QUANTITATIVE CHANGES IN WHOLE MYOFIBRILS AND MYOFIBRILLAR PROTEINS DURING FROZEN STORAGE OF TRUE COD

The extractability of whole myofibrils from true cod decreased more rapidly during frozen storage at −40°C than did the extractability of the component myofibrillar proteins. There was a 95% decrease in extractable myofibrils after 6 months in storage, but only a 23% decrease in extractable myofibrillar proteins.     

THE TEXTURE OF COD MUSCLE

Data on moisture, protein content and pH (after 24 h in ice post mortem) of the flesh of cod of different sizes, captured during several fishing expeditions from Aberdeen to northern fishing grounds in spring and autumn, have been examined in relation to the texture of the cooked material. It is concluded that large fish are slightly tougher than small fish, even when the pH is the same. In addition, the pH of large fish is often lower than that of small fish, so the relative toughness of large fish is enhanced. However, the size-pH relationship is clearly defined only in well-fed fish at certain times of the year. At other times, when food is scarce, the post-mortem pH of the muscle of all sizes of cod varies within wide limits, so that size no longer appears to influence the texture. Of the parameters studied, the post-mortem pH correlated best with the texture after cooking. Since fish with a high pH usually have a high water content, there was also a correlation between texture and moisture. However, the protein content seemed to exercise a negligible influence on texture, an unexpected finding considering that protein accounts for nearly all the ‘substance’ of white fish flesh after the water has been removed.     

CHANGES IN TEXTURE AND MICROSTRUCTURE OF PRESSURE-TREATED FISH MUSCLE TISSUE DURING CHILLED STORAGE

Activities of four endogenous enzymes (cathepsin C, collagenase, chymotrypsin- and trypsin-like enzymes), as well as firmness/strength and elasticity of pressurized fish tissues were monitored over 3 weeks of storage (4–7C). Results indicate that pressurization of fish muscle at 1,000 atm increased firmness whereas pressurization at 2,000 atm or 3,000 atm caused an opposite effect. Changes in tissue elasticity also showed similar trends with correlation between firmness and elasticity. During storage, pressure-inactivated enzymes were reactivated to various extents depending on level of pressurization. Scanning electron microscopy of the tissues revealed some morphological changes with pressurization. At 1,000 atm, there were no significant changes in the myofibers while pressurization at 2,000 atm and 3,000 atm resulted in breakdown of myofibers and connective tissue networks. The results indicate that pressurization may be used to enhance and maintain fresh seafood texture during storage.     

EFFECT OF IN SITU FORMALDEHYDE PRODUCTION ON SOLUBILITY AND CROSS-LINKING OF PROTEINS OF MINCED RED HAKE MUSCLE DURING FROZEN STORAGE

Three forms of minced red hake muscle representing whole-mince, mince with the low molecular weight fraction removed (reconstituted-minced) and mince with low and high molecular weight soluble fractions removed (washed-minced) were stored frozen with added Fe⁺² and ascorbate (trimethylamine oxide (TMAO) was added when necessary). The production of DMA and free formaldehyde was measured as were the decreases in water-soluble and salt-soluble proteins and TMAO as a function of increasing concentrations of ascorbate. Dimethylamine (DMA) production and loss of overall protein extractability were greatest in minced muscle, followed by reconstituted-minced muscle, and least in washed-minced muscle. The minced muscle lost water-soluble proteins, however, less rapidly than the reconstituted-minced muscle. The percentage of formaldehyde that was bound was highest in the minced, next in the reconstituted-minced and least in the washed-minced muscle. This supports earlier data and indicates that formaldehyde reacts with both the small molecular weight fraction and the water-soluble proteins as well as the contractile proteins. Loss of protein extractability in all samples appeared to be heavily dependent on hydrophobic interactions. Disulfide interactions appeared to occur to some extent in the reconstituted-minced and washed-minced muscle but were a minor factor with the minced muscle samples. Surface hydrophobicity of the proteins was inversely related to their extractability. In the sample of minced muscle with the highest concentration of added ascorbate where approximately 79% of the proteins became inextractable, some 2% of the muscle proteins were covalently linked in polymers with molecular weights greater than that of the myosin heavy chains. The data indicate that cross-linking of protein components occurs as well as hydrolysis of a considerable amount of the protein.     

CHANGES IN MOLECULAR SPECIES COMPOSITIONS OF GLYCEROPHOSPHOLIPIDS IN THE ADDUCTOR MUSCLE OF THE GIANT EZO SCALLOP PATINOPECTEN YESSOENSIS DURING FROZEN STORAGE

Changes in lipid components, particularly glycerophospholipids, in the adducto; muscle of giant ezo scallop during storage at −20C were investigated. During storage, the contents of total lipids (TL) and polar lipids (PL) decreased, but that of nonpolar lipids increased. Thiobarbituric acid reactive substances and peroxide values of the TL increased with duration of storage. Glycerylphosphorylcholine (GPC) and glycerylphosphrylethanolamine (GPE) decomposed considerably during storage, and decreased by 50% and 15% of the initial content, while lyso-PC (LPC) and free fatty acids (FFA) increased, respectively. The percentages of polyunsaturated fatty acids (PUFAs) such as 20:5n-3 and 22:6n-3 in the TL and PL during storage decreased, however, those of the PUPAs in the NL increased. Diacylglycerylphosphorylcholine (diacyl-GPC) and diacylglycerylophosphorylethanolamine (diacyl-GPE), major components in the GPC and GPE subclasses, showed a marked decrease with duration of storage. Particularly, diacyl-GPC decreased by 68% of the initial contents of the PL. In the alkenylacyl-GPE and diacyl-GPC, the percentages of the molecular species having longer hydrocarbon chains on the sn-l positions of glycerol moieties decreased at     

ALTERATION IN LIPID OXIDATION OF CHANNEL CATFISH DURING FROZEN STORAGE IN RESPONSE TO ASCORBATE APPLICATIONS

Channel catfish were treated with ascorbate via metabolic absorption and vacuum tumbling. The fillets were subjected to varying periods (0, 1.5, 3, 4.5, and 6 months) of frozen storage at −6C. When muscle ascorbic acid levels were increased two fold by both methods, TBA-RS values were significantly lower than that of the control after 6 months of storage. Vacuum tumbled fillets with muscle ascorbic acid that increased by four fold were found to be the least stable to oxidation. The possible fate of the ascorbic acid in the fish tissue was discussed.     

EFFECTS OF CRYOPROTECTANTS IN MINIMIZING PHYSICOCHEMICAL CHANGES OF BOVINE NATURAL ACTOMYOSIN DURING FROZEN STORAGE1

Physicochemical changes in bovine natural actomyosin extracted from prerigor semimembranosus muscle were investigated during frozen storage at ?28°C as affected by the addition of cryoprotectants (5.6% Polydextrose® or 5.6% mixture (1:1) of sucrose and sorbitol). Proteins were destabilized during freezing and frozen storage as reflected by decreases in protein solubility, the visual appearance of aggregates in protein sols, decrease in intensity of flow birefringence, intrinsic viscosity and ATPase activity, and changes in size, shape, or charge of the protein (especially myosin) as evidenced by nondenaturing electrophoresis. These effects were reduced to some extent by the two cryoprotectant treatments.     

QUALITATIVE AND QUANTITATIVE CHANGES IN AEROBIC MICROFLORA FROM INTESTINAL CONTENTS OF SOUTH-BALTIC COD DURING STORAGE AT 1-2°C

SUMMARY— The bacterial flora of the intestinal content of cod (Gedus morrhua L) were investigated during a period of 1 year. The quantity of bacteria in recently caught fish was studied during the full period. the quality during only 6 months. 3 groups of fish from the same capture and fishing grounds were analyzed: fresh, and stored at 1–2°C for 5 and 10 days. It was seen that in general gram-positive bacterial flora dominated in recently caught fish, while after 5 and 10 days of storage gram-negative flora our numbered the former. In the intestinal contents of fresh fish the Vibrio species dominated, whereas at storage, Pseudomonas spp. became dominant. In fresh fish, the bacterial flora of stored fish amounted to 3.10% of the total initial quantity after 5 days of storage and 1.5% after 10 days. Also, the gram-positive flora decreased comparatively more rapidly than gram-negative flora. The authors believe that the temperature of 1–27°C may play a part in the decreasing number of flora, as well as some other factors not investigated in the present research.     

TEXTURE OF FISH MUSCLE

Morphological and chemical aspects of fish muscle texture are reviewed and differences from red meat are pointed out. A unique feature of fish muscle is its low connective tissue content which accounts for easy disintegration of fish flesh on heating. Thus, the muscle fibers are the main textural elements in cooked fish meat. Because of this, most of the popular texture testing instruments are not applicable to fish. Best results are obtained with the thin blade shear/compression cell.
Texture of fish muscle is affected by the species, age and size of the fish within the species, and nutritional state. Postmortem factors influencing texture include glycolysis, rigor mortis and the accompanying contraction of the muscle often leading to the separation of muscle segments (gaping), temperature profile during storage, temperature of cooking, pH and presence of NaCl.