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Minced Muscle (minced + muscle)
Selected AbstractsAnti-oxidant activity of added tea catechins on lipid oxidation of raw minced red meat, poultry and fish muscleINTERNATIONAL JOURNAL OF FOOD SCIENCE & TECHNOLOGY, Issue 6 2001Shuze Tang The comparative anti-oxidative effects of added tea catechins (TC) and ,-tocopherol to raw minced red meat (beef and pork), poultry (chicken, duck and ostrich) and fish (whiting and mackerel) muscle on susceptibility to lipid oxidation were investigated during 10 days of refrigerated (4 °C) display. Fresh meats, poultry and fish, purchased from a local market, were trimmed to remove bones, skin and surface fat and minced through a 4 mm plate. The minced muscle of each species was treated with either the addition of 300 mg TC kg,1 minced muscle (TC300) or 300 mg ,-tocopherol kg,1 minced muscle (VE300). Minced muscle without any additives served as control (C). Oxidative stability (TBARS) was measured at 3-day intervals. Total lipids, fatty acid composition, total iron and haem iron from minced muscle for each species were also analysed. The susceptibility of untreated minced muscle to lipid oxidation was in the decreasing order: mackerel > beef > duck > ostrich > pork , chicken > whiting. This may be because of the different content of total fat, iron and fatty acid composition between species. The TC300 significantly (P < 0.05) reduced lipid oxidation compared with controls for all seven species as shown by lower TBARS values. The anti-oxidant potential of TC was two to fourfold greater than that of ,-tocopherol at the same concentration and this potential was species dependent. The VE300 showed limited capacity in inhibiting lipid oxidation for pork, chicken, duck and whiting. The results obtained show that TCs are powerful natural antioxidants when used in minced muscle food. [source] ROLE OF INITIAL MUSCLE pH ON THE SOLUBILITY OF FISH MUSCLE PROTEINS IN WATERJOURNAL OF FOOD BIOCHEMISTRY, Issue 4 2004STEPHEN D. KELLEHER The solubility of the myofibrillar and cytoskeletal proteins in water was determined for the muscle tissue often species offish. The flesh of six white-muscled fish had pH's at the time of processing above pH 6.6 and greater than 80% of their myofibrillar/cytoskeletal proteins were soluble in water. The flesh of three pelagic species and a shark had pH values when processed below 6.6 and the water solubility of their myofibrillar and cytoskeletal proteins was less than 40%. When the washed minced muscle of one of the white-fleshed species, cod, was exposed to low pH, the solubility of its myofibrillar and cytoskeletal proteins decreased substantially. The water solubility of the cod myofibrillar and cytoskeletal proteins could be reestablished by washing the acid-treated cod flesh with neutral salt solutions. It is suggested that pH values below 6.6 modify certain proteins which prevent the water-extractability of the rest of the myofibrillar and cytoskeletal proteins from being expressed. [source] | ||||||||||