Low-ingredient meat products and method for their preparation
A technology for meat products and minced meat, which is applied in the field of preparing low-ingredient meat products, and can solve the problems of not being able to improve cooking losses, etc.
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Embodiment 1
[0041] Tyrosinase-catalyzed cross-linking of myofibrillar proteins isolated from chicken breast muscle
[0042] Molecular weight and mobility of isolated salt-soluble protein (SSP) from chicken breast muscle fibrils induced by Trichoderma reesei tyrosinase were analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) The change. SSPs were isolated according to Xiong and Brekke (1989). SSP was suspended in 50 mM sodium phosphate buffer (pH 6, containing 0.6M NaCl) to a protein concentration of 3 mg / ml. Tyrosinase was added at 60, 120 and 240 nkat per gram of protein. The reaction mixture was incubated at 40°C. Samples were taken at 5 minutes, 1 hour, 3 hours and 18 hours. Major changes in protein bands on SDS-PAGE catalyzed by tyrosinase were tentatively identified. Tyrosinase caused the following detectable electrophoretic changes: 1) appearance of large proteins below the wells, 2) disappearance of myosin heavy chain, and 3) disappearance of tropo...
Embodiment 2
[0044] Tyrosinase-catalyzed cross-linking of myofibrillar proteins isolated from rainbow trout fillets
[0045]Changes in molecular weight and mobility of isolated myofibrillar proteins from rainbow trout fillets catalyzed by Trichoderma reesei tyrosinase were analyzed by SDS-PAGE. Basically, myofibrillar protein was isolated in the same manner as chicken breast muscle fibrils in Example 1. Isolated myofibrils were suspended in water containing 8% sucrose to keep the protein in solution. The pH of the suspension was not adjusted. Myofibrillar protein (3 mg / ml) was first treated with different levels of tyrosinase in order to evaluate the cross-linking efficiency of the enzyme. 20, 40, 80, 160, 320 and 640 nkat tyrosinase were added per gram of protein. The reaction mixture was incubated at 40°C for 2 hours, after which samples of the reaction mixture were run on SDS-PAGE. According to the results of SDS-PAGE, tyrosinase doses of 160 and 640nkat / g were selected for further ...
Embodiment 3
[0047] Improvement of gel formation of chicken myofibrils by tyrosinase
[0048] The ability of tyrosinase to form crosslinks in a 4% suspension of chicken myofibrils was investigated as the generation of storage modulus (G') measured the improvement in gel formation induced by tyrosinase at low deformation. Measurements were carried out during heating at 25°C and 40°C using a Bohlin VOR rheometer (Bohlin Reologi, Lund, Sweden) ( figure 1 ). Isolation of chicken breast muscle fibrils according to Xiong and Brekke (1989), omitting EDTA and NaN from the isolation buffer 3 . Isolated myofibrils were suspended in 50 mM sodium phosphate buffer (0.35M NaCl, pH 6) to a protein concentration of 4%. Samples of myofibril suspension were treated with 0, 30, 60, 120 and 240 nkat Trichoderma reesei tyrosinase / g protein at 25°C and 40°C for 3 hours. The results indicated that G' was increased in tyrosinase-treated myofibril suspensions compared to those treated in buffer only. Furtherm...
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