Cryoprotective effect of gelatin hydrolysate from blacktip shark skin on surimi subjected to different freeze-thaw cycles

Conformational Changes and Kinetic Study of Actomyosin from Silver Carp Surimi with Modified Starch–Sucrose Mixtures during Frozen Storage

“…The results suggested that frozen storage possibly induced the exposure of SH groups, which were further oxidized to disulfide bonds (Kittiphattanabawon et al . ). After 28 days of storage, the highest total SH content (3.08 mol/10 5 g protein) was retained in surimi with AAES–sucrose mixture ( P < 0.05).…”

“…; Kittiphattanabawon et al . ). They are usually hydrophilic; the mechanism of cryoprotection of proteins was postulated to be the reinforcement of intramolecular hydrophobic interactions and the maintenance of the structural organization of water in system (Carpenter and Crowe ; Arakawa et al .…”

Effect of freezing on protein denaturation and gelling capacity of jumbo squid (Dosidicus gigas) mantle muscle

“…For most of these products preserving the gelling capacity of the muscle is essential, even after freezingethawing processes. However, without the use of cryoprotectants most muscles lose functionality when they are frozen, due to protein denaturation and/or aggregation (Goeller et al, 2004;Kittiphattanabawon, Benjakul, Visessanguan, & Shahidi, 2012;MacDonald, Lanier, Swaisgood, & Hamman, 1997).…”

Cryoprotective and antioxidative effects of gelatin hydrolysate from unicorn leatherjacket skin

“…Ca 2þ -ATPase activity of NAM from the control (without additive) showed a sharp decrease after freeze-thawing process, especially with 6 freeze-thaw cycles, in which less than 10% activity was retained. Kittiphattanabawon et al (2012a) reported that surimi from threadfin bream without cryoprotectant was particularly susceptible to denaturation as induced by the repeated freeze-thaw cycles. The decrease in Ca 2þ -ATPase activity was possibly due to the conformational change of myosin globular head responsible for ATPase activity as well as the aggregation of this portion (Ochaiai and Chow, 2000).…”

“…Cryoprotective effects of trehalose and sodium lactate on tilapia surimi were reported during frozen storage (Zhou et al, 2006). Kittiphattanabawon et al (2012a) found that the decrease in sulfhydryl groups of NAM extracted from threadfin bream with a concomitant disulphide bond formation was coincidental with the decrease in Ca 2þ ATPase activity during freeze-thawing process. The lower disulphide bond content (P < 0.05) was observed for NS-GH containing system at 0 freeze-thaw cycle, compared with others.…”