• Fisheries and Aquatic Sciences
• /
• v.2 no.1
• /
• pp.12-16
• /
• 1999

Denaturation of actomyosin from the obliquely striated mantle muscle of squids (Todarodes pacificus) was studied by measuring the changes in $Ca^{2+}$-ATPase activity, relative viscosity, and solubility during frozen storage at three different temperature zones of maximum ice crystal formation $(-3^{\circ}C,\;-\;-5^{\circ}C)$, the eutectic point $(-11^{\circ}C)$, and $-20^{\circ}C$. The logarithms of $Ca^{2+}$-ATPase activity, relative viscosity and solubility of the actomyosin solutions (0.6 M KCl) and suspensions (0.05 M KCl) tended to decrease during frozen storage. The denaturation of squid actomyosin at the zone of maximum ice crystal formation significantly differed by only two degree of temperature difference between $-3^{\circ}C$ and $-5^{\circ}C$, and it (0.05 M KCl) at $-3^{\circ}C$ was less than those of other temperature. The denaturation at $-11^{\circ}C$ was more rapid than at $-5^{\circ}C$. The logarithms of $Ca^{2+}$ -ATPase activity, relative viscosity, and solubility were changed slower in the suspensions (0.05 M KCl) than the solutions (0.6 M KCl) at all experimental temperatures.

• Korean Journal of Fisheries and Aquatic Sciences
• /
• v.6 no.3_4
• /
• pp.101-111
• /
• 1973

To study the effect of freezing rate on the duality of frozen abalone(Haliotis gigantea, GMELIN) liquid nitrogen spray freezing, air blast freezing, semi-air blast freezing, and still air freezing were carried out. The rheological change, protein denaturation, and free water content of frozen and thawed abalone were examined at the period of 0, 1, 2, and 3 month during cold Storage at $-20^{\circ}C$. The results are summarized as follows : 1. The onset and duration of rigor mortis of fresh abalone was faster and shorter as compared to that of fishes. 2. There was no difference in compression value and shear value between freezing methods but they varied with a slight decrease in storage period. 3. Gradual decrease in extractibility of salt soluble protein was observed in all samples except those frozen with liquid nitrogen. 4. The free water of the foot muscle remained constant during the storage while that of the adductor muscle tended to increase. 5. A significant correlation was observed among the changes of panel texture and free water (P< 0.01), protein denaturation (P<0.05), and compression value (P<0.01).

• Asian-Australasian Journal of Animal Sciences
• /
• v.15 no.4
• /
• pp.585-590
• /
• 2002

The effects of a high level of sucrose on the moisture content, water activity, protein denaturation and sensory properties in Chinese-style pork jerky were investigated. The pork jerky with different levels (0, 12, 15, 18 and 21%) of sucrose was prepared. Fifteen frozen boneless pork legs from different animals were used in this trial. Sucrose is a non-reducing disaccharides and would not undergo non-enzymatic browning. Some studies pointed out that sucrose might be hydrolyzed during freezing, dehydration and storage into glucose and fructose, and cause non-enzymatic browning in meat products. The results showed that moisture content and water activity of pork jerky decreased with increase of the level of sucrose. At the same time, shear value was increased due to the reduced moisture content and water activity by osmotic dehydration. However, a higher level of sucrose had a significantly negative effect on protein solubility and extractability of myosin heavy chain of pork jerky due to non-enzymatic browning. From the results of sensory panel tests, the pork jerky with 21% of sucrose seems to be more acceptable by the panelists in hardness, sweetness and overall acceptability.

• Korean Journal of Food Science and Technology
• /
• v.21 no.4
• /
• pp.536-541
• /
• 1989

In present paper, we investigated the quality stability of frozen seasoned anchovy meat products during storage at $-25\;{\pm}\;2^{\circ}C$. The pH and VBN contents of the products revealed a tendency to increase slightly during frozen storage 150 days. Viable cell counts and histamine contents of products are $0.8-2.6\;{\times}\;10^5/g,\;70.6-76.7 mg/100g$, respectively. In changes of fatty acid composition, percentage of polyenes such as eicosapentaenoic docosahexaenoic acid slightly decreased, while that of saturates and monoenes increased during frozen storage, The results of changes in POV, TBA values, color values, drips and salt extractable nitrogen contents during frozen storage showed that lipid oxidation and freeze denaturation of products could be retarded, and flavor could be enhanced by adding 0.2% sodium erythorbate and 12.8% emulsion curd.

• Food Science of Animal Resources
• /
• v.36 no.1
• /
• pp.19-22
• /
• 2016

This study was conducted to improve sensory quality of Jokbal (Korean Pettitoes) made from frozen pig feet by addition of herbal mixture (glasswort, raspberry and Sansa powders). After adding herbal mixture, lipid oxidation (2-thiobarbituric acid values, TBARS), sensory property, and textural property were determined. Herbs were individually added into cooking soup at concentration of 6% (low concentration treatment, LCT) or 12% (high concentration treatment, HCT) of raw pig feet. Refrigerated pig feet were used as control. Thawed feet without any herbal mixture were used as freezing treatment (FT). TBARS in LCT or HCT were lower than that in FT, and showed the similar to that in Control. Addition of the herbal mixture was effective in improving the flavor and textural property of thawed feet by inhibiting lipid oxidation and protein denaturation in a dose-dependent manner.

• Korean Journal of Poultry Science
• /
• v.14 no.2
• /
• pp.145-151
• /
• 1987

In order to select the optimum freezing condition for the minimization of physico -chemical changes such as protein denaturation, lipid oxidation and pH change, the effect of freezing rates on the poultry meat quality changes was studied during frozen storage at -20$^{\circ}C$. Results obtained from the experiments are as fellows. When chicken breast and leg meat were frozen at above -3cm/hr or the freezing rate, pH change during frozen storage was minimal Although TBA value and free ratty acids were increased during frozen storage, the effect of freezing rates was different depending on muscle types. In terms of protein extractability, the extractability of salt soluble protein and water soluble protein were the highest at above -3cm/hr of the freezing rate during frozen storage. This trend was more obvious with breast meat than leg meat. Considering the above - described results, above -3cm/hr of the freezing rate seemed to be the optimum freezing condition for chicken meat because or the least pH change, low TBA value and high protein extractability.

• Korean Journal of Food Science and Technology
• /
• v.28 no.2
• /
• pp.267-272
• /
• 1996

Effect of freezing of soybeans on instrumental and sensory textures of soybean curd was investigated. The hardness, gumminess and chewiness of soybean curd prepared with frozen soybeans were about three times as high as those prepared with unfrozen soybeans, while cohesiveness and elasticity were affected little by freezing. Sensory evaluation showed that freezing improved the quality of soybean curd. Instrumental and sensory textures of soybean curd prepared with frozen soybeans were excellent and almost same regardless of the boiling time when the soy slurry was boiled for 2.5 min or 5 min. However, the textures of soybean curd prepared with unfrozen soybeans were deteriorated by reducing the boiling time to 2.5 min. It was postulated that freezing facilitate the heat-denaturation of soyprotein to enhance aggregation of soy proteins and formation of cross-linkage between aggregate and $Ca^{++}$. Frozen soybeans resulted in soybean curd which lower fat content, while protein content of soybean curd was almost he same. Frozen soybeans gave a lower yield of soybean curd, which is supposed to be caused by the more fat loss during whey-off.

• Fisheries and Aquatic Sciences
• /
• v.17 no.3
• /
• pp.291-298
• /
• 2014

We investigate the effects of cryoprotectant mixtures on the quality of sand lance surimi (SLS) during storage at $-30^{\circ}C$. We monitored freeze-induced denaturation of myofibrillar protein in SLS and examined the texture profile of SLS gel. Freeze-induced denaturation was assessed by evaluating SLS $Ca^{+2}$-ATPase activity. SLS gels prepared with sorbitol or sucrose and a mixture of both as cryoprotectant. Higher concentrations of cryoprotectants resulted in significantly higher residual SLS $Ca^{+2}$-ATPase activity at the same storage time (P < 0.05). Residual $Ca^{2+}$-ATPase activity of SLS prepared with sorbitol was higher than that of sucrose when cryoprotectant concentration and storage period were same. A blend of sorbitol and sucrose resulted in a stronger cryoprptective effect of SLS myofibrillar protein than did sorbitol or sucrose alone. The presence of a phosphate compound in SOP (3% sorbitol + 0.2% phosphate compound) resulted in higher SLS $Ca^{2+}$-ATPase activity than that of did 5% sorbitol. The hardness, brittleness, and elasticity values and a folding test of the SLS gels were significantly affected by cryoprotectant concentrations and the storage time. Preference scores and acceptance for texture in a sensory evaluation of the SLS gels increased with increasing sorbitol or sucrose concentration.

• Korean Journal of Food Science and Technology
• /
• v.30 no.4
• /
• pp.862-870
• /
• 1998

This study shows the application of Ci-ELISA method for monitoring the denaturation of myosin by the frozen treatment in order to differentiate thawed beef from chilled. Hanwoo M.Semitendinosus (n=25) was treated under the two different frozen process as follows; simple frozen treatment (Exp-1) at 4 different temperatures, -10, -20, -50 and $-80^{\circ}C$, respectively, and repeated thawing-refreezing treatment (Exp-2) stored at 4 different temperatures, -10, -20, -50 and $-80^{\circ}C$, respectively. Antibodies (Abs) were produced from rabbits immunized with myosin whole molecule (MWM) isolated from beef round, heavy meromyosin S-1 (S-1) and light meromyosin (LMM) prepared by digestion of MWM. Each immunoglobulin G (IgG) was separated from antiserum. At 6 month storage, IA of anti-MWM IgG for myosin was decreased to 32.67, 32. 23, 51.52 and 34.27% in Exp-1 and to 14.82, 15.61, 25.3 and 23.7% in Exp-2 at -10, -20, -50 and $-80^{\circ}C$, respectively (P<0.05). In Exp-1, the reactivities of anti-LMM IgG were decreased to 25.12, 21.42, 49.05 and 28.96%, and those of Exp-2 were to 11.88, 9.56, 20.63 and 12.64% at -10, -20, -50 and $-80^{\circ}C$, respectively, at 6 times thawing (P<0.05). Conclusively, myosin was denaturated by freezing treatment and LMM or myosin rod part might have suffered from more extreme demage than HMM S-1, and samples at $-50^{\circ}C$ were slightly injured less than others by freezing treatment.

• Journal of the Korean Society of Food Science and Nutrition
• /
• v.19 no.4
• /
• pp.349-355
• /
• 1990

Actomyosine prepared from Yellowtail fish(seriola quinqueradiata) were stored at $0^{\circ}C$(ice-cooling) -3.5$^{\circ}C$(partial freeaing) and -2$0^{\circ}C$(freezing) Another actomyosin samples were prepared from the fish previously stored at the temperatures for a week as the maximum .Remaining activity of {{{{ {Ca }^{2+ } }}}}-and {{{{ {Mg }^{2+ } }}}}- dependent adenosine triphosphatase(ATPase) activity was measured fronm the actomyosin preparations. Specific activity of {{{{ {Mg }^{2+ } }}}}-ATPase of actomy-osin before storagew was 0.253$\mu$ mole pi/min/mg of protein and it was 1.5 times higher than that of {{{{ {Ca }^{2+ } }}}} -ATPase. The enzyme activities were markedly decreased during early period of storage. However no significant differences in the enzyme activity were revealed among the samples stored at different temperature. The enzyme of actomyosin prepared from the fish previously stored at the temperatures for a week revealed an acitivity of 2-3 times higher than that of freezing. Apparent denaturation constant of {{{{ {Mg }^{2+ } }}}} -ATPase of actomyosin was between 0.810-1.139 per day and it was about 1.5 times hgiher than that of {{{{ {Ca }^{2+ } }}}} -ATPase. But the constant of {{{{ {Mg }^{2+ } }}}} ATPase of actomyosin extracted from the fist stored for a week at each temperature was between 0.176-0.356 per day. This constant was 4 times higher than that of {{{{ {Ca }^{2+ } }}}}- ATPase in frozen stored fish. It was presumed from these results that denaturation of ATPase is largely accorded to the structural changes of actomyosin.