Fragmentation of myofibrils, limited proteolysis and water holding capacity of meat.

Protein changes in ageing meat result in increased vulnerability of the myofibrils to fragmentation, caused possibly by limited proteolysis. It was investigated which groups of muscle proteases, if any, were involved and what was the relation between fragmentation and hydration of beef meat. In samples ranging in natural pH from 5.4 to 7.0 the least fragmentation after 3 days at 2 degrees C was at pH 6. This could suggest the role of both the cathepsins and neutral proteases. In samples aged in the presence of EDTA fragmentation was significantly lower than in the controls. This could indicate the role of Ca2+ activated neutral proteases, or support the hypothesis on the nonenzymatic mechanism involving Ca2+. The results of PAG electrophoresis could not have been due to the neutral proteases, as the 30,000 g X mol-1 component, resulting from the hydrolysis of troponin T, did not accumulate at pH 7 until the 9th day of ageing, but at pH 5.4 the intensity of this band increased markedly already after 3 days. There was no correlation between the fragmentation and the hydration of the aged meat after cooking. The addition of 0.001% of trypsin or 0.0005% of papain to minced meat did not cause after 9 days any increase in the contents of free amino acids and peptides or significant changes in the PAGE pattern as compared to those in the controls. However, the fragmentation and hydration of the raw meat was larger in the samples containing added enzymes. After cooking the hydration of the samples did not differ.(ABSTRACT TRUNCATED AT 250 WORDS)

The role of collagen in the quality and processing of fish.

Collagen in the muscles of fish constitutes the main component of the connective tissue membranes joining individual myotomes and is responsible for the integrity of the fillets. The content of collagen in fish muscles is from about 0.2 to 1.4% and in squid mantel about 2.6%. Fish and invertebrata collagens contain slightly more essential amino acids than intramuscular bovine connective tissue collagen. The invertebrata collagens are exceptionally rich in sugars linked mainly O-glycosidically to hydroxylysine residues. During maturation of fish the proportion of collagen to total protein in the muscles increases while the extent of crosslinking does not change significantly. The thermal properties of fish collagens depend significantly on the content of hydroxyproline and proline residues which in turn is correlated to the temperature of the habitat. Generally the shrinkage temperature of fish skin collagens is about 20 degrees C lower than that of mammalian hide collagens. In several species of fish the weakening of the connective tissues post mortem may lead to serious quality deterioration that manifests itself by disintegration of the fillets, especially under the strain of rough handling and of rigor mortis at ambient temperature. Thermal changes in collagen are the necessary result of the cooking of fish, squid, and minced fish products and contribute to the desirable texture of the meat. However, they may lead to serious losses during hot smoking due to a reduction in the breaking strength of the tissues when heating is conducted at high relative humidity. Because of the high viscosity of gelatinized collagen, it is not possible to concentrate the fish stickwaters, a proteinaceous byproduct of the fish meal industry, to more than 50% dry matter. Better knowledge of the contents and properties of fish collagens could be helpful in rationalizing many aspects of fish processing.

Modification of technological properties of fish protein concentrates.

Fish protein concentrates are mixtures of cross-linked and aggregated molecules of different muscle proteins. The final conformation of the components of the mixtures is formed as a result of procedures applied to convert the raw materials into a product of desirable and stable sensory properties, containing less than 0.1% of lipids. To achieve this end usually extraction with hot organic solvents, mainly isopropyl alcohol and 1,2-dichloroethene, followed by air drying are employed. These conditions bring about denaturation of many of the proteins followed by aggregation of the molecules due to the interaction of reactive functional groups in extended polypeptide chains. In the final product a large proportion of hydrophobic groups is exposed to the solvent and the proteins exhibit an extremely low water affinity. Such concentrates, although valuable as protein supplements, have only limited suitability as active components of various processed foods, as they have poor technological value. They are insoluble or have a very low water dispersibility and swelling ability, do not form gels after heating, or have any significant fat-emulsifying capacity. Changing the dissociation or number of ionic groups of the molecules prior to extraction, e.g., by acidifying or acylating, can partially reduce the denaturing effect of heat and organic solvents and thus improve the functional properties of the product. An upgrading of the quality of concentrates produced by hot extraction can be achieved by partial enzymatic or chemical deaggregation, hydrolysis followed by the plastein reaction, or formation of suitable derivatives. The best results have been obtained by partial hydrolysis of acylated proteins or precipitation of the aggregated products using sodium hexametaphosphate. The functional properties of such products are comparable to those of vegetable protein isolates used as meat extenders. Various proteins of high technological value can be also obtained by enzymatic hydrolysis of the raw material, followed by separation of the lipids without organic solvent extraction. Such products, however, have a distinct odor and flavor and must be stabilized because of residual lipids.

Protein changes in frozen fish.

Storage of frozen fish brings about a decrease of extractability of myofibrillar proteins. There is also deterioration of the texture and functional properties of the flesh. In model systems, aggregation of myosin, actin, tropomyosin, and whole myofibrils have been described. These changes are caused by concurrent action of partial dehydration due to the freezing out of water, exposure of the proteins to inorganic salts which are concentrated in the remaining nonfrozen fluid, interactions with free fatty acids liberated from phospholipids and with lipid oxidation products, and cross-linking by formaldehyde produced in some species of fish as a result of enzymic decomposition of trimethylamine oxide. The extent of protein alterations increases with time and temperature of storage as well as with advanced disintegration of the tissues and intermixing of their components. The role played by the individual factors and the significance of different types of bonds, i.e., hydrophobic adherences, ionic bonds, and covalent cross-links in particular cases are not yet fully disclosed. Retardation of the deteriorative changes of proteins in frozen fish is possible by avoiding high storage temperatures and oxidation of lipids, removing hematin compounds and other constituents promoting cross-linking reactions, and by adding cryoprotectors like sugars, several organic acids, amino acids, or peptides.

[Protein denaturation in frozen fish]. / Zur Frage der Proteindenaturierung im gefrorenen Fischfleisch

To inhibit the rapid deterioration of the production-technological properties of fish meat minced and frozen on board, it is necessary to become acquainted with the causes of protein denaturation under these conditions. It was found that the protein solubility in codfish is impaired by formaldehyde which develops from trimethyl-amine oxide during storage and also by the salt content. After 7 days at -20 degrees C, the solubility of the sarcoplasmic and myofibrillary proteins in minced fish meat added with 80 mg of formaldehyde per 100 g of total protein amounted to almost 70% and 35%, respectively, of the value determined in controls, i.e., samples without formaldehyde. After this period of storage, only 30% of the added formaldehyde were in the free state. After 1 month, the solubility of the myofibrillary proteins in waterleached fish meat was by 30% higher than in unleached controls, 80 mg of formaldehyde per 100 mg of total protein having been added in both cases. After 1 month at -5 degrees C and -20 degrees C, only 90 and 15 p.p.m. of formaldehyde, respectively, were found in minced fish meat, whereas leached samples contained no formaldehyde. The solubility of the myofibrillary proteins in leached fish meat (the initial salt content of which had been restituted) was by 30% lower than in the unleached controls.