Postmortem Changes in the Adductor Muscle of Scallop (Chlamys tehuelchus) in Chilled and Frozen Storage

Abstract

The effects of freezing and frozen storage on the biochemical properties of scallop adductor muscles stored at 2-4EC were investigated. Glycogen content fell 40% in the first 12 hr of chilled storage and decreased slowly thereafter. ATP content increased for a short time after death and then decreased slowly. Glycogen and ATP degradation was accompanied by a decrease in both pH and 260/250 absorbance ratio of scallop muscle extracts. A significant increase (p < 0.05) in the hypoxanthine (Hx) content was also observed in chilled stored adductor muscles. Adductor muscles showed a significant decrease (p < 0.05) in the 260/250 absorbance ratio of extracts and an increase in the Hx level after freezing. An increase in Hx content was observed during frozen storage of adductor muscles frozen immediately after processing. Expressible juice increased with freezing and frozen storage of the muscles. The results shown in this paper indicate a rapid loss of quality in scallop adductor muscles during storage at 2-4. Freezing and frozen storage enhanced the quality deterioration of the muscles.     

Antibrowning of the Adductor Muscles of Bay Scallop by Glutathione During Hot Air Drying

ABSTRACT

Browning in the adductor muscle of bay scallop (Argopecten irradians) tends to occur during hot air drying due to polyphenoloxidase (PPO) and Maillard reaction and decreases the sensory quality and commercial value of bay scallop adductor muscles (BSAM). In the present study, the effects of glutathione on the browning inhibition of BSAM were evaluated. The PPO activity in BSAM was inhibited by 97.8 with 0.08% glutathione. The browning of BSAM pretreated with glutathione was evaluated during hot air drying. Compared with the control, BSAM pretreated with glutathione resulted in less drying time and browning during hot air drying. The results indicate that pretreatment with glutathione may be a promising method of BSAM browning inhibition during hot air drying.     

Effects of Partial and Complete Replacement of Synthetic Cryoprotectant with Carrot (Daucus carota) Concentrated Protein on Stability of Frozen Surimi

ABSTRACT

The study aimed to evaluate the effects of carrot concentrated protein (CCP) as additive on the functional and textural properties of surimi from striped catfish (Pangasianodon hypophthalmus) during six months of frozen storage (?20°C). The CCP (82.22% crude protein) was used as an additive either a lone or with a synthetic cryoprotectant (sucrose-sorbitol-sodium tri-polyphosphate). Control was made with synthetic cryoprotectant only. Molecular weight of CCP was found to be 36 kDa. After six months, the results revealed that up to 50% of synthetic cryoprotectants could be replaced by CCP during frozen storage of surimi. Biochemical parameters such as protein solubility, Ca²⁺ATPase activity, and gel strength decreased significantly (p < .05) during storage. Treatment T-3 (CCP 0.5% + 50% of synthetic cryoprotectant) maintained quality of protein significantly superior (p < .05) in respect to denaturation and other functional and sensory attributes compared to all the treatments. The microstructure images of surimi confirmed that addition of CCP modified the ice crystal growth during frozen storage. This study suggests that CCP can be a potential additive to protect protein from denaturation along with partial replacement of chemical cryoprotectants.     

Myosin denaturation in heated myofibrils of scallop adductor muscle

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⁺.     

Effects of Bicarbonate,Xanthan Gum,and Preparation Methods on Biochemical,Physicochemical, and Gel Properties of Nile Tilapia (Oreochomis niloticus Linn) Mince

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.     

Effect of Cryoprotectants on Suppression of Protein Structure Deterioration Induced by Freeze-thaw Cycle in Pacific White Shrimp

This study aimed to elucidate the changes in Pacific white shrimp (Litopenaeus vannamei) myofibrillar protein as influenced by multiple freeze-thaw cycles as well as the stabilization effects of sucrose and trisodium citrate on shrimp myofibrils. Shrimp myofibrils in 0.1 M NaCl, 20 mM Tris-HCl (pH 7.5) were mixed individually with sucrose and citrate at concentrations of 0.05 M and were evaluated for Ca²⁺-ATPase activity, salt solubility, total and reactive sulfhydryl, and surface hydrophobicity during three freeze-thaw cycles. Sucrose and citrate had strong cryoprotective effects against freeze denaturation by retaining higher Ca²⁺-ATPase activity and salt-soluble myosin and actin, by slowing the reduction of reactive sulfhydryl (SH) and by exposing less hydrophobic groups at the surface of the protein compared with the no-additive sample. Results indicated that both cryoprotectants had suppressive effect against protein denaturation and helped stabilize white shrimp myofibrillar protein during the freeze-thaw process. This study suggests that sucrose and citrate stabilized the protein structure by retarding the unfolding of protein; thus, the native protein could be protected during frozen storage.     

Effects of Chilled Storage,Freezing Rates,and Frozen Storage Temperature on Lipid Oxidation in Meat Blocks from Cultured Bluefin Tuna Thunnus thynnus

ABSTRACT

The effects of a short chilled storage period before freezing, frozen storage temperature, and freezing rate on lipid oxidation of bluefin tuna (Thunnus thynnus) meat during frozen storage were investigated. After 12-months storage, all samples had increased in peroxide value though they were less at the lower temperatures (?45 and ?60°C). Peroxide values in all samples stored at ?20°C increased after 3 months storage, particularly those processed and stored 51 h after harvest. The lowest increase in peroxide value occurred in the samples frozen rapidly 3 h after harvest. Vitamin E levels decreased faster during frozen storage at ?20°C. There were no apparent differences in levels of triacylglycerides nor in n-3 fatty acid levels between treatments, storage periods, and storage temperatures. After 12-months storage, headspace oxidative volatiles were highest in samples stored at ?20°C and lowest in those stored at ?60°C. Lipid oxidation in tuna meat stored at ?45°C is similar to that at ?60°C, and rapid freezing rather than slow freezing should be used.     

鳙肌肉蛋白质生化特性在冻藏过程中的变化

以肌动球蛋白的盐溶性、肌原纤维蛋白ATPase活性以及肌原纤维蛋白的巯基含量为指标,研究了鳙肌原纤维蛋白在-10℃,-20℃,-30℃和-40℃下冻藏时的变性情况。结果表明,在不同温度下冻藏时,鳙肌动球蛋白的盐溶性、肌原纤维蛋白的ATPase活性以及巯基含量随着冻藏时间的延长,均呈下降趋势。但是,鳙蛋白质的变性速度在不同冻藏温度下的差异是极其显著的(P<0.01)。冻藏温度越低,变性越缓慢。     

Cryoprotective effects of shrimp head protein hydrolysate on gel forming ability and protein denaturation of lizardfish surimi during frozen storage

ABSTRACT:   The effects of shrimp head protein hydrolysate (SHPH) from three species of shrimp (northern pink shrimp [ Pandalus eous ], endeavour shrimp [ Metapenaeus endeavouri ], black tiger shrimp [ Penaeus monodon ]) on gel forming ability and protein denaturation of lizardfish surimi during frozen storage at −25°C were evaluated. The quality of lizardfish surimi with 5% (dried matter) of any of the three SHPH or sodium glutamate (Na-Glu) was examined in terms of gel strength, whiteness, Ca-ATPase activity and the amount of unfrozen water, comparing with those of surimi without additive as the control. The residual Ca-ATPase activity and gel strength of surimi with SHPH were higher than those of the control throughout 180 days of frozen storage, regardless of shrimp species. The highest effect was found in surimi with Na-Glu. The gel strength and Ca-ATPase activity found a high positive correlation. The addition of SHPH to surimi also increased the amount of unfrozen water by approximately 1.29–1.36 fold higher than the control, however kamaboko gels of the control was significantly whiter. From these results, freeze-induced denaturation of lizardfish muscle protein could be lessened by the addition of SHPH, resulting in a high gel strength and Ca-ATPase activity.     

Setting Ability of Threadfin Bream (Nemipterus japonicus) Meat as Affected by Freezing and Frozen Storage with Special Reference to Transglutaminase Enzyme Activity and Rheological Properties

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.     

不同冻藏温度下鲈鱼肌肉胶原蛋白生化特性的变化

研究了鲈鱼在-10℃,-20℃,-30℃和-40℃冻藏过程中胶原蛋白生化特性的变化。通过胶原蛋白的溶出量和SDS-PAGE法分析了鲈鱼在冻藏过程中的胶原蛋白变化情况。结果表明,胶原蛋白在冻藏过程中其溶出量呈波浪变化,但总体上是下降的。其原因可能是在冻藏过程中胶原分子发生凝聚以及胶原分子降解产生的小分子胶原在碱洗过程中溶出而失去。SDS-PAGE的结果证实了胶原蛋白在冻藏过程中确实发生了降解。冻藏温度之间的差异是显著的(P<0.05)。冻藏温度越低,胶原蛋白变化越缓慢。     

Myosin and actin denaturation in frozen stored kuruma prawn Marsupenaeus japonicus myofibrils

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.     

Crosses between two subspecies of bay scallop Argopecten irradians and heterosis for yield traits at harvest

In order to improve the yield of bay scallop Argopecten irradians by exploiting geographic subspecies heterosis, crosses between and within two subspecies, the northern A. i. irradians (Lamarck) and the southern A. i. concentricus (Say), were created and the offspring were cultured under the same environmental conditions. The two parental populations were collected from Bohai Bay in northern China and Beibu Bay in southern China, which were distinct in particular shell colours. The results indicated that the shell colour of bay scallop was inheritable and could be used as a morphological mark to distinguish hybrid and purebred individuals. At harvest, hybrid offspring always produced a significantly higher yield than purebred offspring. Positive heterosis was achieved for shell length, shell height, shell width, total weight and adductor weight, which was 5.02, 5.22, 3.88, 7.53 and 9.47 respectively. Hybrid gain was 10.86% for shell length, 10.48% for shell height, 9.77% for shell width, 34.90% for total weight and 41.69% for adductor weight, respectively, and all were significantly >5%. The present study reveals that it is effective for improving yield by hybridization between different geographic subspecies in the bay scallop.     

Effect of shrimp head protein hydrolysates on the state of water and denaturation of fish myofibrils during dehydration

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.     

Effects of Freezing and Frozen Storage on Protein Functionality and Texture of Some Cephalopod Muscles

The aim of this study was to investigate the effects of freezing and frozen storage on protein functionality and texture of squid (Loligo vulgaris), octopus (Octopus vulgaris), and cuttlefish (Sepia officinalis) muscles. Squid, octopus, and cuttlefish samples were cut into pieces of 4 × 4 cm. These pieces were packed in polyethylene bags. The bags were frozen in a blast freezer at ?45°C until the thermal center reached ?18°C. Frozen samples were stored in a deep freezer at ?18°C for 30 days. After freezing and during frozen storage, total soluble protein and water holding capacity decreased and total free amino acid and cooking loss increased in all cephalopod muscles. According to instrumental texture analysis results, freezing and frozen storage affected textural characteristics of squid and cuttlefish but not of octopus. Sensory hardness and chewiness values of all cephalopods increased after freezing, but elasticity values did not change. There were no significant differences between storage days in hardness values of squid and octopus. However, significant differences in hardness values of cuttlefish were observed between the 1st day of storage and the last day.     

Influence of Previous Washing Process and Storage Time on Chemical Composition and Sensory Quality of Thai Pangas (Pangasius sutchi) Minced Muscle During Frozen Storage

ABSTRACT

This work focuses on the effect of a washing process followed by frozen storage (3 months; ?18°C) on the quality of minced pangas muscle. A previous washing step has led to a positive effect on fish quality according to marked decreases in expressible moisture (28%), volatile amines (25.7%), free fatty acids (24.5%), and thiobarbituric acid reactive substances (29%). However, such indexes showed quality loss throughout the frozen storage. Amongst quality indexes, special attention should be given to the expressible moisture value and the water holding capacity, as being closely related to the gel-forming ability in order to obtain surimi-type commercial products.     

Effects of Whitening Agents and Frozen Storage on the Quality of Sardine (Sardina pilchardus) Surimi: Physicochemical and Mechanical Properties

This work is focused on the effect of using whitening agents (WA) during a process followed by frozen storage (4 months at ?18°C) on the whiteness, quality parameters, and mechanical properties of sardine surimi. The whiteness of surimi exhibited a significant improvement when whitening agents (calcium carbonate and peroxide hydrogen) were used (48.75 to 60.24). Dynamic rheological measurement showed that storage moduli, G′, was considerably higher than loss moduli, G″, for both surimi with WA and control; however, the highest viscoelastic moduli were found in the treated surimi. In addition, the microstructure of surimi with WA showed more compact matrix and higher water holding capacity. On the other hand, most tested indexes showed quality losses throughout the frozen storage in both samples. Proteins underwent denaturation as indicated by the reduction in band intensities, especially myosin heavy chain (MHC) bands. Peroxide value (PV) and thiobarbituric acid reactive substances (TBARS) measurements showed that lipid oxidation took place during storage; however, the degree of lipid oxidation was not relevant. Therefore, it was proved that the addition of whitening agents had a marked effect on the production of surimi with better functional attributes including whiteness, water holding capacity, and mechanical properties.     

虾夷扇贝闭壳肌和外套膜肌原纤维蛋白的特性分析

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。     

红藻糖苷的提取及其对草鱼鱼糜抗冻性能的影响

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。     

不同规格虾夷扇贝捕后耐干露特性比较

为探究商品虾夷扇贝规格与其活品耐藏特性之间的关联,对春季上市虾夷扇贝的规格及质量进行分组,再将各组置于4 ℃下湿布覆盖进行3 d冷却干露贮藏,分别于0、1、2 d和3 d采样进行生化代谢指标分析。试验结果显示,市售春季虾夷扇贝依据壳长大致可分成(105.8±1.5) mm、(98.4± 2.3 ) mm及(90.5±1.7) mm 3个规格组,各规格单贝质量相差20~30 g;(98.4±2.3) mm组扇贝的肥满度及闭壳肌出成率较其他两组高,(90.5±1.7) mm组三磷酸腺苷初始含量最高,表明其捕后胁迫耐力好于较大规格扇贝,(90.5±1.7) mm组扇贝同样表现出更好的耐干露特性,干露3 d 三磷酸腺苷含量和核苷酸能荷均明显优于其他两组;糖原含量各组无明显差异。此外,各组扇贝冷却干露2 d后存活率均为100%,干露至第3 d各组开始出现死亡,其中(90.5±1.7) mm组扇贝耐干露特性最好;各组闭壳肌pH与体腔液pH差异不显著;氨基酸分析结果发现,甘氨酸和精氨酸是扇贝闭壳肌游离氨基酸中含量最丰富的氨基酸,其余游离氨基酸变化趋势不明显;体腔液含氮物中,氨含量较高,其余氨基酸含量均较低并在干露期间无明显变化趋势。