Abstract: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 meas… Show more
“…It showed that the addition of CAR can repair the large number of voids in the gel produced by thermal deformation, and therefore, presenting a more regular and orderly gel network structure. However, with the continuous increase of CAR addition (0.5%), the gel network structure inside the gel of minced shrimp gradually changed into a hierarchical network, which may be due to the addition of too high concentration of CAR which changed the surface hydrophobicity of myofibrillar fibrous protein particles and zeta potential and other particles properties ( Ouyang et al, 2021 ). Fig.…”
“…It showed that the addition of CAR can repair the large number of voids in the gel produced by thermal deformation, and therefore, presenting a more regular and orderly gel network structure. However, with the continuous increase of CAR addition (0.5%), the gel network structure inside the gel of minced shrimp gradually changed into a hierarchical network, which may be due to the addition of too high concentration of CAR which changed the surface hydrophobicity of myofibrillar fibrous protein particles and zeta potential and other particles properties ( Ouyang et al, 2021 ). Fig.…”
“…The possible reason was that the catalysis of TGase promotes the interaction between myofibrillar protein and non-meat protein Effect, so that the rheological properties of these two non-meat protein composite gels were enhanced. Ouyang, Y [25] proved that Compared with MP/WG system without TGase added, G of the system with TGase added increased more rapidly. This may be due to the formation of stable protein crosslinking structures catalyzed by TGase.…”
Section: Rheological Properties Of Mp Composite Gelling Solutionsmentioning
The emulsions prepared by three non-meat proteins, sodium caseinate (SC), soy protein isolate (SPI) and egg white protein (EPI), were individually added to the continuous phase of myofibrillar protein (MP) sol to form MP composite gels to simulate meat products. The research aimed to investigate the effects of Transglutaminase (TGase) on the physicochemical properties, microstructure and water phase distribution of non-meat protein emulsion MP composite gels. The results of this study revealed that TGase played a crucial role in forming a tight gel network structure in the composite gels. This enhanced their ability to retain water and improved their overall gel strength. Additionally, TGase increased the gel formation temperature of myofibrillar proteins. Electrophoresis analysis showed that when catalyzed by TGase, there was a lighter band compared to those not catalyzed by TGase. This indicated that the addition of TGase facilitated cross-linking interactions between meat proteins and non-meat proteins in the composite gels. Furthermore, microscopy observations demonstrated that composite gels treated with TGase exhibited a more uniform microstructure. This could be attributed to an acceleration in relaxation time T2. The uniform network structure restricted the movement of water molecules in the gel matrix, thereby improving its water-holding capacity. Overall, these findings highlight how incorporating non-meat proteins into myofibrillar systems can be effectively achieved through enzymatic treatment with TGase. Such modifications not only enhanced important functional properties but also contributed towards developing alternative meat products with improved texture and moisture retention abilities.
“…Research has shown that non-covalent bonds (hydrogen bonds and hydrophobic interactions) are the most important forces in stabilising animal protein-plant protein complex gels. However, certain studies have also reported that wheat gluten proteins, as plant proteins, do not cross-link with myofibrillar proteins and the interaction between the two proteins must be promoted through TGase to improve their gel properties [52].…”
With increasing awareness of human health, proteins from plant sources are being considered as alternatives to those from animal sources. The market for plant-based meat substitutes is expanding to satisfy the growing consumer demand. However, the functional properties of natural proteins frequently do not satisfy the needs of the modern food industry, which requires high-quality properties. Research on improving the functional properties of proteins is currently a popular topic. Based on the gel properties of proteins, this study focused on the formation mechanism of heat-induced protein gels, which will be helpful in expanding the market for plant protein gel products. Regulatory strategies for heat-induced gels were reviewed, including protein composition, pH, ionic strength, other food components, and processing techniques. The effects of other food components (such as polysaccharides, proteins, polyphenols, and liposomes) are discussed to provide insights into the properties of plant protein gels. Studies have shown that these factors can effectively improve the properties of plant protein gels. In addition, the development and application potential of emerging processing technologies that can contribute to safe and effective applications in actual food production are discussed. For the future, plant protein gels are playing an irreplaceable role in the new direction of future food.
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