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1.
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   

2.
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   

3.
The effect of different thawing methods—running water, microwave, slack water (25°C), air (25°C), and refrigerator (4°C)—and multiple freeze-thaw cycles (0, 1, 3, and 5) on the quality of common carp were investigated. Microwave thawing showed the lowest score for sensory assessment and the highest cooking loss (p < 0.05), while 4°C refrigerator thawing showed less thawing loss and cooking loss but required the longest thawing time. Ca2+-ATPase activity and sulfhydryl content of air thawing were lower (p < 0.05), while no significant differences were observed among other thawing methods. Water loss and the thiobarbituric acid reactive substances (TBARS) value increased (p < 0.05) when freeze-thaw cycles increased. The sensory scores and hardness decreased significantly when the freeze-thaw cycles increased (p < 0.05). A significant decrease (p < 0.05) was observed in salt-extractable protein content after five freeze-thaw cycles. Different thawing methods affected the quality of common carp. Frozen common carp subjected to freeze-thaw cycles resulted in accelerated lipid and protein oxidation and caused mechanical damage to muscle tissues.  相似文献   

4.
红藻糖苷的提取及其对草鱼鱼糜抗冻性能的影响   总被引：1，自引：0，他引：1  
为探讨红藻糖苷的醇提工艺以及红藻糖苷对冷冻草鱼鱼糜蛋白变性作用的影响,首先采用响应面分析法对乙醇浓度、提取温度、时间和液料比4个因素进行优化,随后以冷冻鱼糜的盐溶性蛋白含量、巯基含量及肌原纤维蛋白Ca~(2+)-ATP酶活性等参数为指标,探测冷冻草鱼鱼糜在冷藏过程中添加红藻糖苷对蛋白质变性作用的影响。结果显示,红藻糖苷的最佳醇提条件为乙醇72.3%、提取温度60°C、时间4 h、液料比14∶1(m L/g),在此条件下的提取率为3.46%;抗冻性能结果显示,随红藻糖苷浓度升高,抗冻效果增强;以10%红藻糖苷处理冷冻鱼糜4周后,盐溶性蛋白含量和巯基含量分别比空白组高30.62%、32.80%,肌原纤维蛋白的Ca2+-ATP酶活性的下降率比空白组低37.51%,解冻失水率的增长率比空白组低133.07%。研究表明,红藻糖苷能有效延缓草鱼鱼糜肌原纤维蛋白的冷冻变性。  相似文献   

5.
The cryoprotective effects of trehalose on fish myofibrillar protein were compared with those of sucrose, glucose and sorbitol. The frozen surimi with trehalose exhibited significantly higher Ca2+-ATPase activity through-out the storage periods, resulting in higher gel-forming ability than that of without trehalose. The amount of unfrozen water was significantly increased in the surimi upon addition of trehalose at any concentrations tested. The findings suggest that trehalose constructed bound water molecules in protein structure, consequently suppressed freeze-induced denaturation of protein and maintained gel-forming ability. An addition of 5.0% to 7.5% concentration of trehalose showed threshold behavior to increase the amount of unfrozen water and to prevent freeze-induced denaturation of protein. The effects of trehalose were almost similar to those of other sugars.  相似文献   

6.
ABSTRACT

The conformational changes of natural actomyosins prepared from fresh and freeze-thaw tilapia (Oreochromis niloticus) in the presence of Ca2+ or Mg2+ were investigated. The Ca2+-activated adenosine triphosphatase (Ca2+-ATPase) activities of actomyosins extracted from fresh and freeze-thaw fish were comparable (p > 0.05). The denaturation temperatures (Td) of actomyosins extracted from fresh fish were lower than those from freeze-thaw counterparts (p < 0.05). The addition of Ca2+ or Mg2+ reduced the Td of actomyosins. Ca2+ and Mg2+ enhanced protein aggregation at ≥ 40°C (p < 0.05). Based on the sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) pattern, the myosin heavy chain (MHC) and actin bands tended to form large aggregates to a greater extent in the presence of 100mM Ca2+ or Mg2+. Ca2+ and Mg2+enhanced disulfide linkages and hydrophobic interactions among actomyosin molecules. The onset temperature of elastic modulus (G′) of both actomyosins was shifted to lower temperature as 100mM of Ca2+ or Mg2+ was added. Mg2+ at 20mM increased the breaking force of washed tilapia mince at 40°C. Our results revealed that the intrinsic properties of actomyosins extracted from fresh and frozen fish were distinct, and divalent ions Ca2+ or Mg2+ affected their gelation differently.  相似文献   

7.
The effect of freezing and frozen storage of threadfin bream fish (Nemipterus japonicus) meat on the setting and gel-forming ability has been evaluated. The dynamic viscoelastic properties of fish meat during setting and thermal gelation process were evaluated using Controlled Stress Rheometer under oscillatory mode. A sharp decrease in setting ability was recorded immediately after freezing as revealed by storage modulus (G?) values. The transglutaminase (TGase) enzyme activity of fish meat decreased from the initial value of 81.09 to 51.46 U/g meat/min at the end of 200 days of frozen storage. A decrease in setting ability of fish meat beyond 160 days of frozen storage is probably related to lower TGase enzyme activity. The gel-forming ability was related to setting ability during the frozen storage period. Although the protein solubility showed a decreasing trend during 200 days of frozen storage, the decrease was not significant. The effect of freezing and frozen storage on calcium-activated adenosine triphosphatase (Ca2+-ATPase) enzyme activity of fish mince was significant (P < 0.05). A reduction in protein solubility and Ca2+-ATPase enzyme activity is an indication of aggregation/denaturation of myofibrillar proteins.  相似文献   

8.
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   

9.
虾夷扇贝闭壳肌和外套膜肌原纤维蛋白的特性分析   总被引：4，自引：2，他引：2  
吴忠  刘俊荣  田元勇 《水产学报》2015,39(11):1640-1649
为探索采捕后活品虾夷扇贝品质变化与其肌肉蛋白质生理特性变化间的关联,本研究以虾夷扇贝2个可食部肌肉为研究对象,以肌原纤维蛋白ATPase活性为指标(Ca2+-ATPase,Mg2+-ATPase),对扇贝肌原纤维蛋白(Mf)的稳定性进行了系统探索。首先,分别提取闭壳肌肌原纤维(A-Mf)和外套膜肌原纤维(M-Mf);然后,考察了不同因素(离子强度I、pH、温度)对Mf的ATPase活性的影响规律;对A-Mf及M-Mf的稳定性进行了探索;进一步比较了闭壳肌和外套膜肌原纤维蛋白ATPase的失活特性。研究结果表明:(1)虾夷扇贝闭壳肌与外套膜的Mf的理化性质相似,A-Mf与M-Mf的pI均在5.0附近,粘度分析发现A-Mf热稳定性高于M-Mf。(2)ATPase活性变化规律的结果发现,与脊椎动物中的鱼类一样,作为无脊椎动物的扇贝,与Mg2+-ATPase相比,Ca2+-ATPase更能准确地反映Mf的稳定性。(3)闭壳肌和外套膜二者的Mf的Ca2+-ATPase呈现出共同特性,在pH为中性时活性最高;A-Mf与M-Mf的差异性则表现为前者的Ca2+-ATPase在较低离子强度(I=0.2)下活性最高,后者则在较高离子强度(I=0.5)下活性最高;离子强度对A-Mf的热稳定性影响不明显,而M-Mf的热稳定性明显受到离子强度的影响,其在较低离子强度下表现出更好的稳定性。(4)Ca2+-ATPase失活速率的研究发现,无论是闭壳肌还是外套膜,其稳定性与离子强度I和温度均呈现显著正相关(R2=0.8181、0.8436和R2=0.9887、0.9557);二者在pH 7.0左右的稳定性最好,偏离中性会促使Ca2+-ATPase失活,与碱性条件相比,酸性对蛋白质稳定性的破坏更加明显。  相似文献   

10.
This study was aimed to determine the effects of phosphate compound substitutions (sodium bicarbonate and xanthan gum) and preparation methods—headed, gutted whole fish, and mince; fresh and after frozen storage (?20°C for 3 months)—on Nile tilapia mince qualities. Results showed that bicarbonate (0.3% with 8% sucrose/sorbitol) is an efficient phosphate compound replacement as evidenced by the comparative values of salt extractable protein, Ca2+-ATPase activity, total sulfhydryl content, and textural properties to those of the phosphate-added—0.3% sodium tripolyphosphate (STPP) with 8% sucrose-sorbitol—sample after 3-month frozen storage (p > 0.05). Both cryoprotected samples containing STPP or bicarbonate exhibited higher denaturation temperatures of myosin than others. Xanthan gum (0.5%) could neither stabilize the biochemical and physicochemical properties of mince during 3-month frozen storage nor improve textural properties of gel from frozen whole fish.  相似文献   

11.
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   

12.
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   

13.
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   

14.
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   

15.
研究鲢(Hypophthalmichthys molitrix)在冷冻-解冻过程中的品质变化规律。鲢于–18℃条件下冻藏10 d,流水解冻后再贮藏于–18℃条件下,5 d后解冻,共反复冷冻-解冻5次。在解冻1、3、5次后随机取3条鲢测定其解冻损失、蒸煮损失、硬度、咀嚼性、恢复性、硫代巴比妥酸(TBA)值、L*值、b*值、盐溶性蛋白(SSP)含量、Ca2+-ATP酶活性、总巯基含量、表面疏水性和感官值等指标,评价反复冷冻-解冻对鲢品质的影响。结果表明,在第1次冷冻-解冻时,硬度、咀嚼性、恢复性、盐溶性蛋白(SSP)含量和Ca2+-ATP酶活性与鲢初始值相比显著降低(P<0.05),b*值和表面疏水性显著升高(P<0.05);解冻损失、L*值和TBA值在第3次冷冻-解冻时显著上升(P<0.05);总巯基含量在第5次冷冻-解冻时显著下降(P<0.05);而蒸煮损失在冷冻-解冻过程中没有显著变化(P>0.05);感官值在第5次冷冻-解冻时为47,感官品质已不可接受。各指标变化表明,鲢品质会随着反复冷冻-解冻次数增加而下降,在运输、贮藏和销售过程中要防止温度波动,避免反复冻融对鲢品质造成不利影响。  相似文献   

16.
ABSTRACT

In the present study, investigated were the preparation of water-soluble chitosan (WSC) by hydrolysis of original chitosan with commercial α-amylase and the suppressive effect of WSC on denaturation of bay scallop adductor muscle myofibrillar protein (Mf) during frozen storage at ?18°C for 12 months. The WSC (2.5- to 10-g dry weight) was added to 100 g of the Mf, and the changes in the Ca-ATPase activity, solubility, and sulfhydryl content were examined during frozen storage. The addition of WSC significantly reduced the denaturation of the Mf Ca-ATPase. Moreover, a significant increase in Mf solubility and sulfhydryl content was observed in the WSC-treated bay scallop adductor muscles compared with the control (p < 0.05) during frozen storage at ?18°C.  相似文献   

17.
复合鱼肉肌原纤维蛋白加热过程中理化特性变化的研究   总被引：2，自引：0，他引：2  
考察了鲢(Hypophthalmichthys molitrix)、小黄鱼(Pseudosciaena polyactis)及其以质量比1∶1复合的肌原纤维蛋白的浊度、Ca2+-ATPase活性和巯基含量在加热过程中的变化规律。结果显示:随着加热温度的升高,三种蛋白溶液的浊度呈S型曲线增加。复合肌原纤维蛋白的增加模式与小黄鱼肌原纤维蛋白的增加模式相似,不同于鲢肌原纤维蛋白的增加模式。鲢肌原纤维蛋白和小黄鱼肌原纤维蛋白的Ca2+-ATPase活性随温度的升高逐渐下降。复合肌原纤维蛋白的Ca2+-ATPase活性在20～35℃略有上升,而后剧烈下降,55℃时活性完全丧失。复合肌原纤维蛋白的总巯基含量随着加热温度的升高呈下降趋势。当温度在30～60℃时下降缓慢,高于65℃时剧烈下降。  相似文献   

18.
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   

19.
The objective of the present study was to confirm previous results on the mediation of GnRH signal in tilapia by providing evidence from experiments in cultured pituitary cells and from perifusion experiments using a GnRH-antagonist. After 4 days in culture under identical conditions, cells taken from pituitaries of fish maintained at 26°C were more sensitive to GnRHa ([D-Ala6, Pro9-NEt]-LHRH) than those taken from fish maintained at 19°C. Cells from female pituitaries were more responsive than those from males. taGTH release in culture was augmented by Ca2+ ionophore (A23187; 1–100 μM) or ionomycin (0.02–10 μM). The response of perifused pituitary to GnRH was reduced by nimodipine (1–10 μM) indicating that Ca2+ influx via voltage-sensitive Ca2+ channels is involved in the stimulation of GTH release. Activation of protein kinase C by OAG (1-oleyl-2-acetyl glycerol; 0.16–160 μM) or TPA (1-O-tetra-decanoyl phorbol-13-acetate; 1.25–125 nM) resulted in a dose-dependent stimulation of taGTH release from cultured cells. Arachidonic acid (0.33–330 μM) also augmented the release of taGTH from the culture. Four sequential pulses of sGnRH (100 nM) at 2h intervals resulted in surges of taGTH release from perifused pituitary fragments; the surges were similar in magnitude with no signs of desensitization. Sequential stimulation with graded doses of sGnRH (0.1 nM to 1 μM) in the presence of GnRH-antagonist ([Pro2,6, Trp3]-GnRH) resulted in an attenuation of taGTH release. However, the GnRH-antagonist did not alter the pattern of forskolin-stimulated GTH release, indicating that forskolin stimulation is exerted at the level of the adenohypophyseal cells. It is concluded that, as in other vertebrates, the transduction of GnRH stimulation of GTH release involves Ca2+ influx through voltage-sensitive Ca2+ channels, mobilization of the ion from intracellular sources, arachidonic acid and activation of PKC. Adenylate cyclase-cAMP system us also involved in the mediation but its relationship with other transduction cascades requires further investigations.  相似文献   

20.
The present study investigated physicochemical and protein structural changes in common carp muscle subjected to different freeze–thaw (FT) cycles. With increasing number of FT cycles, the thawing losses, cooking loss, L*- and b*-value increased, and shear forces and a*-value decreased (p < 0.05). The study showed that multiple FT processes were detrimental to color and water-holding capacity of carp muscle. The increases in thiobarbituric acid reactive substances and carbonyl content with concomitant decrease in sulfhydryl group content (p < 0.05) showed that multiple FT caused carp lipid and protein oxidation, especially for the carp muscle subjected to five freeze–thaw cycles. Myofibrillar protein isolated from FT muscle showed an increased hydrophobicity, reduced ATPase activity, and enhanced susceptibility to thermal aggregation (p < 0.05). These protein structural changes resulted in major losses in muscle quality. Overall, the disrupted protein structure, together with the denaturation of myofibrillar protein induced by FT, was most likely associated with lowered muscle quality.  相似文献   

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