蛋白质(如肌原纤维蛋白、乳清蛋白分离物、大豆蛋白分离物、酪蛋白)可作为

Proteins (such as myofibrillar protein, whey protein isolate, soy protein isolate, casein) can be used as matrix materials to prepare heat-set emulsion gels. Under normal circumstances, protein solutions need to be heated above the temperature of heat denaturation (usually> 65 ℃), in order to prepare thermal coagulation emulsion gel. Heat treatment can denature proteins, and denatured protein molecules can polymerize and form three-dimensional structures through chemical action (ie, chemical action), such as disulfide bonds, electrostatic interactions, hydrophobic interactions, hydrogen bonds, and ionic bonds. For example, the WPI denaturation temperature is 70°C, and the hydrophobic interaction between a series of exposed non-polar lactoglobulin molecules leads to aggregation and gelation of lactoglobulin. In addition, the covalent interaction between disulfide groups may also enhance the network structure strength of the lactoglobulin gel. The three-dimensional network of protein molecules is formed with a sufficiently high degree of dispersion in the aqueous solution, and this aqueous solution occupies the volume of the entire system, thereby forming a gel.

Proteins (e.g. myoglynia, whey protein isolates, soy protein isolates, casein) can be used as matrix materials to prepare thermocsolid emulsion gels. In general, the protein solution needs to be heated above the thermal degeneration temperature (usually 65 degrees C) in order to prepare the hot solidified emulsion gel. Heat treatment can denature proteins, and denatured protein molecules can be polymerized and formed into three-dimensional structures such as disulfur bonds, electrostatic segeneration, hydrophobic action, hydrogen bonds, and ion bonds. For example, WPI has a denatured temperature of 70 degrees C, and a series of exposed hydroglobulin molecules cause the hydrophobic interaction swelling and geling processes. In addition, covalent interactions between disulfur-based cells may also increase the mesh structural strength of the milk globulin gel. The three-dimensional network of protein molecules is formed in aqueous solutions with sufficient dispersion, which occupies the volume of the entire system to form a gel.

Proteins (such as myofibrillar protein, whey protein isolate, soy protein isolate and casein) can be used as matrix materials to prepare heat setting emulsion gel. In general, it is necessary to heat the protein solution above the denaturation temperature (usually > 65 degrees Celsius) to prepare the thermo coagulation emulsion gel. Heat treatment can denaturate protein, and denatured protein molecules can coalesce and form three-dimensional structures by chemical action, such as disulfide bond, electrostatic interaction, hydrophobic interaction, hydrogen bond and ionic bond. For example, the denaturation temperature of WPI is 70 degrees, and the hydrophobic interaction between a series of exposed nonpolar lactoprotein molecules leads to the aggregation and gelation process of lactoglobulin. In addition, the covalent interaction between two sulfur groups may also enhance the reticular strength of lactoprotein gel. The three-dimensional network of protein molecules is formed in aqueous solution at high enough dispersion, which occupies the volume of the whole system and forms gel.<br>