Microstructure and instrumentally measured textural changes of rainbow trout (Oncorhynchus mykiss) gravads during production and storage

BACKGROUND: Gravad fish belong to a group of low‐processed products obtained from fresh fish by rubbing fillets with a mixture of sugar and salt and then placing them in cold storage. Little is known about changes in the tissue during the production and storage of gravads. The aim of the present study was to investigate the microstructural and textural changes in rainbow trout (Oncorhynchus mykiss) gravad during processing and vacuum storage at 3 °C and ?30 °C. RESULTS: Microscopic observations of gravad showed greater compactness of structure when compared with raw trout muscle, characterised by the disappearance of the divisions between adjoining myofibrils in gravad. Freezing, on the other hand, caused the myofibrils to again become more clearly distinguishable despite being partly agglomerated into lamellae. The above changes in structure were accompanied by changes in the textural and rheological properties of the product. It was observed that the texture profile (TPA) changed, resulting in an increase in the cohesiveness and chewiness of the gravads when compared to the raw fillets. There was also a lowering of stress decay during the relaxation test and a decrease in the value of the storage modulus (G′) as analysed by oscillatory rheometry. Further changes observed during storage were mainly concerned with an increase in the hardness and chewiness of gravads. CONCLUSION: Gravading significantly changes the rainbow trout fillets by making the microstructure more compact. This process is accompanied by changes in texture and rheological properties, which next are running during the storage of a chilled or frozen product. These changes are significant enough for potential consumers to be made aware of the fact that the texture of the product changes considerably during its shelf life. Copyright © 2009 Society of Chemical Industry     

Comparison of chitosan–gelatin composite and bilayer coating and film effect on the quality of refrigerated rainbow trout

The effect of chitosan–gelatin coating and film on the rancidity development in rainbow trout (Oncorhynchus mykiss) fillets during refrigerated storage (4 ± 1 °C) was examined over a period of 16 days. Composite and bilayer coated and film wrapped fish samples were analysed periodically for microbiological (total viable count, psychrotrophic count) and chemical (TVB-N, POV, TBARS, FFA) characteristics. The results indicated that chitosan–gelatin coating and film retained their good quality characteristics and extend the shelf life of fish samples during refrigerated storage .The coating was better than the film in reducing lipid oxidation of fillets, but there was no significant difference between them in control of bacterial contamination.     

Effect of chitosan coatings enriched with cinnamon oil on the quality of refrigerated rainbow trout

The effects of a chitosan (Ch) coating enriched with cinnamon oil (Ch + C) on quality of rainbow trout (Oncorhynchus mykiss) during refrigerated storage (4 ± 1 °C) were examined over a period of 16 days. A solution of Ch (2%, w/v) and Ch + C (2%, w/v Ch + 1.5%, v/v C) was used for the coating. The control and the coated fish samples were analysed periodically for microbiological (total viable count, psychrotrophic count), chemical (TVB-N, PV, TBA), and sensory (raw and cooked fish) characteristics. The results indicated that the effect of the Ch + C coating on the fish samples was to enable the good quality characteristics to be retained longer and to extend the shelf life during the refrigerated storage.     

The determination of flesh productivity and protein components of some fish species after hot smoking

Chemical changes in pike perch (Sander lucioperca L Kottelat 1997), rainbow trout (Oncorhynchus mykiss WALBAUM 1792) and eel (Anguilla anguilla L 1766) after hot smoking were investigated. Some differences in water, protein, lipid, ash and carbohydrate contents of the fish were established as significant (P < 0.01). The flesh productivity of fresh eel and pike perch was found to be very high. Differences in group averages of total microprotein content of fresh, smoked and stored eel, rainbow trout and pike perch were found to be significant (P < 0.01). Using polyacrylamide gel electrophoretic analysis, 18 protein bands in rainbow trout, 12 bands in pike perch and 14 bands in eel were determined. Most of the bands disappeared after smoking and storage owing to denaturation of the fish proteins. © 2001 Society of Chemical Industry     

Restoration of EPA and DHA in rainbow trout (Oncorhynchus mykiss) using a finishing fish oil diet at two different water temperatures

Feeding fish a fish oil finishing diet (FOFD) after grow-out on vegetable oil diet is one strategy to restore eicosapentaenoic acid (EPA) and docosahexaenoic acid (DHA) levels. We investigated restoration of EPA and DHA in rainbow trout fed a FOFD preceded by a grow-out period on 50% or 75% palm fatty acid distillate (PFAD) diets at optimal (15 °C) or elevated (20 °C) water temperatures. Using the FOFD restored EPA and DHA in fillet and whole carcass of fish previously fed either 50% PFAD diet from 85% to 98% or 75% PFAD from 66% to 93% of values obtained for fish fed FO diet throughout. Water temperature did not influence EPA and DHA restoration. Growing rainbow trout with diets where FO was replaced by either 50% or 75% PFAD followed by a FOFD reduced FO usage by around 30% and 44% at 15 °C, respectively, and 32% and 48% at 20 °C, respectively.     

Quality and Shelf Life of Cold and Frozen Rainbow Trout (Oncorhynchus mykiss) Fillets: Effects of Fish Protein-Based Biodegradable Coatings

The Klunzinger’s ponyfish (Equulites klunzingeri) protein powder extracted with acid or alkali aided process as a biodegradable coating material for rainbow trout (Oncorhynchus mykiss) fillets during cold (+2°C) and frozen storage (–18°C) were investigated. The coating with alkaline treated protein (AlPC) and acid treated protein (AcPC) extended the shelf life of fillets from 11 to 14 days in cold storage and improved the quality parameters in three months frozen storage period. According to total viable count and total psychrophile count results, bacteria grew more quickly in uncoated fillets than coated fillets. The protein-based coating did prevent spoilage of the rainbow trout fillets as reflected by a decrease in pH, total volatile base-nitrogen and free fatty acids during cold and frozen storage period. Therefore, this study demonstrated that fish protein-based coating had a positive effect on maintaining the rainbow trout fillets quality, and edible coatings from discard fish can offer a promising alternative for preserving fish fillets.     

Myosin heavy chain degradation during post mortem storage of Atlantic cod (Gadus morhua L.)

Post mortem proteolytic degradation of fish fillets leads to textural changes like muscle softening and gaping. In this study proteolytic degradation of myosin heavy chain (MHC) was monitored during storage of muscle and of isolated myofibrils at different temperatures and pH-values by the use of MHC-specific antibodies. The ability of cathepsin D to associate to myofibrillar proteins was also studied. Muscle stored at 6 °C and isolated myofibrils stored at 0 °C, 6 °C and 20 °C were degraded at pH 6.3 or lower. Cathepsin D could be found associated with extensively washed myofibrils. Inhibition of cathepsin D during storage affected the observed MHC-degradation at pH 5.5, but not at pH 6.3. This indicates that cathepsin D to a less extend than formerly believed, is responsible post mortem degradation of MHC.     

Peptides in rainbow trout (Oncorhynchus mykiss) muscle subjected to ice storage and cooking

Although proteolysis during post mortem storage is an important factor affecting fish texture, little is known about degradation end-products. This study was performed to investigate the occurrence of low molecular weight peptides (<5 kDa) in post mortem rainbow trout muscle, during ice storage, and to evaluate their stability during cooking. It combined quantitative (amino acid analysis) and qualitative approaches (mass spectrometry). The results showed that muscle of trout was poor in peptides. These were mainly anserine and glutathione. Their concentration was almost unaffected by the seven days of ice storage and vacuum cooking for 5 min at 70 °C. MS analysis revealed a limited but highly reproducible appearance of small peptides in trout muscle during the ice storage and after cooking. The compounds detected by MS analysis remain to be characterised.     

Interaction between fish myoglobin and myosin in vitro

Interaction between tuna myoglobin and myosins from tuna and sardine was investigated in a model system at 4 °C for up to 24 h. Both sardine and tuna myosins bound progressively with tuna myoglobin as the storage time increased (P < 0.05). The soret absorption peak was noticeable in the myoglobin–myosin mixture. The oxidation of oxymyoglobin in the presence of myosin was generally greater than that found in the absence of myosin (P < 0.05). Oxymyoglobin underwent oxidation to a greater extent in the presence of tuna myosin than sardine myosin (P < 0.05). The interaction between fish myoglobin and myosin also caused changes in reactive sulfhydryl content and altered the tryptophan fluorescent intensity. The loss in Ca²⁺-ATPase activity of myosin varied with fish species and was governed by the myoglobin added. Thus, the interaction between fish myoglobin and myosin most likely occurred as a function of time and was species-specific.     

Physicochemical changes in ω − 3-enhanced farmed rainbow trout (Oncorhynchus mykiss) muscle during refrigerated storage

Physicochemical changes of ω − 3-enhanced farmed rainbow trout (Oncorhynchus mykiss) fillets developed by dietary modification with flaxseed oil and α-tocopheryl acetate (α-TA) were determined during storage at 2 °C. Trout were fed experimental diets for 120 days followed by processing to obtain boneless skinless fillets. The dietary modification increased concentration of total ω − 3 fatty acids in the fillets, which enhanced chances for lipid oxidation during storage. The fillets were vacuum or non-vacuum packed and stored at 2 °C for 10 or 12 days. Dietary α-TA resulted in higher (P < 0.05) concentration of α-tocopherol in fillets during storage; however, it did not retard (P > 0.05) lipid oxidation. Vacuum packaging resulted in much lower (P < 0.05) TBARS and higher (P < 0.05) retention of α-tocopherol during storage than non-vacuum packaging. However, α-tocopherol unlike vacuum packaging better protected ω − 3 FA in the fillets during storage.     

The effects of thyme (Thymus vulgaris L.) oil concentration on liquid-smoked vacuum-packed rainbow trout (Oncorhynchus mykiss Walbaum, 1792) fillets during chilled storage

This study examined the effects of thyme oil on chemical properties, microbiological changes, and sensory quality in vacuum-packed liquid-smoked rainbow trout fillets under chilled storage. After 150 days of storage, the total volatile basic nitrogen (TVB-N) values were 30.52, 27.5 and 39.43 mg/100 g, and total viable counts (TVC) were 5.34, 4.96 and 5.53, for thyme oil additions of 10 (T10), 50 (T50) and 0 (control; T0) mL/L brine, respectively. The highest acceptable TVB-N value was adopted as 30 mg /100 g, corresponding to shelf lives of 135, 150, and 105 days for T10, T50, and T0, respectively. T50 addition of thyme oil to liquid-smoked rainbow fillets extended shelf life T10 and T50, gave acceptable sensory quality and limited microbiological growth during chilled storage.     

Effects of chitosan molecular weight and degree of deacetylation on the properties of gelatine-based films

The effect of chitosan molecular weight (MW) and degree of deacetylation (DD) on the physicochemical properties of gelatine-based films was studied with the goal of improving the films. Determination of the dynamic viscoelastic properties (elastic modulus G′ and viscous modulus G″) of the film-forming solutions revealed that the interactions between gelatine and chitosan were stronger in the blends made with chitosan of higher molecular weights or higher degrees of deacetylation than the blends made with lower molecular weights or degrees of deacetylation. Fish gelatine films modified with chitosan of higher molecular weights or higher degrees of deacetylation had higher tensile strengths (TS, 72.4 MPa for 550 kDa vs. 62.2 MPa for 200 kDa; 63.2 MPa for 93.6% DD vs. 38.0 MPa for 76.5% DD) and higher glass transition temperatures (T_g, 130 °C for 550 kDa vs. 108 °C for 200 kDa; 108 °C for 93.6% DD vs. 103 °C for 76.5% DD). Fourier transform infrared spectra (FTIR) and X-ray diffraction (XRD) studies indicated that gelatine and chitosan interactions determined the properties of the film. Thus, combining gelatine and chitosan may be a method for improving the physicochemical properties of gelatine films, especially when using chitosan of higher molecular weights and higher degrees of deacetylation.     

Thiol oxidation and protein cross-link formation during chill storage of pork patties added essential oil of oregano,rosemary, or garlic

The effect of two levels (0.05% and 0.4%) of essential oil of rosemary, oregano, or garlic on protein oxidation in pork patties was studied during storage under modified atmosphere (MAP: 70% O₂: 20% CO₂: 10% N₂) or under aerobic conditions (AE) at 4 °C. The oxidative stability of the meat proteins was evaluated as loss of thiols for up to 9 days of storage, and as formation of myosin cross-links analyzed by SDS-PAGE after 12 days of storage. Protein thiols were lost during storage to yield myosin disulfide cross-links. Essential oils of rosemary and oregano were found to retard the loss of thiols otherwise resulting in myosin cross-links. Garlic essential oil, on the contrary, was found to promote protein oxidation, as seen by an extreme loss in thiol groups, and elevated myosin cross-link formation compared to control.     

Effect of beef ultimate pH and large structural protein changes with aging on meat tenderness

This study investigated the effect of ultimate pH (pH_u) in beef on the degradation of large structural proteins during refrigerated storage using SDS-PAGE. M. longissimus dorsi from bull carcasses were selected and classified into three groups: low pH_u (≤ 5.79), intermediate pH_u (5.80–6.19) and high pH_u (≥ 6.2) muscles. Samples were then stored at − 1.5 °C for 1, 2, 7, 14, 21 and 28 days. Meat tenderness was measured at each aging time. Depending on meat pH_u, different protein patterns and degradation rates of structural proteins were found. Rapid changes of large structural proteins took place within 48 h post mortem. Besides titin and nebulin, degradation of filamin was clearly revealed. Two more large protein bands corresponding to myosin family members also exhibited fast decline with storage time. It suggested that the fast degradation of these proteins is a key factor in the improvement of meat tenderness.     

Effect of delayed icing on quality changes of iced rainbow trout (Onchorynchus mykiss)

The effect of delayed icing on quality deterioration of rainbow trout (Onchorynchus mykiss) iced 0, 4 and 8 h after catch was assessed by chemical, microbiological and sensory methods. Total volatile basic nitrogen (TVB-N), free fatty acids (FFA), peroxide value (PV) and thiobarbituric acid (TBA) values increased during the pre-icing duration. Delayed icing led to significant increased (p < 0.05) in total viable counts (TVC) throughout the period of storage. This study showed that sensory analysis of rainbow trout correlated well with microbiological analysis. Results of this study according microbiological and sensory data indicated that the shelf-life of rainbow trout stored in ice immediately after catch was approximately 9–11 days, while delay in icing for 4 and 8 h shortened the shelf-life was around 5–7 and 1–3 days, respectively.     

The effects of an iron-catalyzed oxidation system on lipids and proteins of dark muscle fish

The effects of a hydroxyl radical-generating system induced by iron catalyzed oxidation (Fe²⁺/H₂O₂) on lipids and proteins of sardine, Atlantic bonito, anchovy and bluefish were investigated. Thiobarbituric acid-reactive substances (TBARs, mg malonaldehyde/kg fish muscle) formation was used to evaluate oxidative damage of the lipid in dark muscle fish due to iron catalyzed oxidation. The amount of TBARs was observed to increase significantly in sardine and anchovy as the incubation time increased, while Atlantic bonito and bluefish reached their maximum values of TBARs within the first 3 h of incubation, and after that did not change (p < 0.05). Carbonyl contents (nmol carbonyl/mg protein) of all fish samples measured as an index of protein oxidation were affected differently by the iron-catalyzed oxidation system during incubation. However, significant increases in the carbonyl groups were detected in sardine, Atlantic bonito and bluefish, but not in anchovy as a result of the long incubation time (5 h) (p < 0.05). When comparing to increases Atlantic bonito showed the maximum increase protein carbonyl. The electrophoretic patterns in the presence and absence of β-mercaptoethanol showed that a loss of proteins generally occurred in all fish at the end of incubation, and the greatest alteration in protein bands was observed in anchovy during Fe²⁺-catalyzed oxidation. The bands above 50 kDa disappeared within the first 1 h of incubation. The loss of protein (both high and low molecular weight) may involve disulfide and non-disulfide covalent linking during the iron catalyzed incubation. These data suggest that an increase in TBARs and fragmentation, and a loss of proteins exposed to iron-catalyzed oxidation may explain the oxidative damage of lipids and proteins which causes quality loss and limits the storage life of dark muscle fish.     

Chemical and biochemical changes of hybrid catfish fillet stored at 4 °C and its gel properties

Chemical and biochemical changes of aquacultured hybrid catfish fillet (Clarias macrocephalus × Clarias gariepinus) and its gel-forming ability as affected by age and sex of fish along with storage time were investigated. Fillets were stored at 4 °C for 0, 3, 6, 9, 12 and 15 days. There was no significant effect of sex and age of fish as well as storage time on fat, moisture and ash contents (P > 0.05). The total protein, water soluble protein, and salt soluble protein contents of the fillets significantly decreased with storage time (P < 0.05). On the other hand, pH, total volatile base nitrogen (TVB-N) and autolytic degradation products (ADP) increased as storage time continued (P < 0.05). Decreases in Ca²⁺-ATPase activity and gel properties were observed as storage time increased. However, there was no significant effect of either sex or age of fish on textural properties of gel (P > 0.05). Hybrid catfish fillet stored at 4 °C should be processed within 6 days.     

Effects of cooking methods on the formation of heterocyclic aromatic amines of two different species trout

Heterocyclic aromatic amines (HAAs) are sometimes formed in meats and fish cooked at high temperatures. In the present study, the effects of cooking methods by deep-fat frying, pan-frying, grilling and barbecuing on the formation of HAAs of fillets of rainbow trout (Oncorhynchus mykiss) and brown trout (Salmo trutta fario) were investigated. Barbecued brown trout (1 g) was estimated to contain 0.12 ng of IQ (2-amino-3-methylimidazo[4,5-f]quinoline), 0.02 ng 4,8-DiMeIQx (2-amino-3,4,8-trimethylimidazo[4,5-f]quinoxaline). Grilled rainbow trout (1 g) was estimated to contain 0.02 ng 4,8-DiMeIQx. MeIQ (2-amino-3,4-dimethylimidazo[4,5-f]quinoline), MeIQx (2-amino-3,8-dimethylimidazo[4,5-f]quinoxaline) and PhIP (2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine) were not detectable in all cooked fish.     

Rheological and functional properties of gelatin from the skin of Bigeye snapper (Priacanthus hamrur) fish: Influence of gelatin on the gel-forming ability of fish mince

The rheological and functional properties of gelatin from the skin of bigeye snapper (Priacanthus hamrur) fish were assessed. The protein content of dried gelatin was 94.6% and moisture content was 4.2%. The amino acid profile of gelatin revealed high proportion of glycine and imino acids. The bloom strength of solidified gelatin was 108 g. The average molecular weight of fish skin gelatin was 282 kDa as determined by gel filtration technique. The emulsion capacity (EC) of gelatin at a concentration of 0.05% (w/v) was 1.91 ml oil/mg protein and with increase in concentration, the EC values decreased. The gelling and melting temperatures of gelatin were 10 and 16.8 °C, respectively as obtained by small deformation measurements. The flow behavior of gelatin solution as a function of concentration and temperature revealed non-Newtonian behavior with pseudoplastic phenomenon. The Casson and Herschel–Bulkley models were suitable to study the flow behavior. The yield stress was maximum at 10 °C with the concentration of 30 mg/ml. Thermal gelation behavior of threadfin bream (Nemipterus japonicus) mince in presence of different concentration of gelatin was assessed. Gelatin at a concentration of 0.5% yielded higher storage modulus (G′) value than control. Frequency sweep of heat set gel with gelatin revealed strong network formation.     

Effect of thermal process on connective tissue from jumbo squid (Dosidicus gigas) mantle

The effect of two thermal treatments (fast freezing at −40 °C and vapor cooking at 100 °C) on connective tissue extract (CTE) from jumbo squid (Dosidicus gigas) was investigated. Samples of CTE frozen at −40 °C were taken at 0, 3, 5 and 12 min. Also CTE was cooked at 100 °C and samples were taken at 0, 1, 2.5 and 5 min. Light microscopic observations of CTE after 12 min of freezing showed rupture of fibres. The CTE fibres showed agglutination during cooking time. The CTE insoluble fraction increased with freezing and cooking time. Maximum zeta potential value of untreated CTE was detected at pH 5.0 at +30 mV, meanwhile in the frozen CTE it was detected at pH 7.0 at +30 mV and two peaks (at pH 5.5 and 9.0) were observed at +20 mV in the cooked CTE. One endothermic peak was found at 105.9 °C in the untreated CTE, while in the frozen and cooked CTE the endothermic peaks were found at lower temperatures and enthalpies. Electrophoresis analysis of untreated CTE showed three bands. In the frozen CTE two bands appeared above 200 kDa, and in the cooked CTE, a 45 kDa band disappeared. These results suggest that during freezing and cooking processes there were modifications to molecular bonds that hold the integrity of the structure of the connective tissue of the jumbo squid mantle.