Thermal properties and heat-induced aggregation of natural actomyosin extracted from goatfish (Mulloidichthys martinicus) muscle as influenced by iced storage

Effect of frozen storage on thermal stability of sarcoplasmic protein and myofibrillar protein from common carp (Cyprinus carpio) muscle

“…S0 and S2 exhibited a higher rate in turbidity development than did S5 above 48 °C, and turbidity values of S2 were higher than those of S0. The differences in turbidity were most probably due to the varying size and/or rate of protein aggregation (Yarnpakdee et al ., ). A higher rate of protein aggregation and a higher increase in turbidity could be observed.…”

“…Yarnpakdee et al . () reported that the decrease in total SH groups was due to the formation of disulphide bond through oxidation of SH group or disulphide interchanges.…”

Cross-linking activity of oxidised tannic acid towards mackerel muscle proteins as affected by protein types and setting temperatures

“…Increased turbidity of NAM solution indicated the formation of the protein aggregate induced by OTA added. Absorbance reading is commonly used to monitor the extent of protein aggregates (Benjakul et al, 1997;Yarnpakdee, Benjakul, Visessanguan, & Kijroongrojana, 2009). At all levels of OTA incorporated, NAM solutions incubated at 40°C became more turbid, compared with those incubated at room temperature (P < 0.05).…”

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

“…Disulphide bond formation of fish actomyosin and myosin occurred at 40 and 45°C, respectively (Niwa, 1992). Yarnpakdee, Benjakul, Visessanguan, and Kijroongrojana (2009) reported that the disulphide bond formation in goatfish actomyosin required a temperature above 40°C.…”

“…The observed T max of myosin and actin were in the temperature range reported for various fish species. Yarnpakdee et al (2009) reported that NAM from goatfish had two endothermic transitions, with the T max of myosin and actin found at 47.4 and 63.5°C, respectively. Fresh bigeye snapper (Priacanthus tayenus) muscle proteins had two major endothermic peaks, with the T max at 47.7 and 70.6°C, and DH values of 1.42 and 0.69 J/g, respectively (Benjakul, Visessanguan, & Leelapongwattana, 2002).…”