Effects of thermal aggregation treatment on the structural, gelation properties and microstructure of phosphorylated rice glutelin gel

Wang, Yaru; Qin, Yang; Li-Sha, Yi-Jing; Chen, Hanqing

doi:10.1016/j.jcs.2021.103252

Cited by 21 publications

(5 citation statements)

References 28 publications

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“…The ability of gels to effectively retain water molecules in a three-dimensional network structure is very important [34] , with higher WHC indicating a more compact gel network structure [1] . As shown in Fig.…”

Section: Resultsmentioning

confidence: 99%

Improvement of gelation properties of silver carp surimi through ultrasound-assisted water bath heating

et al. 2022

Ultrasonics Sonochemistry

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Highlights Ultrasound improved the strength, textural properties and WHC of surimi gel. Ultrasound promoted the unfolding of α-helix structures of protein. Ultrasound facilitated the formation of more compact microstructures. Ultrasonic-assisted preheating treatment had the most remarkable improvement on the gel properties of surimi.

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Section: Resultsmentioning

confidence: 99%

Improvement of gelation properties of silver carp surimi through ultrasound-assisted water bath heating

et al. 2022

Ultrasonics Sonochemistry

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“…A prior study demonstrated that TG action was higher when protein solubility increased [31]. As previously discussed, at a pH near 6.00, rice glutelins showed poor solubility, and they are stabilized mainly for disulfide bonds and hydrophobic interactions [32]. Disulfide bonds closed the protein structure and diminished the cross-linking reaction promoted by TG due to an insufficient exposure of the lysine and glutamine residues of proteins [33].…”

Section: Texture Parameters and Microstructure Of Hybrid Sausages Ela...mentioning

confidence: 92%

Effect of Transglutaminase Treatment on the Structure and Sensory Properties of Rice- or Soy-Based Hybrid Sausages

dos Santos,

Ribeiro,

Monteiro

et al. 2023

Foods

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Partial substitution of meat with non-protein sources in hybrid meat products generally leads to a decrease in texture attributes and, consequently, in sensory acceptance. In this study, we investigated the effects of transglutaminase (TG) at two concentrations (0.25% and 0.5%) on the physicochemical, textural, and sensory properties of hybrid sausages formulated with concentrated soy or rice proteins. TG caused a reduction in the heat treatment yield of hybrid sausages, particularly those made with rice protein. pH and color parameters were marginally affected by TG addition. Texture parameters increased substantially with TG, although escalating the TG level from 0.25% to 0.5% did not result in a proportional improvement in texture parameters; in fact, for rice-based hybrid sausages, no difference was achieved for all attributes, while only cohesiveness and chewiness were improved for soy-based ones. TG enhanced the sensory attributes of soy-based hybrid sausages to a level comparable to control meat emulsion, as evidenced by ordinate preference score and projective mapping. Our findings suggest that TG is a viable strategy for enhancing texture and sensory parameters in hybrid sausages, particularly for plant proteins that exhibit greater compatibility with the meat matrix.

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“…Molecular forces of MP‐SPIH plural gels were analyzed following the procedure of Wang et al 20 . by measuring protein solubility in denaturing solutions.…”

Section: Methodsmentioning

confidence: 99%

“…The characteristic peak of the amide I fraction (1700-1600 cm −1 ) was analyzed via the Peak Fit v 4.12 software to calculate the relative amounts of secondary structures, including ⊍-helix, ⊎-sheet, ⊎-turn, and random coil structures. 18,19 Molecular forces Molecular forces of MP-SPIH plural gels were analyzed following the procedure of Wang et al 20 by measuring protein solubility in denaturing solutions. Hydrogen bonds, hydrophobic interactions, and disulfide bonds were analyzed via denatured solutions of 8 mol L −1 urea, 0.5% sodium dodecylsulfonate (SDS), and 0.25% ⊎-mercaptoethanol, respectively.…”

Section: Fourier Transform Infrared Spectroscopy (Ftir)mentioning

confidence: 99%

Impacts of soybean protein isolate hydrolysates produced at high hydrostatic pressure on gelling properties, structural characteristics, and molecular forces of myofibrillar protein

et al. 2022

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BACKGROUND Soybean protein isolate hydrolysates (SPIHs) produced at high hydrostatic pressure have higher bioactivity. The aim of the study was to analyze the effects of different SPIH concentrations obtained under various pressures (0.1, 100, 200, and 300 MPa) on gelling properties, structural characteristics, and main forces of myofibrillar protein (MP) in MP‐SPIH plural gels. RESULTS The MP‐SPIH plural gel with 3% SPIH produced under 200 MPa had the maximum gel strength (0.42 N) and water holding capacity (53.69%). A decline in thermal stability and a rise in storage modulus (G′) of MP‐SPIH plural gels were found with increased SPIH pressure and concentration. Additionally, the addition of SPIHs increased the amounts of α‐helix and β‐sheet, decreased random coil structural content of MP in MP‐SPIH plural gels, and facilitated the generation of a denser and uniform gels network. The molecular forces in MP‐SPIH plural gels were mainly hydrophobic interaction and hydrogen bond. CONCLUSION This study showed that the interaction of MP with 3% SPIH obtained at 200 MPa improved the quality of plural gels. © 2022 Society of Chemical Industry.

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Effects of thermal aggregation treatment on the structural, gelation properties and microstructure of phosphorylated rice glutelin gel

Cited by 21 publications

References 28 publications

Improvement of gelation properties of silver carp surimi through ultrasound-assisted water bath heating

Improvement of gelation properties of silver carp surimi through ultrasound-assisted water bath heating

Effect of Transglutaminase Treatment on the Structure and Sensory Properties of Rice- or Soy-Based Hybrid Sausages

Impacts of soybean protein isolate hydrolysates produced at high hydrostatic pressure on gelling properties, structural characteristics, and molecular forces of myofibrillar protein

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