Ultrasound-Assisted Transglutaminase Catalysis of the Cross-Linking and Microstructure of αs-Casein, β-Casein and κ-Casein

Abstract

The effects of ultrasonic treatment (UT)-assisted transglutaminase (TGase) catalysis on the physicochemical properties of individual αs-casein (αs-CN), β-casein (β-CN), and κ-casein (κ-CN) were investigated. After 60 min of incubation at 30 °C, αs-CN, β-CN, and κ-CN were cross-linked with TGase (6.0 units/mL), and high molecular weight polymers (>200 kDa) were formed. The use of TGase in conjunction with UT (20 kHz, power of 400 W, and amplitude 20%) led to an increase in the rate of αs-CN, β-CN, and κ-CN polymerization compared to the individual casein that contained TGase but did not undergo UT. SDS-PAGE scrutiny showed that the intensities of αs-CN, β-CN, and κ-CN incubation with regard to TGase and UT at 30 °C for 60 min noticeably decreased to 5.66 ± 0.39, 3.97 ± 0.43, and 26.07 ± 1.18%, respectively (p < 0.05). Particle size analysis results indicated that the molecule size appropriation for the cross-linking of αs-CN, β-CN, and κ-CN ranged from 6000 to 10,000 nm after 60 min incubation with TGase and UT. Transmission electron microscopy investigation showed network structures of cross-linking αs-CN, β-CN, and κ-CN were formed from αs-CN, β-CN, and κ-CN, respectively. As our results show, the comprehensive utilization of TGase and UT will be a superior method for the polymerization of αs-CN, β-CN, and κ-CN.

Cross-Linking of White Proteins in Soft-Shell Turtle Eggs Using Transglutaminase, Reductant, and Thermal Pretreatment

“…Egg white samples were analyzed by SDS-PAGE following a modified method described by Chen et al [15], and these samples were analyzed by SDS-PAGE. The 0.25 mL sample was mixed with 0.75 mL of the sample buffer solution (70 mM Tris-HCl, pH 6.8).…”