Gel properties

Solubility

During the heating process, the structure of pea protein and the salt-soluble protein in chicken is fully expanded, the interaction is enhanced, and denaturation and aggregation occur, which restrains the movement of water molecules and forms a dense three-dimensional network structure, which enhances the gel's Water retention improves the gel cooking yield.

Pea protein is combined with salt-soluble protein, and the movement of water molecules is restrained. The interaction between proteins is enhanced, denatured and aggregated, forming a relatively dense three-dimensional network gel structure, thereby enhancing the water retention of the gel.

Since pea protein has strong emulsifying and gelling properties, as the amount of pea protein added increases, the number of gel molecules per unit volume and the probability of intermolecular collisions increase, which promotes the intermolecular interaction between pea protein and beef salt-soluble protein. Cross-linking forms a stable gel network structure.

It is speculated that pea protein can promote the formation of beef salt-soluble protein gel structure, mainly through physical filling, embedding and mechanical support, and the two may work through chemical interactions such as hydrophobic interaction, hydrogen bonding, and disulfide bonding. of.

Modified peanut protein isolate (AH-PPI)

Neutral proteolysis of peanut protein isolate and its enzymatic hydrolyzate

Wheat protein may be uniformly dispersed throughout the gel and tightly combined with surimi protein fibers, preventing the aggregation of myofibrillar proteins under high-temperature treatment, resulting in an increase in elastic properties.

The addition of FVP leads to an increase in the polarity of the microenvironment in which amino acids are located, indicating that the hydrophobic groups of the protein are exposed, which will enhance the interaction between the protein and oil and facilitate the improvement of emulsification performance.

After adding FVP, the hydrophobic groups inside the protein are more likely to react with the carbonyl groups, thereby reaching a new hydrophobic-hydrophilic balance, which is beneficial to the formation and stability of emulsions.

Because FVP fills the available space between proteins in the MP gel system, it connects the particles to each other and improves the mixed gel properties.

When the ratio of thermally modified FVP to MP is 1:9, the microstructure of the composite gel becomes denser and the roughness is reduced. This is because FVP, as a small molecule non-animal source protein, can form a well-interconnected gel with MP. The continuity of the matrix and protein matrix is ​​enhanced, and after the FVP is preheated, the protein structure unfolds, which makes the ability to bind water within the gel stronger, resulting in a more uniform and dense structure that enhances the gel properties.

The β-sheet content of the gel increased slightly after the addition of modified FVP, which was consistent with the results of the protein gel properties.

During the modification of FVP with 1% FVSP, the combination of protein and polysaccharide resulted in stronger electrostatic interaction. When mixed with MP, the heat treatment caused the polysaccharide particles to combine with MP in a network form to form a network coagulation. glue.

Adding mung bean protein enhances the interaction between proteins and promotes the formation of a tighter gel network structure.

Mung bean protein can reduce the content of free water and increase the content of non-flowing water, which helps the minced meat form a good three-dimensional gel structure, increase capillary force and retain more moisture.

Quinoa protein is a water-soluble protein, mainly composed of albumin and globulin. The content of gliadin and glutenin is low, so its solubility is higher than that of ordinary grain proteins. Therefore, as the amount of quinoa protein added increases , the protein solubility of the complex solution increases significantly.

After adding quinoa protein, the chemical force of the composite gel changes, and the content of ionic bonds and hydrogen bonds increases and is positively correlated with the amount of quinoa protein added. Through hydrogen bonding and ionic bonding, the binding between quinoa protein and MP becomes tighter, which makes the composite protein have better gelling properties.

Quinoa protein is rich in lysine and other polar amino acids, which form ionic bonds with the functional groups exposed inside MP during the heating process. As the quinoa protein content increases, the ionic bond content continues to increase.

Quinoa protein is rich in cysteine. During the heating process, the structure of quinoa protein is opened due to heating, causing the hydrophobic groups and sulfhydryl groups in the cysteine ​​side chains to be more exposed to the environment, promoting hydrophobic interactions. and disulfide bond formation.

The addition of quinoa protein will promote the transformation of random coil structure into β-sheet and α-helical structure. The increase in β-sheet and α-helical structures is conducive to high temperature induction of protein cross-linking, thereby improving gel strength.

After quinoa protein is mixed with MP, it is heated to form a network gel. The quinoa protein is filled in the three-dimensional grid structure formed by MP heating, and relies on the effects of hydrogen bonds and ionic bonds to further increase the interaction with water molecules in the gel. The adsorption capacity not only increases the water retention, making it difficult for water to flow out, but also makes the gel structure denser and smoother.

Adding rice protein can increase the absorption of water by meat, and more importantly, it can interact with surimi protein to promote the formation of a relatively dense spatial three-dimensional network structure of surimi, enhance the network structure strength of surimi gel, and promote the release of water that is not easy to flow. The mobility is reduced, the ability to be captured is enhanced, and more free water is diverted in the direction of less mobile water. This further reduces the loss of surimi gel during the cooking process and enhances the water holding capacity of surimi gel.

The interaction between chickpea protein emulsion (CPE) and myosin has occurred during the heating process, resulting in the formation of a certain three-dimensional network structure. This may be due to the fact that chickpea protein nanoparticles (CPNs) in CPE can stabilize the oil-water interface layer and participate in building the myosin gel network structure.

During the gelation process, myosin and chickpea proteins are denatured, exposing their hydrophobic groups and improving the surface hydrophobicity and hydrophobic interactions of the composite gel.

Oat globulin is an oligomeric protein. Its tertiary structure mainly connects subunits through non-covalent bonds to form a stable structure, and the connection of subunits is composed of acidic and alkaline polypeptide chains.

The globulin in OPE has a hexameric structure composed of 6 protein monomers, and its thermal stability is relatively high. Heating treatment of oat globulin at 100°C will trigger the dissociation of the hexameric structure and the aggregation of protein monomers, thereby forming a gel.

Oat globulins and myofibrillar proteins are associated through hydrogen bonds and hydrophobic interactions.

When gelled by heating, more hydrophobic groups are exposed and combined with proteins to enhance the gel strength of the complex protein.

The extracted naked oat globulin shows good solubility, emulsification and foaming properties under alkaline conditions, as well as good emulsification stability and foaming stability. Its viscosity value is also positively correlated with concentration changes. .

When the ratio of MP to OPE is 7:3, the gel strength is maximum. This may be because a small amount of OPE participates in the formation of the composite gel network in the form of filler, which significantly improves the gel strength of the composite gel.

As an exogenous protein, OPE undergoes cross-linking to a certain extent after contact with MP, forming thick filaments and pores. This structure can improve the mechanical properties of the gel.

When the gel is formed, it is accompanied by the production of fine crystallites, and the viscoelasticity of the gel network is provided by locally ordered small crystallites. These crystallites are connected in a network structure by entangled flexible polymers. The structure is stabilized primarily by a combination of hydrogen bonds and other secondary forces, thereby increasing the amount of recoverable energy stored in the elastic gel.

OPE contains a variety of amino acids in balanced proportions, which creates the possibility of synergistic effects after full contact with MP. Therefore, as the frequency gradually increases, the modulus change of the composite gel gradually increases and becomes stable. Make the viscoelastic properties of the gel more valuable.