structure, wherein hydrogen bonding and hydrophobic interaction were the primary binding forces between proteins and Myr. Moreover, the thermal stability, storage stability, and sustained-release properties of Myr were significantly enhanced via these protein delivery systems. These findings can provide scientific guidance for deeper utilization of food alternative protein sources.

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Section: Resultsmentioning

confidence: 99%

Section: ■ Materials and Methodsmentioning

confidence: 99%

Comparison of Alternative Protein Hydrogels for Delivering Myricetin: Interaction Mechanism and Stability Evaluation

Wang,

Wu,

et al. 2024

J. Agric. Food Chem.

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“…A significant increase in the gel strength and mechanical properties of SPI was observed when CG was incorporated. It had been reported that the change in gel strength may be linked to the network structure of SPI-CG cold-set gels and the interaction within the gel matrix between SPI-CG aggregates [ 16 , 33 ]. Thus, the apparent increase in gel strength may be explained by the formation of a firm and ordered network structure and the increased disulfide bond ratio in SPI-CG cold-set gel.…”

Section: Resultsmentioning

confidence: 99%

Investigating Texture and Freeze–Thaw Stability of Cold-Set Gel Prepared by Soy Protein Isolate and Carrageenan Compounding

Wang,

Yu,

Ren

et al. 2024

Gels

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In this study, the purpose was to investigate the effects with different concentrations of carrageenan (CG, 0–0.30%) on the gel properties and freeze–thaw stability of soy protein isolate (SPI, 8%) cold-set gels. LF-NMR, MRI, and rheology revealed that CG promoted the formation of SPI-CG cold-set gel dense three-dimensional network structures and increased gel network cross-linking sites. As visually demonstrated by microstructure observations, CG contributed to the formation of stable SPI-CG cold-set gels with uniform and compact network structures. The dense gel network formation was caused when the proportion of disulfide bonds in the intermolecular interaction of SPI-CG cold-set gels increased, and the particle size and zeta potential of SPI-CG aggregates increased. SG20 (0.20% CG) had the densest gel network in all samples. It effectively hindered the migration and flow of water, which decreased the damage of freezing to the gel network. Therefore, SG20 exhibited excellent gel strength, water holding capacity, freeze–thaw stability, and steaming stability. This was beneficial for the gel having a good quality after freeze–thaw, which provided a valuable reference for the development of freeze–thaw-resistant SPI cold-set gel products.

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Heat-induced Pleurotus ostreatus protein gel improved by konjac glucomannan: Physicochemical, gel and structural properties

Qian,

Qiu,

Zhang

et al. 2025

Colloids and Surfaces A: Physicochemical and Engineering Aspect

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Delaying In vitro gastric digestion of myofibrillar protein gel using carboxymethylated cellulose nanofibrils: Forming a compact and uniform microstructure

Cited by 25 publications

References 51 publications

Comparison of Alternative Protein Hydrogels for Delivering Myricetin: Interaction Mechanism and Stability Evaluation

Comparison of Alternative Protein Hydrogels for Delivering Myricetin: Interaction Mechanism and Stability Evaluation

Investigating Texture and Freeze–Thaw Stability of Cold-Set Gel Prepared by Soy Protein Isolate and Carrageenan Compounding

Heat-induced Pleurotus ostreatus protein gel improved by konjac glucomannan: Physicochemical, gel and structural properties

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