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Immunochemical quantification of heat denaturation of bovine meat soluble proteins
- Levieux, D., Levieux, A., Venien, A.
- Journal of food science 1995 v.60 no.4 pp. 678-684
- beef, immunoglobulins, lactate dehydrogenase, myoglobin, transferrin, denaturation, heat treatment, duration, immunochemistry, kinetics, protein content, thermodynamics, temperature, equations, solubility
- Immunoquantification of myoglobin, L-lactic dehydrogenases (LDH) M4 and H4, albumin, transferrin and immunoglobulin G (IgG) was performed after heat treatment of crude soluble sarcoplasmic protein extract over a range of 54-70 degrees C for 30-780 min. Heat denaturation occurred in the following order: transferrin > IgG > LDH M4 > LDH H4 = myoglobin > albumin and could be described by first order reaction kinetics. The very low coefficient of variation (24%) of the single radial immunodiffusion technique resulted in a very weak calculated error (+/- 0.1-0.2 degrees C) on temperature determination. Monitoring the concentration of LDH M4 appears appropriate for determining the minimum heating achieved in long-time low-temperature cooking and albumin or myoglobin could be monitored for meat cooked at 69 degrees C without holding time.