Effects of CaCl2 on chemical interactions and gel properties of surimi gels from two species of carps

Effect of electron irradiation and heat on the structure of hairtail surimi

“…The most important functional characteristics of surimi products are the gel properties. Gelation is the result of protein denaturation, affected by inter and intramolecular covalent and noncovalent chemical interactions that include disulfide bonds, nonspecific associations, ionic bonds, hydrogen bonds, and hydrophobic interactions (Ding et al, 2011). Therefore, to better understand the internal mechanism of the gel properties, protein-protein chemical interactions should be investigated.…”

Rheological behavior of heat-induced actomyosin gels from yellowcheek carp and grass carp

“…At the end of the cooling, G 0 of YAM in the concentration range of 24-10 mg/mL was 4,924.5-213.1 Pa, which was much higher than that of GAM (3,443.0-14.0 Pa), especially at lower protein concentrations. Our preliminary data also suggested that suwari and kamaboko gels from yellowcheek carp exhibited higher breaking force, deformation and gel strength than those from grass carp [1].…”

“…Grass carp (Ctenopharyngodon idellus) is herbivorous, and grass carp surimi is a typical commercial freshwater fish surimi in China. However, the gel forming ability of surimi from grass carp was inferior to that from yellowcheek carp [1]. Actomyosin is a major myofibrillar protein in fish surimi, which largely contributes to the textural and water-holding properties of surimi gel.…”

Impact of zinc salts on heat-induced aggregation of natural actomyosin from yellow stripe trevally

“…Furthermore, protein molecules also underwent aggregation via hydrophobic interaction, electrostatic and hydrogen bonds, Van de Waals interaction and disulphide bond during a heat induced gelation process (Chawla, Venugopal, & Nair, 1996;Xiong, 1997). Divalent metal ions might cause changes in protein conformation and interact with negative charges on the polypeptide chains of proteins, thereby inducing cross-linking via salt bridges (Ding et al, 2011).…”

“…Ding et al (2011) reported that divalent metal ions might cause changes in protein conformation and interact with negative charges on the polypeptide chains of proteins and induce cross-linking by the formation of salt bridges. However, the higher decrease in negative charge was observed in NAM added with ZnSO 4 , compared with ZnCl 2 (P < 0.05).…”