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1.
Thermal inactivation of Ca2+ ATPase of squid myofibrils was significantly suppressed in the presence of Ca2+. Monomeric myosin content decreased much faster than Ca2+ ATPase inactivation in Ca medium, which was well explained by fast rod denaturation. In contrast, rod denaturation was slower than S-1 in EDTA medium. The decrease in monomeric myosin content was explained by faster S-1 denaturation. Comparing the S-1 and rod denaturation rates at a fixed temperature, it was concluded that S-1 denaturation was suppressed by Ca2+ whereas the rod denaturation was not. An unfolding experiment with isolated myosin rod confirmed that there was no stabilizing effect of Ca2+ on myosin rod. It was concluded that significant stabilization of the S-1 portion by Ca2+ generated the apparently different myosin denaturation patterns in the two media.  相似文献   

2.
Thermal denaturation profiles of catfish myosin when heated as myofibrils (Mf) were compared with those of tilapia. The Ca2+-ATPase inactivation rate of catfish myofibrils was the same as that of tilapia myofibrils. The conclusion was the same with isolated myosin. Catfish Mf was clearly distinguished from tilapia Mf in terms of subfragment-1 (S-1) and rod denaturation. Quick denaturation of rod relative to S-1 was characteristic of catfish Mf, while slower denaturation of rod relative to S-1 was the pattern for tilapia Mf. These patterns were greatly affected by the pH for heating. Rod denaturation was accelerated with increasing pH for heating and oppositely suppressed by lowering the pH, for both Mf. Tilapia Mf showed a S-1 and rod denaturation pattern similar to that for catfish Mf, but at 1 pH unit higher; for example, the pattern of catfish Mf at pH 7.5 was similar to that for tilapia Mf at pH 8.5. Less rigid filament structure of catfish Mf than tilapia Mf was demonstrated by studying chymotryptic digestion at various pH values. Accordingly, the difference in the S-1/rod denaturation patterns between the two fish species can be explained by the different rigidity of their myosin filaments.  相似文献   

3.
ABSTRACT:   Suppressive effects of non-ionic (sorbitol, maltose, and trehalose) and ionic (Na-glutamate, Na-acetate, Na-sulfate, and ammonium sulfate) compounds on the thermal inactivation of myosin subframgent-1 (S-1) and myofibril Ca2+-ATPase were compared. All compounds suppressed S-1 denaturation. When myofibrils were used (at 0.1 M KCl), sugars and sugar alcohol (non-ionic compounds) suppressed denaturation similar to S-1, while Na-glutamate, Na-acetate, and Na-sulfate weakly suppressed them. Ammonium sulfate accelerated denaturation, but suppressed denaturation when heated in 2 M KCl, at which myosin lost protection by F-actin. It was thus concluded that ionic compounds affected the denaturation of myofibrils in two ways; suppression as established with S-1, and acceleration as a result of loss of protection by F-actin caused by increase in ionic strength.  相似文献   

4.
The thermal inactivation of Ca2+ ATPase of scallop myofibrils (0.1 M KCl, pH 7.5) was found to be unaffected by the presence of Ca2+. Monomeric myosin content and salt solubility decreased much faster than Ca2+ ATPase inactivation in both Ca and EDTA media, which was well explained by faster denaturation of the rod portion than subfragment-1 of myosin. In contrast, when the myofibrils were heated at 0.5 M KCl, a slow decrease in salt solubility was observed, which was also explained by slow denaturation of the rod portion of myosin. Myofibrils from scallop smooth muscle showed the same denaturation pattern as those from adductor muscle. These results show that mollusk myosin is not always stabilized by Ca2+.  相似文献   

5.
ABSTRACT:   The effect of salt concentration on the thermal denaturation profile of myosin in walleye pollack and carp myofibrils was compared by studying the subfragment-1 (S-1) and rod denaturation rates upon heating. Species-specific denaturation mode observed at 0.1 M KCl was no longer detected when samples were heated above 0.5 M KCl, where S-1 and rod denaturation rates were identical to each other. As the heating of the chymotryptic digest of myofibril formed practically no rod aggregates, S-1 denaturation in a form of myosin was the rate limiting step for rod aggregate formation. As the aggregate formation by rod was remarkably suppressed by lowering the temperature, the free movement of myosin tail upon heating was suggested to play an important role in the rod aggregate formation in a high salt medium.  相似文献   

6.
The effects of non-ionic (sorbitol, maltose, trehalose) and ionic compounds (Na-glutamate, Na-acetate, Na-sulfate, ammonium sulfate) on freeze denaturation of myosin subfragment-1 (S-1) and of myofibrils were compared. Sugars, Na-glutamate and Na-acetate well suppressed the freeze denaturation of myofibrils as well as S-1 in a concentration dependent manner. Although sulfate suppressed freeze denaturation of S-1 irregularly, it accelerated myofibril denaturation. It was concluded that sulfate salts were useless as cryoprotectant for myofibrils. Stabilization extent by F-actin in frozen storage was much less than that in heating.  相似文献   

7.
Suppressive effects of neocarrabiose 4-O-sulfate on the thermal and freeze denaturation of myosin subfragment-1 (S-1) and on myofibrils were investigated. The compound strongly suppressed the thermal denaturation of S-1. Its suppressive effect was greater than that of sorbitol and similar to that of maltose. However, it tended to accelerate the denaturation of myofibrils, suggesting a loss of protection by F-actin upon its addition. The compound suppressed the freeze denaturation of myofibrils and S-1. The effect was similar to that of sorbitol or maltose, and completely different from that of Na-sulfate. The compound solubilized myofibrils at concentrations similar to KCl. Therefore, it was concluded that neocarrabiose 4-O-sulfate behaved as an ionic salt in the thermal treatment process, whereas it behaved as a sugar in the frozen storage process.  相似文献   

8.
The suppressive effects of Ca2+ on the thermal denaturation of myosin and myofibrils of squid mantle muscle were compared. The stabilization effect on myosin was smaller than that on myofibrils and was not affected by KCl concentration. The stabilizing effect of Ca2+ on myosin decreased as the heating temperature dropped, showing no stabilization at 20°C, while the effect on myofibrils was the same at all temperatures tested. The stabilizing effect of Ca2+ on myosin disappeared even at 30°C in the presence of sorbitol, where a small inactivation rate was found, while the effect of Ca2+ on myofibrils was equally detected irrespective of the reduction in inactivation rate in the presence of sorbitol. Stabilization of myosin by Ca2+ again appeared even in the presence of sorbitol when the heating temperature was raised to 38°C. It was suggested that Ca2+ confers stabilization on myosin only when myosin is under unstable conditions. The stabilization effect of Ca2+ on myosin was enhanced upon F-actin binding: Ca2+-bound myosin was more significantly stabilized by F-actin binding, and the effect was no longer affected by the conditions for heating.  相似文献   

9.
ABSTRACT: Heating temperatures of 30–40°C and KCl concentrations of 0.1–0.5 M altered the denaturation mode of carp myofibrils. In 0.1 M KCl medium, heating temperature affected the denaturation of rod more significantly than of subfragment-1 (S-1), and a slow decrease in solubility at 30°C was accompanied by a slow denaturation of rod. KCl concentration at heating altered the denaturation mode differently at 30°C and 40°C. Increased KCl concentrations for heating reduced the rod denaturation rate at 40°C, but it was increased at 30°C. At concentrations above 0.3*Τ*M KCl, the denaturation rate for rod became identical to that for S-1 at both temperatures. Upon heating of chymotryptic digest of myofibrils, S-1 denaturation was similarly detected as in intact myofibrils, whereas practically no rod denaturation was detected. Thus, it was concluded that myosin structure connecting S-1 and rod has an important role in the denaturation process.  相似文献   

10.
Myosin and actin denaturation in kuruma prawn myofibrils stored frozen (0.1 M NaCl, pH 7.5) at ?20 °C was investigated. The inactivation profile of Ca2+-ATPase in the myofibrils was identical to that for myosin, indicating that myosin in myofibrils was not protected by actin. The presence of myosin detached from actin in the soluble fraction was proven by ammonium sulfate fractionation in the absence and presence of Mg-ATP. Actin denaturation in myofibrils was further confirmed by its increased susceptibility to chymotryptic degradation. In the frozen myofibrils, actin denatured more rapidly quicker than myosin: actin had completely denatured by storage day 1, followed by a gradual denaturation of myosin. Both myosin and actin in the frozen stored myofibrils retained their high salt-solubility, which decreased slowly during the frozen storage period. The presence of aggregated inactivated myosin in the salt-soluble fraction was proven by precipitation at 40 % saturation of ammonium sulfate in the presence of Mg-ATP, leaving active monomeric myosin in the soluble fraction. Almost no actin denaturation was observed with heated myofibrils.  相似文献   

11.
Fisheries Science - The thermal stability of myosin and the protective effect of F-actin on myosin in kuruma prawn myofibrils were investigated from the thermal inactivation rates at...  相似文献   

12.
A quantitative conversion of tuna meat into muscle homogenate made it possible to study myosin denaturation in Bluefin tuna meat. Myosin denaturation was accessed by measuring Ca2+-ATPase activity, salt-solubility with and without Mg-ATP, monomeric myosin content, and amount of subfragment-1 (S-1) and rod produced by chymotryptic digestion. Commercially available tuna used in this study showed a pH around 5.4–5.7. Myosin in the meat lost the salt-solubility measured in the absence of Mg-ATP; however, such myosin showed full salt-solubility when released from actin in the presence of Mg-ATP. Incubation of tuna meat at 30 °C for up to 90 min caused obvious myosin denaturation. However, the tuna meat dialyzed against neutral pH buffer showed practically no myosin denaturation by the same heating. It was suggested that exposure to lowered pH to around 5.5 and increased temperature of 30 °C led myosin denaturation. Myosin denaturation in the “Burnt” Bluefin tuna sample was analyzed. A significant myosin denaturation was observed with the part showing the “Burning” symptom, the inner part of the tuna meat near the spine. Myosin in that part showed almost no Ca2+-ATPase activity, no salt-solubility even with Mg-ATP, no recovery of monomeric myosin, and almost no production of S-1 by chymotryptic digestion. However, myosin denaturation was not detectable for the meat taken from outer parts of the same tuna near the skin with normal appearance. It was demonstrated that “Burning” of tuna meat occurring in the deep part of the body is accompanied by myosin denaturation. The above results suggested that insufficient cooling of the deep part of body would be the reason for “Burning” of tuna meat.  相似文献   

13.
Eriko  ABE  Kazunori  HAYAKAWA  Meiko  KIMURA  Ikuo  KIMURA  Nobuo  SEKI 《Fisheries Science》2003,69(3):605-614
ABSTRACT:     Formaldehyde (FA)-induced denaturation of myofibrillar proteins and its prevention were investigated by means of measuring the solubility, adenosine triphosphatase (ATPase) activity, and thermal gel formability of myofibrils and surimi proteins in the presence and absence of free amino acids and glutathione, reduced form. The addition of FA decreased the solubility of myofibrils in 0.5 M NaCl at pH 7.0 and 0°C depending on its concentration and incubation time. The solubility decrease was completely inhibited by the presence of equal, twofold, and threefold amounts of cysteine (Cys), glutathione, and histidine (His) to the amount of FA, respectively. Myofibrillar Ca-ATPase was markedly activated at the initial phase and then decreased later by the addition of FA. The K-ATPase was inactivated with an increase in the amount of FA. The FA-induced changes in both ATPase activities were inhibited in the presence of Cys and His. Thermal gel formability of surimi paste increased only in a short period after the addition of a low concentration of FA. Practically, FA inhibited the thermal gelation and setting effect through the inactivation of transglutaminase. In the presence of Cys, His or glutathione, a strong elastic surimi gel was produced because FA-induced detrimental effects were inhibited.  相似文献   

14.
The structural stability of fish myosin depends upon species and temperatures of water in which fish live. Primary, secondary, and quaternary structures of myosin heavy chain (MyHC) from three species of fish living at different temperature ranges have been compared with those of rabbit MyHC in order to investigate the differences in stability. Primary structure of MyHC, although being accessible for warm-water and cold-water fish (carp and walleye pollack), was not available in previous for tropical-water fish literature; so in this study primary structure of MyHC of the tropical-water fish amberjack has been determined by cloning and sequencing its cDNA. The MyHC has 1938 amino acid residues (AA), which are almost as much as as those of carp and walleye pollack. The amberjack MyHC is 91–95% homologous with other fish and rabbit MyHCs. There is a discernible difference between animal species with stable myosin rod (amberjack, carp, and rabbit) and walleye pollack with unstable rod. Stable rod species have a high probability of forming coiled-coil around the COOH-terminal end of the rod, while the pollack has a low coiled-coil formation probability. In addition, the average scores of the coiled-coil for myosin rod were rabbit (1.738) > amberjack (1.691) > carp (1.680) > walleye pollack (1.674) which correlated exactly with the observed stability. The results suggest that coiled-coil forming ability, particularly around the COOH-terminal end, directs structural stability of fish myosin rod.  相似文献   

15.
Fan  Xinru  Konno  Kunihiko  Lin  Xiaoyu  Yu  Xilaing  Liu  Yuxuan  Dong  Xiuping 《Fisheries Science》2020,86(6):1111-1120
Fisheries Science - The effect of fish freshness on myosin denaturation during the frozen storage of flounder muscle was studied. The muscle of instantaneously killed flounder was immediately...  相似文献   

16.
ABSTRACT:   To utilize fisheries waste products as food materials with functional properties, shrimp head protein hydrolysates (SHPH) from three species of shrimp, that is, Northern pink shrimp ( Pandalus eous ), Endeavour shrimp ( Metapenaeus endeavouri ) and Black tiger shrimp ( Penaeus monodon ), were produced by enzymatic hydrolysis using endopeptidase derived from Bacillus subtilis and exopeptidase derived from Aspergillus oryzae at a level of 0.1% (w/w). SHPH were rich in protein (90–91%) and amino acids (71–84%) but little fat (0.01–0.02%). The average molecular weight of SHPH was 300–1400. The effect of 5% SHPH (dry basis) addition on the state of water and denaturation of lizard fish myofibrils (Mf) during the dehydration process was evaluated by the desorption isotherm and the Ca-ATPase activity, and compared with the effect of sodium glutamate (Na-Glu). SHPH decreased the water activity and the Ca-ATPase inactivation, and increased monolayer sorbed water and multilayer sorbed water of Mf, although these effects of SHPH were smaller than those of Na-Glu. These findings suggest that the SHPH suppressed dehydration-induced denaturation of myofibrillar protein by stabilizing the hydrated water surrounding myofibrils.  相似文献   

17.
Changes in physical properties of two-step heated gels on addition of gluconate were investigated in terms of relationships between breaking strength and gel stiffness. Regression lines between the breaking strength and the gel stiffness were extended to the x-axis (gel stiffness), and the intercept was defined as SBSO. The SBSO of the two-step heated gels increased with gluconate contents in salt-ground surimis, suggesting that the harder but less elastic gels formed on addition of gluconate were dose-dependent. Conversely, the denaturation rate constants of myosin in salt-ground surimis during preheating estimated by means of Ca-ATPase inactivation, loss of salt solubility, and decrease of denaturant solubility were considerably reduced by gluconate. Thus, the progress of myosin denaturation was strongly suppressed. Increments of SBSO (δSBSO) of the two-step heated gels on addition of gluconate were inversely correlated with the denaturation rate constants of myosin in salt-ground surimis for every index. Thus, the changes in physical parameters of two-step heated gel caused by gluconate may be associated with the sluggish progress of myosin denaturation in salt-ground surimi during preheating.  相似文献   

18.
ABSTRACT:   Enzymatic and structural properties of white croaker fast skeletal muscle myosin were determined and compared with those of walleye pollack counterpart. Ca2+-ATPase activity of white croaker myosin was decreased to approximately 70% of the original activity during 1 day of storage at 0°C and pH 7.0 in 0.5 M KCl and 0.1 mM dithiothreitol, whereas that of walleye pollack was decreased to approximately 20% under the same condition. The activation energy ( E a) for inactivation of white croaker myosin calculated by the Arrhenius plot for inactivation rate constant (KD) was 1.2-fold higher than that of walleye pollack. While Ca2+-ATPase showed a similar KCl-dependency for the two species, the maximal activity was observed at pH 6.2 and 6.3 for white croaker and walleye pollack, respectively. Actin-activated myosin Mg2+-ATPase activity of white croaker was approximately half that of walleye pollack at 0.05 M KCl and pH 7.0, although the two myosins showed a similar affinity to F-actin with K m of 1.7 and 1.4, respectively. Limited proteolysis with α-chymotrypsin cleaved heat-denatured white croaker myosin mainly at heavy meromyosin/light meromyosin (HMM/LMM) junction, whereas walleye pollack myosin was cleaved at several sites in LMM as well as at the HMM/LMM junction.  相似文献   

19.
ABSTRACT: To utilize Antarctic krill as functional food, protein hydrolysates were prepared by enzymatic hydrolysis. Their effects on the state of water in myofibrils of lizard fish and dehydration-induced denaturation were compared with those from two species of shrimp, glucose, and sodium glutamate. Peptides are major components in hydrolysates, occupying approximately 85–93% of the total materials. The Antarctic krill protein hydrolysates stabilized the bonding of water molecules, leading to suppressed denaturation of myofibrils during the dehydration process. Similar effects were observed for shrimp protein hydrolysates. The effect of the hydrolysate was less than that by glucose and sodium glutamate.  相似文献   

20.
ABSTRACT:   Myosin rod regions prepared from carp Cyprinus carpio dorsal muscle and scallop Pecten yessoensis striated adductor muscle were non-enzymatically reacted with glucose (glycation), and the changes in the filament-forming ability and the size distribution of the rod filaments during glycation were examined to discuss the molecular mechanism of the water solubilization of myosin molecules under physiological conditions. Both myosin rods became solubilized in 0.1 M NaCl (pH 7.5), and their filament-forming ability was weakened with the progress of glycation. The size of the insoluble filaments of the myosin rods was diminished with an increase in the solubility under physiological conditions, and glycated myosin rods finally existed as monomers in 0.1 M NaCl (pH 7.5). These results supported the hypothesis that the water solubilization of myosin by glycation was caused by the loss of the filament-forming ability of myosin molecules. Water solubilization seemed to occur through the same molecular mechanism regardless of the species, whereas the scallop myosin rods required a much larger number of lysine residues reacted with glucose to collapse the insoluble filaments, in contrast to the carp myosin rods.  相似文献   

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