低温贮藏中华管鞭虾肌肉品质及组织蛋白酶H活性变化

为探究不同贮藏条件下中华管鞭虾组织蛋白酶H活性及肌肉品质的变化情况,以中华管鞭虾为对象,分别在冷藏（4 ℃,0~6 d）和冻藏（?18 ℃,0~120 d）条件下,比较分析完整虾组和去头虾组肌肉pH、持水力、硬度、弹性、肌原纤维蛋白含量、水分含量及各亚细胞分级中组织蛋白酶H活性等指标的变化。结果表明,随着贮藏时间的延长,整虾和去头虾肌肉pH均不断升高,但去头虾组pH升高幅度略低于完整虾组;虾肉中肌原纤维蛋白含量随贮藏时间延长而逐渐降低,完整虾组和去头虾组在冷藏至6 d时分别降低了38.32%和30.88%,在冻藏至120 d时分别减低了61.67%和52.09%;在整个冻藏过程中,两组虾的硬度和弹性均出现先上升后下降的趋势,而冷藏贮藏过程中则始终呈现下降趋势;组织蛋白酶H在不同亚细胞分级中活性变化不同,冻藏条件下两组虾组织蛋白酶H酶活整体低于冷藏条件下酶活,且完整虾组组织蛋白酶H活性整体高于去头虾组。综上,在低温贮藏过程中,相比于完整虾形式,以去头虾的贮藏方式更有利于对虾肌肉品质的保障,且组织蛋白酶H活性受贮藏温度影响较大。研究结果为不同贮藏方式下中华管鞭虾理化特性及组织蛋白酶活性变化提供了理论基础。     

Superchilled,chilled and frozen storage of Atlantic mackerel (Scomber scombrus) fillets – changes in texture,drip loss,protein solubility and oxidation

Changes in quality characteristics in relation to protease activity and protein oxidation in chilled, superchilled and frozen mackerel fillets during storage were studied. The solubility of sarcoplasmic proteins was quite stable in mackerel samples for all storage experiments, whereas the solubility of myofibrillar proteins decreased in both superchilled and frozen samples. A significant correlation (r = 0.983, P < 0.05) between the increased activity of cathepsin B+L in chilled fillets and softening of the fish flesh during storage was revealed. Contrary with chilled samples, the texture of superchilled mackerel fillets became tougher along the storage period, which can be explained by a higher rate of myofibrillar oxidation (r = 0.940, P < 0.05). The hardness and drip loss decreased slightly at the end of frozen storage. Superchilling preserved the quality of mackerel fillets with the least side effects in relation to protein solubility, drip loss and softening of the fish tissue as compared to chilled and frozen storage.     

Effects of Chilling and Partial Freezing on Rigor Mortis Changes of Bighead Carp (Aristichthys nobilis) Fillets: Cathepsin Activity,Protein Degradation and Microstructure of Myofibrils

To investigate the effects of chilling and partial freezing on rigor mortis changes in bighead carp (Aristichthys nobilis), pH, cathepsin B, cathepsin B+L activities, SDS‐PAGE of sarcoplasmic and myofibrillar proteins, texture, and changes in microstructure of fillets at 4 °C and –3 °C were determined at 0, 2, 4, 8, 12, 24, 48, and 72 h after slaughter. The results indicated that pH of fillets (6.50 to 6.80) was appropriate for cathepsin function during the rigor mortis. For fillets that were chilled and partially frozen, the cathepsin activity in lysosome increased consistently during the first 12 h, followed by a decrease from the 12 to 24 h, which paralleled an increase in activity in heavy mitochondria, myofibrils and sarcoplasm. There was no significant difference in cathepsin activity in lysosomes between fillets at 4 °C and –3 °C (P > 0.05). Partially frozen fillets had greater cathepsin activity in heavy mitochondria than chilled samples from the 48 to 72 h. In addition, partially frozen fillets showed higher cathepsin activity in sarcoplasm and lower cathepsin activity in myofibrils compared with chilled fillets. Correspondingly, we observed degradation of α‐actinin (105 kDa) by cathepsin L in chilled fillets and degradation of creatine kinase (41 kDa) by cathepsin B in partially frozen fillets during the rigor mortis. The decline of hardness for both fillets might be attributed to the accumulation of cathepsin in myofibrils from the 8 to 24 h. The lower cathepsin activity in myofibrils for fillets that were partially frozen might induce a more intact cytoskeletal structure than fillets that were chilled.     

Effect of severing skeletal muscle at different stage of rigor on the quality of pacific white shrimp (Litopenaeus vannamei)

Effect of severing skeletal muscle (by beheading) at different stages of rigor on the quality of pacific white shrimp (Litopenaeus vannamei) during ice storage was assessed by physical, chemical, and sensory evaluation. Shrimps were divided into three lots, one lot (T₁) beheaded immediately after killing, 2nd (T₂), and 3rd (T₃) lots were beheaded after 5 h and 35 h post‐mortem corresponding to pre‐rigor, in‐rigor, and post‐rigor stages, respectively. There was an increase in the moisture content in all the treatments during the storage. PV, TVB‐N, and TMA‐N values also increased with the storage time, though the values of all these parameters were well within the acceptable limits. Total protein, Sarcoplasmic protein, NPN, and water holding capacity showed a decreasing trend in all the treatments. Hardness, springiness, cohesiveness and chewiness values did not differ significantly (p ≤ .05) between the treatments. L* value showed a decreasing trend throughout the study. Information provided in this study can serve as baseline for postharvest preservative treatments of crustacea products.

Practical applications

This work examined the effect of the time of beheading on the quality of shrimps in ice storage. No work ever looked at the possibility of whether the quality of shrimp varies if its skeletal muscle is severed (by beheading) during pre‐rigor, on‐rigor, and post‐rigor stages. The ice storage studies of three lots demonstrated similar deterioration of quality, without significant differences among the lots. This strongly suggests that the transportation of the whole shrimps to a processing factory at a distant site provides no comparative advantage in terms of quality.     

BIOCHEMICAL AND MORPHOLOGICAL CHANGES IN GRASS SHRIMP (PENAEUS MONODON) MUSCLE FOLLOWING FREEZING BY AIR BLAST AND LIQUID NITROGEN METHODS

Grass shrimp (Penaeus monodon) at prerigor stage were frozen at rates ranging from 3.41 to 16.1 cm/h by using an air blast freezer at –35C or a liquid nitrogen freezer at – 80, – 100 and – 120C. Immediately after freezing, the spacing between muscle fiber bundles was larger (21.3 ± 5.7 μm) in shrimp frozen at 3.4 cm/h than in shrimp frozen at 8.6 ～ 16.1 cm/h (6.0 ± 0.6 to 8.8 ± 1.1 μm, respectively). The spacing between fibers increased during frozen storage at – 20C and remained different for slow and fast frozen samples within 4 weeks. The lysosomal fraction from fresh shrimp had more cathepsin D-like activity (187 units/mg protein) than that from shrimp frozen at 10.2 cm/h (179 units/mg protein) and at 3.4 cm/h (86 units/mg protein). During frozen storage at – 20C the cathepsin D-like activity of intact lysosomes decreased and was negligible after 4 weeks. The solubility of muscle protein in 0.6 M KCl was not consistently different in samples frozen by different methods and stored at – 20C for 4 weeks. Liquid nitrogen freezing produced frozen shrimp of higher muscle integrity than air blast. But the differences disappeared after one-month storage at – 20C.     

盐浓度对冷藏即食中华管鞭虾肌肉品质的影响

以中华管鞭虾为研究对象,探究NaCl浓度（0%、2%、4%和6%）对即食中华管鞭虾仁冷藏期间肌肉品质变化的影响。在冷藏0、10、20、30、40和50 d时,比较不同组别中华管鞭虾肌肉色差、质构特性、水分含量、持水力、pH、挥发性盐基氮含量（TVB-N）、菌落总数、TBA值及组织微观结构的变化情况。结果表明,在冷藏过程中,相比于0%NaCl处理组（对照组）,4%和6%NaCl可以显著（P<0.05）抑制虾仁肌肉色泽和质构特性的劣化,延缓肌肉TVB-N含量和TBA值的增加及微生物的快速生长。冷藏期间,各NaCl处理组虾仁肌肉持水力随贮藏时间延长而显著上升（P<0.05）,且NaCl浓度越高虾仁肌肉持水力保持效果越好。随冷藏时间延长,各组虾仁肌肉水分含量呈先上升后下降趋势,而肌肉pH则先下降后上升,但添加NaCl使得虾仁肌肉水分含量和p H均显著低于对照组（P<0.05）。冷藏第40 d时,与对照组相比,NaCl浓度增加抑制了虾仁肌纤维组织的劣化,其中以4%NaCl处理虾仁肌肉组织结构保持较为完整,肌纤维组织排列较为紧密。综上,选用4%NaCl浸泡处理可以改善保持中华管鞭...     

Changes on enzymatic activity and on sarcoplasmic and myofibrillar proteins of frozen-stored hake (Merluccius merluccius) pre-treated by high pressure

High-pressure (HP) pre-treatments were applied on European hake (Merluccius merluccius) followed by a frozen accelerated experiment (−10 °C). A central composite design ranging pressure levels (150–450 MPa) and frozen storage time (0–150 days) was used, being evaluated the enzymatic activities and muscle proteins. Acid phosphatase and calpain activities decreased after 150 days of frozen storage (58%/56% and 38%/56% for non-/HP-treated samples, respectively). Cathepsin B showed higher reductions (98%) for longer storage times. Furthermore, HP and frozen storage did not affect significantly cathepsin D activity, only slightly decreasing at 169 MPa. Furthermore, HP seemed to not affect myofibrillar proteins, while sarcoplasmic proteins were clearly affected by HP and frozen storage time, resulting in a reduction of about 53% or 23% for 431 or 450 MPa, respectively. Thus, HP could be used to lowering the deleterious effect of proteases on frozen European hake.     

Superchilled,chilled and frozen storage of Atlantic mackerel (Scomber scombrus) – effect on lipids and low molecular weight metabolites

Quality changes in Atlantic mackerel fillets during superchilled, chilled and frozen storage focusing on lipid quality, colour and changes in low molecular weight metabolites relevant for quality and safety were studied. Low formation of oxidation products was observed in chilled (up to 7 days), superchilled (up to 14 days) and frozen storage (up to one year). Only slight formation of TBARS was measured in the samples which correlated with the increasing fillet yellowness. The profile of low molecular weight compounds, analysed by high-resolution NMR, showed clear grouping of the different samples according to both treatment and storage time. The increase in K-value was highest in the chilled samples, reaching a K-value of 93 ± 3% on day 5, exceeding the proposed limit of human consumption (80%) while superchilling reached a K-value of ca 90 % after 14 days. Frozen samples showed acceptable quality in the whole storage period.     

Comparison of the Cryoprotective Effects of Trehalose,Alginate, and Its Oligosaccharides on Peeled Shrimp (Litopenaeus Vannamei) During Frozen Storage

The cryoprotective effects of trehalose, alginate, and its oligosaccharides on peeled shrimp (Litopenaeus vannamei) during frozen storage was investigated by monitoring thawing loss, color, texture, myofibrillar protein content, Ca²⁺‐ATPase activity, and performing microscopic structural analysis. Data revealed significant (p < 0.05) inhibitory effects on thawing loss and textural variables (springiness and chewiness) in trehalose‐, alginate oligosaccharides‐, and sodium pyrophosphate‐treated shrimp compared with the control and alginate‐treated batches. L* values revealed that these saccharides had a positive effect on color stability during frozen storage. In addition, the results of chemical analyses showed that trehalose and alginate oligosaccharide treatments effectively maintained an increased myofibrillar protein content and Ca²⁺‐ATPase activity in frozen shrimp. In addition, hematoxylin & eosin staining and SDS‐PAGE confirmed that these cryoprotective saccharides slowed the degradation of muscle proteins and the damage to muscle tissue structures. Overall, the application of trehalose and alginate oligosaccharides to peeled frozen shrimp might maintain better quality and extend the commercialization of these refrigerated products.     

Broad‐spectrum inhibition of proteolytic enzymes by allicin and application in mitigating textural deterioration of ice‐stored grass carp (Ctenopharyngodon idella) fillets

The inhibitory effect of allicin on proteolytic enzymes and textural deterioration of ice‐stored grass carp (Ctenopharyngodon idella) fillets was investigated. The results of in vitro study showed that allicin inhibited the activity of cathepsin B, L and D, calpain and collagenase in crude extract of grass carp muscle. Among endogenous enzymes, cathepsin B, L and collagenase were the most susceptible to allicin. Proteolysis of myofibrillar proteins by either crude enzyme or cathepsin B and L was almost prevented by allicin when employed at a concentration higher than 100 mm . After storage of 21 days, shear force of fillets treated with allicin at 10–100 mm was 39–51% higher than that of control. Myofibrillar proteins of fillets during storage were well protected against degradation when allicin concentration increased to 100 mm , as evidenced by SDS‐PAGE. Therefore, allicin could be a potential broad‐spectrum inhibitor to retard softening of fish fillets via mitigating myofibrillar proteolysis by endogenous enzymes especially cathepsin B and L during ice‐storage.     

Application of Antifreeze Protein for Food Preservation: Effect of Type III Antifreeze Protein for Preservation of Gel-forming of Frozen and Chilled Actomyosin

Type III antifreeze protein (AFP) remarkably preserved Ca²⁺ ATPase activity of actomyosin during frozen and chilled storage. Under frozen conditions, AFP helped to retain the Ca²⁺ ATPase activity of actomyosin much higher than that of conventional cryoprotectants (sucrose‐sorbitol mixture). The Ca²⁺ ATPase activity increased with increasing AFP concentration and reached a maximum at 50g/L AFP. After 3‐d chilled storage, the Ca²⁺ ATPase activity of control and sucrose‐sorbitol samples had lost 80% and 50%, respectively, while the AFP samples remained unchanged. A Type III AFP mechanism based on freezing temperature depression (more unfrozen water) and inhibition of ice recrystallization that protects against the freezing of muscle proteins in chilled or frozen conditions is proposed.     

Quality changes during the frozen storage of sea bass (Dicentrarchus labrax) muscle after pressure shift freezing and pressure assisted thawing

Quality of frozen sea bass muscle stored (1, 3 and 5 months) at two levels of temperature (−15 and −25 °C) after a pressure shift freezing process (200 MPa) — PSF — and/or a pressure assisted thawing process (200 MPa) — PAT — was evaluated in comparison with samples frozen and thawed using conventional methods (air-blast AF and AT, respectively). Frozen storage of high-pressure treated samples did not significantly affect initial quality of frozen muscle. Thus, parameters related to protein denaturation and extractability, water holding capacity and color presented similar values than those obtained for not stored samples. In addition, the improvement of the microstructure achieved by PSF application remains unchanged during frozen storage. On the other hand, conventional treated samples experienced significant changes during frozen storage, such as protein denaturation, and water holding capacity and color modifications. Storage temperatures did not have influence in the quality of PSF and PAT samples, but it showed some effects in AF muscle.Industrial relevance: This work demonstrates the potential application and benefits of high pressure (HP) in the freezing and thawing of fish meat in comparison to conventional methods, due to an improvement on the cellular integrity of the tissue. Although some negative effects are produced during processing with HP, no additional modifications occur during the frozen storage. The studied methodologies seemed to be very suitable for fish freezing and thawing, especially for products which will be frozen stored and/or cooked.     

Quality Characteristics of Broiler Chicken Meat on Salt at Different Temperatures

The aim of this investigation was to compare the quality characteristics and muscle structure of broiler chicken meat stored at different temperatures in the retail market in Oman. The meat quality characteristics of broiler breast meat were analysed. Ten samples were randomly selected from each group of fresh, frozen, and chilled chicken meat. Colour L?, a?, b?, pH, expressed juice, cooking loss, sarcomere length, W-B-shear force and muscle structure (using scanning electron microscopy) were determined. Fresh meat samples had significantly (P < 0.05) lower pH values and lightness L? than those of chilled and frozen samples. The chilled meat samples were significantly (P < 0.05) lighter and had lower shear force values than fresh and frozen samples. Frozen samples had significantly (P < 0.05) higher expressed juice and cooking loss values than either fresh or chilled samples. The pH values of fresh, chilled, and frozen breast samples were related to colour and expressed juice. Electron microscopy demonstrated that the changes in the physical properties of the chilled meat were related to breakdown of the muscle fiber bundles. The quality characteristics of broiler meat from different storage temperatures varied significantly.     

海藻糖类抗冻保水剂对冻藏南美白对虾(Litopenaeus vannamei)品质的影响

以冻藏南美白对虾(Litopenaeus vannamei)虾仁为研究对象,0.5%和1.0%(w/v)海藻糖、海藻酸钠、海藻酸钠寡糖溶液作为抗冻保水剂,蒸馏水、0.5%和1.0%(w/v)焦磷酸钠分别为阴性对照组和阳性对照组,于-18 ℃下贮藏6周,通过对冻藏南美白对虾仁的解冻损失、颜色、肌原纤维蛋白含量、Ca2+-ATPase活性以及微观结构等指标进行分析,评价海藻糖类等对冻藏虾仁品质的影响。结果表明,与对照组相比,海藻糖、海藻酸钠寡糖、焦磷酸钠处理组虾仁的解冻损失显著降低(p<0.05)。海藻糖类提高了南美白对虾冻藏期间颜色的稳定性。海藻糖和海藻酸钠寡糖处理有效地保持了冻藏虾仁中肌原纤维蛋白含量和Ca2+-ATP酶活性,其中肌原纤维含量分别为104.2、103.2 mg/g,Ca2+-ATP酶活性分别为0.141、0.142 μmol Pi/mg·min。染色实验和电泳实验结果表明,海藻糖类对冻藏后肌肉蛋白质的降解和肌肉组织结构的损伤具有减缓作用,虾仁肌肉肌纤维结构完整,肌肉间无较大空隙形成,较好地保持了冻藏虾仁组织完整性,副肌球蛋白和肌动蛋白条带的强度都没有明显的降低。研究表明:在南美白对虾的冻藏过程中,海藻糖和海藻酸钠寡糖抗冻剂起到了良好的抗冻效果,能够更好地保证冻藏虾仁的质量和品质,得到一种冻藏水产品复合磷酸盐保水剂的较好替代品。     

基于内源酶活性变化的冷藏哈氏仿对虾肌肉品质研究

目的：探究冷藏条件下哈氏仿对虾内源酶活性及肌肉品质特性的变化情况。方法：以哈氏仿对虾为对象,在0℃冷藏0、2、4、6 d,比较分析完整虾组和去头虾组肌肉的质构、TCA-可溶性肽、肌原纤维蛋白含量及其小片化指数以及虾头与肌肉中各种内源酶活性的变化规律。结果：随着冷藏时间的延长,两组虾肌肉中TCA-可溶性肽含量及肌原纤维小片化指数均呈现上升趋势;肌原纤维蛋白含量呈下降趋势,完整虾组和去头虾组肌肉在冷藏6 d后分别降低了56.65%和44.63%;而两组虾肉的硬度和弹性也始终呈现出下降趋势。在冷藏过程中,完整虾组虾头中胰蛋白酶活性逐渐下降,而其肌肉中活性则不断增加,去头虾组肌肉中该酶活缓慢下降,完整虾组虾头及肌肉、去头虾组肌肉中分别变化了16.9%、68.8%和15.2%;钙蛋白酶活性在两组肌肉中均随冷藏时间延长而不断下降,其中以完整虾组肌肉下降幅度较明显;在冷藏过程中组织蛋白酶B、D、H及L活性变化情况有所不同,其中去头虾组肌肉中4种组织蛋白酶活性整体高于完整虾组;两组虾肌肉中4种组织蛋白酶的活性在各亚细胞组份中,随着冷藏时间延长而逐渐下降,且完整虾组中活性高于去头虾组。结论：在冷藏过程中...     

Protein changes in shrimp (Metapenaeus ensis) frozen stored at different temperatures and the relation to water-holding capacity

To study the effects of freezing temperature on muscle proteins, shrimp (Metapenaeus ensis) were frozen stored at either −18 or −60 °C up to 90 and 210 days. Shrimp frozen at −18 °C had higher thawing and compression loss and poor myofibril water-holding capacity compared with those frozen at −60 °C. In terms of protein characteristics, shrimp frozen at −18 °C had higher levels of carbonyls and reduced sulphhydryls. Moreover, the shrimp frozen at −18 °C had higher surface hydrophobicity and reduced Ca²⁺-ATPase activity, indicating increased protein denaturation. Proteomics revealed that seventy-five proteins were classified as differentially abundant proteins (DAPs) following freezing. There were sixty-four DAPs in the F18-CON comparison group (shrimp frozen at −18 °C vs. control) and thirty-two DAPs in the F60-CON comparison group (shrimp frozen at −60 °C vs. control), suggesting that freezing at −18 °C results in more DAPs than freezing at −60 °C. A comparison between F18 and F60 revealed that ribosomal proteins (L44, L7a) and heat shock protein 21 were downregulated in F18. These results increase our understanding of the variable quality associated with shrimp frozen at different temperatures.     

Quality of superchilled vacuum packed Atlantic salmon (Salmo salar) fillets stored at −1.4 and −3.6 °C

The most important factor for increasing shelf life is the product temperature, and since fish is more highly perishable than meat, the temperature is even more important. In the present study, portions of fillets of farmed Atlantic salmon (Salmo salar) were superchilled at two temperature levels, −1.4 and −3.6 °C. Texture, drip loss, liquid loss, cathepsin activities and protein extractability were investigated during storage and compared to ice chilled and frozen references. Drip loss was not a major problem in superchilled salmon. Textural hardness was significantly higher in superchilled salmon fillets stored at −3.6 °C compared to those stored at −1.4 °C, ice chilled and frozen references. Cathepsins B and B + L were not deactivated at the selected storage temperatures. The storage time of vacuum packed salmon fillets can be doubled by superchilled storage at −1.4 °C and −3.6 °C compared to ice chilled storage.     

Efficacy of freezing, frozen storage and edible antimicrobial coatings used in combination for control of Listeria monocytogenes on roasted turkey stored at chiller temperatures

The presence and growth of Listeria monocytogenes on ready-to-eat (RTE) turkey is an important food safety issue. The antilisterial efficacy of four polysaccharide-based edible coatings (starch, chitosan, alginate and pectin) incorporating sodium lactate (SL) and sodium diacetate (SD) as well as commercial preparations Opti.Form PD4, NovaGARD™ CB1, Protect-M and Guardian™ NR100 were compared against L. monocytogenes on roasted turkey. Pectin coating treatments incorporating SL/SD, Opti.Form PD4 with or without Protect-M, and NovaGARD™ CB1 displayed higher antimicrobial efficacy against.L. monocytogenes than the other antimicrobials and coating materials. In the second phase of the study, it was investigated whether frozen storage could enhance the antilisterial effectiveness of pectin coating treatments on chilled roasted turkey. Inoculated roasted turkey samples coated with pectin-based treatments were frozen for up to 4 weeks and subsequently stored at 4 °C for 8 weeks. Frozen storage significantly enhanced the antilisterial activity of various coating treatments; with selected treatments reducing the L. monocytogenes populations by as much as 1.1 log CFU/cm² during the subsequent 8-week chilled storage. This study demonstrates that pectin-based antimicrobial edible coatings hold promise in enhancing the safety of RTE poultry products and frozen storage has the potential to enhance their effectiveness.     

微冻贮藏对牛肉保水性的影响

本实验以冷藏（2 ℃）和冷冻（－18 ℃）作为对照组,从肌原纤维蛋白结构和水分迁移等方面分析了微冻（－4 ℃）贮藏条件下牛肉保水性变化的机制。结果表明：微冻贮藏牛肉的汁液损失率和蒸煮损失率显著高于冷藏和冷冻处理组（P＜0.05）,保水性最差。微冻贮藏过程中,牛肉中的水分弛豫时间逐渐变长,结合水相对含量无明显变化,不易流动水相对含量显著下降,自由水相对含量显著上升（P＜0.05）。随着贮藏时间的延长,3 种贮藏方式下牛肉的总巯基含量和活性巯基含量均显著下降,蛋白质表面疏水性显著上升（P＜0.05）,且贮藏温度越低,变化速率越慢。微冻贮藏过程中,牛肉肌原纤维蛋白降解程度较低,贮藏后期蛋白质变性程度较高,提升了肌原纤维蛋白网络中不易流动水的自由度,使得部分不易流动水转化为自由水,导致了微冻牛肉较差的保水性。     

Use of microbial transglutaminase and sodium alginate in the preparation of restructured fish models using cold gelation: Effect of frozen storage

Changes in physicochemical properties of raw-appearing restructured models made from hake (Merluccius capensis) muscle, using cold gelation technology by addition of sodium alginate and microbial transglutaminase (MTGase), were studied during frozen storage at ? 15 °C.Among the more interesting results, addition of MTGase produced more protein aggregation in models processed by muscle homogenization and thus the protein network that formed in the gel was better than in samples with added sodium alginate. All samples presented enhanced changes in mechanical properties such as gel strength in the course of frozen storage. The protein network that formed was better organized as shown by the ultrastructure analysis and by protein aggregation data from the beginning of storage, and as a result Water Binding Capacity was greater in restructured models processed by muscle homogenization. Some of the models studied presented lipid oxidation during frozen storage, slightly more in the ones with MTGase added.Industrial RelevanceThe industrial relevance of the present work is to establish bases for using fish fillet trimmings and minced muscle to prepare restructured products that can be commercialized in a raw state and that could also support frozen storage in order to prolong the self-life in the market. The models studied here are not final products but the base with which to prepare them. One possibility of them is to process this kind of products with technologies normally used in whole fish muscle such as smoked fish fillets, carpaccios or marinated products. In addition, these raw restructured products can be commercialized to be cooked as a normal fresh fish fillet or pieces of fillet in a variety of preparations, and also products that contain a high amount of salt. Samples elaborated by binding larger muscle fragments imitate well the original fibrousness of the muscle so that it could be used to elaborate products similar to hamburgers or others that will be fried in batter.