Solubilization of type I and V collagens in Japanese flounder muscle during chilled storage

ABSTRACT:   The post-mortem changes of type I and V collagens in Japanese flounder muscle during chilled storage were examined. The muscle softened significantly within 12 h under chilled storage. Both type I and V collagens isolated by ion-exchange chromatographies showed no remarkable changes in band patterns even after 24 h of storage, suggesting that degraded collagen molecules may be removed from the collagen fraction by a conventional preparation method. In contrast, type I and V collagen molecules were detected by Western blotting with each specific antibody in a saline extract and gradually increased during chilled storage. These results suggest that both type I and V collagens may participate in the post-mortem softening of fish muscle.     

Suppression of fish meat softening by strict control of storage temperature

ABSTRACT:   Changes in meat firmness and structure of cultured yellowtail at several storage temperatures, from −1.5°C to 10°C, were compared. Firmness decreased less at −1.5°C and 10°C than at the other temperatures. During storage at temperatures from −0.5 to 4.0°C, expansion of intercellular space, which indicates weakening of the connecting force between muscle cells, began to increase after 8 h storage, and the ratio of space to the whole area increased by 3.4–4.9 times after 24 h of storage. However, at −1.5°C and 10°C, the increase of intercellular space was suppressed, and the ratio was 2.4–2.6 times, even after 24 h storage. Collagen fibrils connecting muscle cells disintegrated after 24 h storage at all storage temperatures. Conversely, in 10°C storage, the fine structure of muscle, except for collagen fibrils, was maintained better than at other storage temperatures. These findings indicate that −1.5 and 10°C storage could maintain fish-meat quality for longer periods than storage at −0.5, 1.0, or 4.0°C, the normal refrigeration temperature.     

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.     

Quality of Filleted Atlantic Mackerel (Scomber Scombrus) During Chilled and Frozen Storage: Changes in Lipids,Vitamin D,Proteins, and Small Metabolites,including Biogenic Amines

Quality changes of vacuum-packed Atlantic mackerel (Scomber scombrus) fillets during 12 months’ frozen storage at ?27°C and 9 days’ chilled storage at +4°C were evaluated. Freezing at ?27°C preserved the long chain n-3 polyunsaturated fatty acids (LC n-3 PUFAs), both in light and dark muscle, vitamin D, and the low molecular weight metabolites (LMW) (studied by high resolution nuclear magnetic resonance spectroscopy, HR NMR). Protein oxidation took place, especially between 1 and 7 months, decreasing water holding capacity and protein extractability. During chilled storage, no lipid or protein oxidation was observed, but lipolysis increased, and several LMW metabolites relevant for sensory and nutritional quality degraded into non-favorable compounds. The content of biogenic amines was high at day 9 (e.g., 18 mg histamine/100 g), jeopardizing safety. Preservation of mackerel fillets by freezing at ?27°C is thus a better option compared to prolonged chilled storage at +4°C; the quality was well preserved for 12 months’ frozen storage.     

Immunological detection of translation products of type V/XI collagen α1 gene and their degradation products in red sea bream muscle

We previously cloned cDNA of type V/XI collagen α1 chain (ColVa1) gene from cultured cells derived from red sea bream embryo. We raised an antibody against the deduced C-telopeptide of ColVa1 in order to detect the translation products of this cDNA and their degradation products in red sea bream muscle. To improve its specificity, the antibody was purified from rabbit antiserum by use of an affinity column cross-linked with recombinant C-terminal peptide of ColVa1 produced by Epicurian coli. The purified antibody recognized a band corresponding to the α chain of type V/XI collagen in western blot analysis of the extract of cultured cells. The antibody also recognized two bands in acid-soluble and pepsin-solubilized collagens, indicating that the translation products of the ColVa1 gene are present in muscle and that bands correspond to α and β chains of type V/XI collagen. A band corresponding to a molecular weight of approximately 65 k was detected in the NaOH extracts of muscle, suggesting that type V/XI collagen α1 chain is restrictedly digested in red sea bream muscle.     

Preventive method of color deterioration of yellowtail dark muscle during frozen storage and post thawing

ABSTRACT:   The aim of this study was to develop a practical preventive method for color deterioration of sliced or filleted yellowtail muscle, especially of dark muscle, during frozen storage and post thawing. When the sliced meats were packaged in a vacuum with low oxygen permeable flexible films and then stored frozen below −40°C, no significant discoloration or browning of dark muscle was observed for 9 months or more. For higher temperature storage at −20°C or −30°C, nitrogen gas substituted packaging was a useful practical method for storing sliced meats for 6 weeks. In order to prevent color deterioration of sliced meats after thawing and subsequent storage at 0°C, the efficacy of materials of packaging was investigated. The most desirable result was obtained by using a film with oxygen permeability of 50–90 cm³/m² per 24 h.     

Inhibition of post-mortem muscle softening following in situ perfusion of protease inhibitors in tilapia

ABSTRACT:     A method of introducing protease inhibitors into fish muscle through the bulbus arteriosus was developed using an in situ perfusion technique. Perfusion efficiency was initially tested using eosin and [³⁵S]-methionine. Visible fluorescence was observed in the gill, liver, intestine and dorsal muscle of the eosin-treated tilapia, and the occurrence of eosin in the blood vessels of the dorsal muscle was confirmed under a fluorescence stereoscopic microscope with ultraviolet light. The radioactivity of [³⁵S]-methionine was taken into the dorsal muscle and liver at a concentration of 7.8 Bq/g and 70.2 Bq/g, respectively, after perfusion with 1000 Bq/mL solution. Using the perfusion technique with four kinds of protease inhibitors dissolved in physiological saline, the type of proteases implicated in the post-mortem muscle softening in tilapia (867 ± 195 g, n  = 10/protease inhibitor) was investigated. After the perfusion of leupeptin (serine and cysteine protease inhibitor), benzyloxycarbonyl-Val-Ala-Asp-fluoromethylketone (Z-VAD-fmk; caspase inhibitor), chymostatin (serine protease inhibitor) and ο -phenanthroline (metalloprotease inhibitor), the breaking strength of the perfused muscle was measured as a parameter of the meat toughness and compared with that of the control fish, which were perfused with physiological saline only. The reduction of breaking strength during storage was inhibited by the perfusion of leupeptin and Z-VAD-fmk.     

Degradation of myofibrils in cultured yellowtail <Emphasis Type="Italic">Seriola quinqueradiata</Emphasis> burnt meat: effects of a myofibril-bound EDTA-sensitive protease

“Burnt meat” is a term used to describe the white (pale, grainy, exudative) muscle of yellowtail or tuna. It (with lightness parameter, L* ≥ 55) was observed after 2 h storage in the suffocate in air (SA) 29°C group and after 4 h storage in the spinal cord destruction (SCD) 29°C group. In the SA 17°C group, burnt meat was also observed after 4 h storage. In contrast, the meat in the SCD 17°C group was normal until after 12 h storage. The myosin heavy chain (MHC) was more degraded than the other myofibrillar proteins, and some protein bands increased in the burnt meat. The protease that leads to the degradation of MHC was investigated using myofibrils from the meat. EDTA completely suppressed the degradation, indicating that a myofibril-bound EDTA-sensitive protease (MBESP) may exist in yellowtail muscle and this caused the degradation of MHC. The optimum pH and temperature of MBESP in yellowtail were 5.0 and 50–60°C, respectively.     

Effect of dietary taurine supplementation on growth performance of yellowtail juveniles <Emphasis Type="Italic">Seriola quinqueradiata</Emphasis>

ABSTRACT:   The effect of taurine on growth of yellowtail juveniles Seriola quinqueradiata was investigated by a feeding experiment of diets containing various taurine levels. Test diets supplemented with 0, 0.5, 1.0, 1.5 and 2.0% of taurine were prepared. These diets were fed to yellowtail juveniles with an initial mean body weight of 0.5 g for 6 weeks. Supplementation of taurine in the diet of yellowtail improved their growth performance significantly ( P  < 0.05) over the initial 3-week period. The fish fed with the taurine-supplemented diet improved in percent gain and feed efficiency over both 3 and 6 weeks. Taurine content in the muscle proportionally increased with the dietary taurine level. The fish fed without supplemented taurine diet showed higher contents of serine in the muscle. With each increase in the inclusion level of taurine content in the diet, the concentration of serine in the muscle decreased. The cystathionine content in the muscle of each group was unchanged. These results suggest that taurine supplementation in the diet not only improves growth but also affects the sulfur amino acid metabolism of yellowtail juveniles.