Effects of Brief Summer or Winter Fasting on the Muscle Quality of Cultured Pacific Bluefin Tuna (Thunnus orientalis)

The effects of fasting on the quality of the dorsal and ventral ordinary muscles from cultured Pacific bluefin tuna (Thunnus orientalis) during chilled storage were investigated. Tuna were subjected to fasting for 2 days in the summer or 6 days in the winter prior to harvesting. The breaking strength of the dorsal ordinary muscle sampled in the summer increased until 24 h and then decreased. There were no significant differences in the lipid and glycogen content of the ordinary muscle after 9 h of storage between the controls and either fasting group. The pH of the ordinary muscle subjected to summer and winter fasting was higher than in the controls after 24–48 h of storage. However, the relationship between the pH and glycogen content was unclear. The metmyoglobin content during chilled storage was lower in the ordinary muscles from either fasting group than in the controls. In conclusion, fasting for 6 days in the winter improved the color stability of the ordinary muscle without a decline in its lipid content.     

The changes in proximate compositions and glycogen contents in the dorsal ordinary muscles of the full-cycle cultured Pacific bluefin tuna Thunnus orientalis occurring with growth

ABSTRACT:   Using full-cycle cultured (FC) Pacific bluefin tuna (body length [BL], 42.6–66.4 cm; body weight [BW], 1.66–7.40 kg, n  = 15), the changes in chemical compositions and histological structure of the cephalal parts of the dorsal ordinary muscles (DOM) occurring with growth were investigated. A positive correlation ( r  = 0.9644, P  < 0.05) was observed between BL and BW with growth. The protein, lipid and ash contents of DOM and condition factor did not change with growth. However, the glycogen content of DOM increased ( P  < 0.05) from approximately 55 cm (BL) in this study. Using optical microscopic photographs, the various shapes of muscle fibers were observed and it was noted that the muscle fiber diameter increased ( P  < 0.05) with growth. Using transmission electron microscopic observation, many glycogen granules were observed in muscle fibers (especially, side of connective tissue) of DOM throughout the growth stage in this study. These results indicate that the glycogen content of DOM of FC Pacific bluefin tuna increases before the lipid with growth.     

Myofibrillar proteolysis by myofibril-bound serine protease from white croaker <Emphasis Type="Italic">Argyrosomus argentatus</Emphasis>

ABSTRACT:   The modori phenomenon is defined as heat-induced myofibrillar degradation caused by endogenous serine protease(s) of fish muscle during Kamaboko fish meat gel production. This study was undertaken to analyze myofibrillar proteolysis of white croaker Argyrosomus argentatus muscle, which is an ingredient of high quality Kamaboko, by myofibril-bound serine protease (MBSP) under conditions corresponding to the modori phenomenon. White croaker MBSP was stable between pH 2–11 and below 65°C, and about 60% of its initial activity remained after incubation for 2 h under the conditions at 65°C and pH 7.5. About 60% of the enzyme activity was suppressed by 0.5 M NaCl. White croaker MBSP degraded various myofibrillar proteins between 40 and 70°C and pH 6.0–9.0, and preferentially degraded myosin heavy chain rather than other myofibrillar proteins. The enzyme degraded the myosin heavy chain most strongly at 55°C and pH 7.0, and a major part of the bands of myosin heavy chain and its degradation products disappeared for a period of 2 h. These degradation characteristics are very similar to those observed during the modori phenomenon, indicating that MBSP could be a modori-inducing protease involved in the modori phenomenon of white croaker Kamaboko production.     

Characteristics of burnt meat in cultured yellowtail <Emphasis Type="Italic">Seriola quinqueradiata</Emphasis>

ABSTRACT:   In order to understand the characteristics of burnt meat in cultured yellowtail Seriola quinqueradiata , fish were kept at two different temperatures (13 and 30°C) and slaughtered by either spinal cord destruction (SCD) or suffocation in air (SA). Early postmortem changes during storage at 32°C were analyzed by rheological, biochemical, and histological methods. The burnt meat (with lightness parameter, L* ≥ 55) was observed at 1-h storage in the SA 30°C group, at 2 h in SCD 30°C, and at 4 h in SA 13°C; meat was normal for the SCD 13°C group until 6 h of storage. Breaking strength scores were higher for the normal meat (200 g/cm²) than burnt meat (70 g/cm²) at 4 h of storage. Expressible water content was higher for the burnt meat than for the normal meat. Adenosine triphosphate concentrations for the SCD groups were higher than for the SA counterparts. Moreover, pH decrease was much faster in the 30°C groups, showing pH 5.6 at 2 h of storage. A negative correlation between the pH and lactic acid contents in muscle ( P  < 0.001) was found. Histological analysis evidenced a larger pericellular area (40%) in the burnt samples than in the normal samples (16%). It was confirmed that a higher fish-keeping water temperature and a stressful slaughter method (faster glycolytic process) were determinative factors that influence the occurrence of burnt muscle in yellowtail, and that the effect of the former is larger than the latter.     

Changes of proximate compositions and myoglobin content in the dorsal ordinary muscles of the cultured Pacific bluefin tuna <Emphasis Type="Italic">Thunnus orientalis</Emphasis> with growth

ABSTRACT:   Using the dorsal ordinary muscle (DOM) of cultured Pacific bluefin tuna (body length [BL]: 47.5–81.8 cm, body weight [BW]: 2.1–13.5 kg, n  = 15), the changes of proximate compositions and myoglobin (Mb) content with growth were investigated. There was a positive correlation ( r  = 0.9832, P  < 0.05) of BL and BW in cultured tuna. The protein contents of the DOM of cultured tuna decreased ( P  < 0.05) and the lipid contents had a tendency to increase (not significantly) with growth. The meat color changed from pink to red with growth. In addition, the Mb contents of the DOM of cultured tuna increased ( P  < 0.05) from 1.0 mg/g (minimum BW fish) to 3.8 mg/g (maximum BW fish) with growth. These results indicate that the increase of the Mb content in the DOM of cultured tuna is not caused by the restriction of exercise and overfeeding between 2.1 kg and 13.5 kg of BW.     

Changes in the pericellular connective tissue and breaking strength of the three types of muscles of the cultured carp Cyprinus carpio during storage in ice

To elucidate the structural changes in pink (P), white (W), and red (R) muscles during storage in ice, we measured the breaking strength and changes in pericellular connective tissues of cultured carp. The breaking strength just after killing was highest in R muscle (1.00 ± 0.20 N), lowest in W muscle (0.37 ± 0.07 N), and intermediate (0.84 ± 0.12 N) in P muscle. During the storage period, the breaking strength decreased first in R muscle, then in P muscle, followed by W muscle. The diameter of muscle fibers was greater in W muscle (113 ± 15 μm) than in P muscle (72 ± 3 μm) and R muscle (48 ± 2 μm). Destruction of the honeycomb structure of the pericellular connective tissue occurred most rapidly in W muscle and most slowly in R muscle. These results suggest that the interposing of P muscle fibers in the dorsal ordinary muscle contributes to the acceleration of post-mortem tenderization in fish.     

Isolation of ice-nucleating active bacterium from mackerel and its properties

ABSTRACT: An ice-nucleating bacterium, designated MACK-4, was isolated from ice-stored mackerel ( Scomber australasicus ) and identified as a Pseudomonas fluorescens . The optimal temperature and pH for its growth in nutrient broth with 2.5% glycerol (NB-G) were 15°C and 6.5, respectively. The maximal ice-nucleating activity (INA) was obtained after 54 h incubation at 15°C. However, the INA was almost completely lost after 48 h incubation at 25°C or higher. The growth and INA decreased with increase of NaCl added in NB-G within 0.0–4.0%. The INA of MACK-4 was very stable at 5–25°C, pH 4.0–9.5, while that of isolated ice-nucleating matter from MACK-4 was stable at 5–25°C, pH 5.5–9.0.     

Preparation and characterization of water-soluble chitosan produced by Maillard reaction

ABSTRACT:   The objective of this research was to improve the solubility of chitosan by Maillard reaction with 1% chitosan and 2% reducing sugar (glucose or glucosamine) dissolved in 0.2 M acetic acid, which was adjusted to pH 6.0, and incubated at either 50°C or 70°C for 1–7 days. The physicochemical and rheological properties of the chitosan–saccharide derivatives were also investigated. Results indicated that the solubility of modified chitosan derivatives was significantly greater than that of native chitosan. The solubility of chitosan–glucosamine was higher than that of chitosan–glucose, and the chitosan–glucosamine derivative remained soluble at pH 10. The degree of deacetylation of the derivatives decreased with increasing reaction time. Rheological investigation revealed that the apparent viscosity of the water-soluble chitosan derivatives in aqueous solution depended upon system conditions such as pH, ionic strength, and solution temperature. The measured apparent viscosity decreased as all system conditions increased. As calculated by the Arrhenius equation, the activation energy ( E _a ) of the derivatives in aqueous solution generally decreased with increasing the extent of Maillard reaction with respect to the reducing sugars used.     

Properties of extracellular ice-nucleating substances from <Emphasis Type="Italic">Pseudomonas fluorescens</Emphasis> MACK-4 and its effect on the freezing of some food materials

ABSTRACT:   Pseudomonas fluorescens MACK-4, isolated from mackerel surface, has an ice-nucleating activity (INA). In addition to bacterial cells, this strain could also produce an extracellular ice-nucleating substance (INS) with a maximal INA at pH 6.0. The extracellular INS (EINS) was stable at pH 6–9 during 1-h incubation with 3–5% of saccharides including maltose, trehalose and sucrose at 15°C. However, glycerol dramatically lowered the INA in both bacterial cells and the EINS. The addition of either the EINS or bacterial cells significantly elevated the ice-nucleating temperatures of pure water, full-cream milk, and 10% starch solution, but not orange juice and mackerel mince. The EINS produced from this strain could serve as crystal nuclei and accelerate ice crystallization during freezing.     

C-protein (MyBP-C) isoforms from carp ordinary and dark muscles and muscle type-specific binding to myosin

ABSTRACT:   C-protein is a myosin-associated protein of vertebrate striated muscle, and its function and properties have been extensively examined. However, there has been no report of C-protein of fish skeletal muscle so far. C-protein was identified in carp skeletal muscle by immunoassay using antibody against chicken C-protein, and the muscle-type specific C-protein was purified from carp ordinary and dark muscles for the first time. Although C-protein could be prepared from crude myosin by the reported procedure, C-protein degraded appreciably during the purification steps. Accordingly, C-protein was selectively extracted from the muscle with 0.15 M K-phosphate buffer (pH 5.8), and purified by ammonium sulfate fractionation, followed by AF-blue chromatography. Myosin free from the accessory proteins was obtained by diethylaminoethyl (DEAE) chromatography and used to assay the binding of C-protein with myosin. Ordinary muscle C-protein bound to ordinary muscle myosin in a saturable manner, but its maximum amount of binding was approximately twice that of dark muscle myosin. Similarly, dark muscle C-protein bound to dark muscle myosin much more than to ordinary muscle myosin. These results suggest that C-protein isoforms specifically bound with myosin isoforms originated from the same type of muscle.     

Influence of death struggle on the structural changes in chub mackerel muscle during chilled storage

ABSTRACT: Chub mackerel (34–35 cm, approximately 500 g), which were caught by fishing with a rod and line at the Bungo Channel, Oita prefecture, were rested overnight in a fish preserve and either killed by decapitation (control group) or allowed to struggle in air for 30 min (struggled group). Muscle samples were excised every 4 h, and measurements on breaking strength and histological observations were done for both groups. The breaking strength of muscle in the control group was significantly higher than that in the struggled group, whereby a decrease in breaking strength was delayed for 12 h compared to the struggled group. Light microscopy showed space extension among muscle cells in association with a decrease in breaking strength. Especially in the struggled group, the extended area was larger and the difference in area was significant at the time when breaking strength showed a significant difference. Using electron microscopy, the extended area showed cut and/or disappeared collagen fibrils. From these results, it was demonstrated that struggling to death promoted the degradation of collagen fibrils and the weakening of connective tissue and, resultantly, led to the faster softening of muscle of chub mackerel.     

Lipid composition and deposition of cultured yellowtail Seriola quinqueradiata muscle at different anatomical locations in relation to meat texture

ABSTRACT:   The present study was undertaken to assess the lipid composition and deposition in muscle at three anatomical locations in cultured yellowtail and to investigate the effect of lipid composition and deposition on meat texture. Lipid deposition in muscle was studied by histochemical staining of lipid with Sudan dye. Lipid class composition analysis showed that neutral lipids were the main constituents of lipid in cultured yellowtail and accounted primarily for the variation in muscle lipid content with the anatomical location of meat, as well as with season, whereas the polar lipid content remained almost constant. Furthermore, muscle neutral lipid content was correlated negatively with meat breaking strength; however, no correlation was observed between muscle polar lipid content and meat breaking strength. The histochemical study revealed that, in yellowtail muscle, lipid is preferentially deposited in the myosepta and, with increases in muscle lipid content, additional fat is deposited along sparsely distributed thin connective tissue. It was also observed that the greater the lipid deposition in collageneous connective tissue, the lower the meat breaking strength; presumably, higher lipid deposition in the connective tissue resulted in weakening of the muscle structure.     

Thermally induced gelation of paramyosin from scallop adductor muscle

ABSTRACT:   Thermally induced gelation of paramyosin from scallop smooth adductor muscle was investigated by dynamic rheological measurements under various conditions. The paramyosin thermal gel was produced at pH 6.5 and 7.2 at temperatures above 30°C through a two-step increase in storage (G') and loss (G') moduli; these values were higher than in gels produced from actomyosin at a high temperature. The thermal gel properties were very firm and brittle. In contrast, one main peak of G' was observed during gelation at pH 8.0. The gel produced at pH 8.0 was more transparent and less soluble in a 6 M urea−0.5 M NaCl solution than those formed either at pH 6.5 or 7.2. These differences in the thermal gel properties are presumed to derive from the pH dependence of the gel matrix-forming process, such as oxidative cross-linking between cysteine residues, rather than from the thermal unfolding of the paramyosin molecules. The thermal gelation profile of chymotrypsin-digested paramyosin showed marked depression of G' at high temperature.     

Characterization of 38 kDa and 42 kDa chitinase isozymes from the liver of Japanese common squid Todarodes pacificus

ABSTRACT: Characterization was investigated on the 38 kDa and 42 kDa chitinase (EC3.2.1.14) isozymes from the liver of Japanese common squid Todarodes pacificus . Optimum pH toward colloidal chitin was observed at pH 3.0 for the 38 kDa chitinase, and pH 3.0 and 9.0 for the 42 kDa chitinase. K _m and k _cat of the 38 kDa and 42 kDa chitinases toward a longer substrate, glycol chitin, were 0.071 mg/mL and 1.22/s, and 0.074 mg/mL and 0.196/s, respectively. Alternatively, strong substrate inhibition of both chitinases were observed toward a short substrate, N -acetylchitopentaose (GlcNAc₅). Both chitinases decomposed not only chitin but also chitosan (D. A. 95%). The cleavage pattern and reaction rate were investigated using N -acetylchitooligosaccharides (GlcNAc_n, n  = 2–6). Both chitinases hydrolyzed GlcNAc_n ( n  = 4,5, and 6). The release of GlcNAc was not observed. The speed of the reaction was observed to be in the following order: GlcNAc₄ > GlcNAc₅ > GlcNAc₆ for the 38 kDa chitinase, and GlcNAc₆ > GlcNAc₅ > GlcNAc₄ for the 42 kDa chitinase. Both the chitinases released p -nitrophenol from p -nitrophenyl GlcNAc_n ( n  = 2, 3, and 4). N-terminal amino acid sequences of the 38 kDa and 42 kDa chitinases were YLLSXYFTNWSQYRPGAGKYFPQNI and EYRKVXYYTNWSQYREVPAKFFPEN, respectively.     

Possibility for decreasing of mercury content in bluefin tuna <Emphasis Type="Italic">Thunnus orientalis</Emphasis> by fish culture

ABSTRACT:   The bluefin tuna tested were reared for 22 months from eggs before the beginning of the experiment, and sampling was performed every 3 months over the following year. The experimental results showed that the mercury concentration in the muscle ranged from 0.32 to 0.85 μg/g, which is lower than that found in wild bluefin tuna of a similar size. Increase in the mercury concentration corresponding to the increase in body weight was not shown, and it was quite different with wild bluefin tuna. Furthermore, no significant relationship was found between the lipid concentration and the mercury concentration in muscle. Among the internal organs of cultured bluefin tuna, the heart (0.32–0.66 μg/g), liver (0.43–0.99 μg/g) and spleen (0.59–1.0 μg/g) contained higher concentrations of mercury. It was estimated that the full-cycle cultured bluefin tuna had been fed small fish containing lower concentrations of mercury, and that the mercury concentration of tuna would be almost equal throughout the year because the effect of mercury accumulation would be weakened by body growth. Therefore, it was concluded that selecting diet fish species might decrease mercury contents in cultured bluefin tuna.     

Changes in meat texture of three varieties of squid in the early stage of cold storage

ABSTRACT: The present study examined the changes in texture and protein components during cold storage of different squid varieties. Raw oval squid, Japanese common squid and arrow squid were sliced fresh and the muscles were stored at 4°C for 0, 4, 8, 12, 18, 24, 48 and 120 h. The rheological measurements, protein components and amounts of collagen were examined. The adhesiveness of each squid increased significantly in the early stage of cold storage. In all varieties, penetration decreased at 4 h, which is considered to be rigor mortis, then increased. The amounts of total collagen, 20°C water-soluble collagen and 70°C water-soluble collagen did not change significantly in each variety during cold storage. Sodium dodecylsulfate–polyacrylamide gel electrophoresis (SDS-PAGE) pattern showed that the 580 kDa component gradually disappeared up to 48 h. The correlations between the amounts of 580 kDa component and adhesiveness or firmness were high. Models of fit based on chemical kinetics accurately expressed the behavior of adhesiveness, firmness and penetration showing that 63.2% of adhesiveness changes occurred in 13–19 h and that 63.2% of firmness changes occurred in 18–24 h.     

Larval molting and growth of the Japanese spiny lobster Panulirus japonicus under laboratory conditions

ABSTRACT:   Ten newly hatched phyllosoma of Panulirus japonicus were cultured individually to monitor body length ( BL ) and intermolt period, and 2000 were cultured in groups to sample specimens for measurement of body weight. Phyllosoma were fed with Artemia and mussel gonad; the culture seawater temperature was 24–26°C. The individually cultured phyllosoma showed an increment in body length by the first molt of approximately 0.5 mm, and the molt increment increased to approximately 1 mm at 5 mm BL ; it was constant to 15 mm BL . Thereafter, the molt increment increased exponentially. The duration of the first instar was 6–7 days. Instar duration increased with development up to approximately 2 weeks at the 20th instar (∼16 mm BL ) and then became constant. Of the 10 larvae reared individually, five metamorphosed to the puerulus stage. The entire phyllosoma life ranged from 245–326 days (mean 289.0 days), and the number of instars ranged from 22–29 (mean 26.2). Body length in the final instar ranged from 28.50–33.10 mm (mean 30.280 mm). For the phyllosoma cultured in groups, relationships between BL and wet/dry body weights ( WW / DW , mg) were expressed as exponential equations: WW  = 0.0686 BL ^2.2023 and DW  = 0.0209 BL ^2.1905.     

Analysis of mesh breaking loads in cotton gill nets: Possible solution to ghost fishing

ABSTRACT:   A small number of fishers in Chiba Prefecture of eastern Japan use cotton gill nets to catch Japanese spiny lobster Panulirus japonicus. To examine the advantages of cotton gill nets, we analyzed changes in mesh breaking load of a new cotton gill net used in a fishing operation. A new cotton gill net was also soaked in a seawater tank to simulate ghost fishing conditions. The average mesh breaking load of new cotton mesh was 50.3 N. This value decreased to 19.0 N after 38 days (∼912 h), and after 82 days (∼1968 h) the mesh could be easily torn (breaking load 0.07 N). Under fishing conditions, the cumulative soak time was only 744.4 h over 19 months. The average breaking load at the end of this period was 43.1 N, a strength 86% that of the presoaked mesh. The mesh breaking load of a cotton gill net continuously soaked for 744.4 h was 26.1 N, as estimated from tank experiment data. Thus, a cotton gill net maintains reasonable strength under typical use conditions, but will degrade if lost at sea.     

Purification and characterization of lysozyme from purple washington clam Saxidomus purpurata

ABSTRACT:   Lysozyme was purified from purple washington clam Saxidomus purpurata by sequential procedures using Chitopearl Basic BL-01 affinity and TSKgel ODS-120T column chromatographies. Molecular mass of the purified enzyme was estimated to be 12 kDa by SDS-PAGE. Optimum pH of the enzyme was 5.2 toward Micrococcus lysodeikticus cells. The optimum temperature was 50°C. The enzyme was stable in the range of pH 4.8–6.8 and 20–90°C. Further, the N-terminal amino acid sequence of the enzyme showed similarity to lysozymes from invertebrates. However, the specific activity of the enzyme toward M. lysodeikticus cells and p -nitrophenyl penta- N -acetyl- β -chitopentaoside was 143 times and 12 times higher than that of hen egg white lysozyme, respectively.     

Effect of pH-shifting on the gel forming characteristics of salt-ground meat from walleye pollack

ABSTRACT:   In order to elucidate the mechanism of the changes in gel forming characteristics of fish meat by pH-lowering, the gelation-temperature curve and the gelation-moisture content curve were examined using the acidified walleye pollack surimi or neutralized one after acidification. In the gelation-temperature curve, the gel strength was highest at 30°C and lowest at approximately 50–60°C, irrespective of pH shifting. The gel strength at 30°C and 80°C decreased with the decrease in pH value. The neutralization of acidified surimi improved the gel strength, but it was considerably lower than the original gel strength. The gel strength at 50–60°C was not affected by pH lowering. The gel strength at 80°C could not be revived to the original by pH readjustment, either in the presence or in the absence of EDTA. These results suggest that irreversible changes of meat protein take place under the low pH, and the oxidation ability of sulfhydryl (SH) groups of protein molecule is not affected by pH-shifting.