Preparation and characterization of high molecular weight vinyl-containing poly[(3,3,3-trifluoropropyl)methylsiloxane.

Prior to crosslinking and vulcanization, fluorosilicone rubber is a linear polymer. This linear polymer contains 3,3,3,-trifluoropropyl methyl siloxane links, a few methyl vinyl siloxane links, and is formed by co-polymerization of 1,3,5-trimethyl-1,3,5-tris(3,3,3-trifluoropropyl) cyclotrisiloxane (D3F) with 2,4,6,8-tetramethyl-2,4,6,8-tetravinylcyclotetrasiloxane (V4) under alkaline conditions. To improve the performance of fluorosilicone rubber, three key points should be considered during the synthesis of vinyl-containing high-molecular-weight linear fluorosilicone polymers (fluorosilicone raw rubber): first, avoid the generation of low molecular weight equilibrium by-products; second, eliminate the influence of impurities; and third, increase the copolymerization participation rate of monomer V4. From the three aspects above, this study optimized the reaction conditions for the synthesis of high-molecular-weight linear fluorosilicone polymers containing vinyl. Various factors influencing polymerization were thoroughly investigated. These factors include the initiation system, accelerator, equilibrium reaction, feeding ratio, feeding sequence, neutralization mode, impurity content, etc.

Effect of high intensity ultrasonic treatment on structural, rheological, and gelling properties of potato protein isolate and its co-gelation properties with egg white protein.

The study aimed to investigate the effect of high intensity ultrasonic (HIU) treatment at different times (0, 10, 20, and 30 min) on the structure and gel properties of water-soluble potato protein isolate (WPPI) and to further investigate the improvement of gel properties of ultrasonicated WPPI (UWPPI) by the addition of egg white protein (EWP). HIU reduced the particle size of WPPI, whose structure became loose and disordered, which improved gelling properties of UWPPI. Fourier transform infrared results indicated that α-helix content decreased, whereas the proportion of irregular curl increased with the increase in ultrasonication time (0-20 min), indicating that the initially ordered structure of UWPPI became disordered. After HIU treatment, the free sulfhydryl groups of UWPPI and surface hydrophobicity decreased and fluorescence intensity increased. These results demonstrated that the HIU loosened the structure of UWPPI, exposing more chromogenic groups while embedding more hydrophilic groups. After thermal induction, UWPPI gel hardness increased and exhibited excellent water holding capacity. After the addition of EWP, rheological properties stabilized, and the hardness of UWPPI-EWP gels increased significantly, forming internally structured protein gels with a tightly ordered structure and increased brightness. Thus, HIU changed the structure and gelling properties of WPPI, and the addition of EWP further enhanced the performance of hybrid protein gels. PRACTICAL APPLICATION: High intensity ultrasonic changed the structure of water-soluble potato protein isolate (WPPI) and improved the properties of WPPI gels. The addition of egg white protein significantly improved the quality of mixed protein gels which showed great potential industrial value.

Effect of high-intensity ultrasound on the structural, rheological, emulsifying and gelling properties of insoluble potato protein isolates.

The denaturation and lower solubility of commercial potato proteins generally limited their industrial application. Effects of high-intensity ultrasound (HIU) (200, 400, and 600 W) and treatment time (10, 20, and 30 min) on the physicochemical and functional properties of insoluble potato protein isolates (ISPP) were investigated. The results revealed that HIU treatment induced the unfolding and breakdown of macromolecular aggregates of ISPP, resulting in the exposure of hydrophobic and R-SH groups, and reduction of the particle size. These active groups contributed to the formation of a dense and uniform gel network of ISPP gel and insoluble potato proteins/egg white protein (ISPP/EWP) hybrid gel. Furthermore, the increase of solubility and surface hydrophobicity and the decrease of particle size improved the emulsifying property of ISPP. However, excessive HIU treatment reduced the emulsification and gelling properties of the ISPP. Meanwhile, HIU treatment changes the secondary structure of ISPP. It could be speculated that the formation of a stable secondary structure of ISPP initiated by cavitation and shearing effect might play a dominant role on gel strengthens and firmness. Meanwhile, the decrease in relative content of ß-turn had a positive effect on the formation of small particle to improve emulsifying property of ISPP.