Immunochemical Quantification of Heat Denaturation of Bovine Meat Soluble Proteins |
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Authors: | D LEVIEUX A LEVIEUX A VENIEN |
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Affiliation: | The authors are affiliated with INRA, Meat Research Station, Immunochemistry Unit, Theix, 63122 Saint Gene Champanelle, France. |
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Abstract: | 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°C for 30–780 min. Heat denaturation occurred in the following order: transfenin > IgG > LDH M4 > LDH H4 = myoglobin > albumin and could be described by first order reaction kinetics. The very low coefficient of variation (2–4%) of the single radial immunodiffusion technique resulted in a very weak calculated error (± 0.l–0.2°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°C without holding time. |
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Keywords: | meat bovine denaturation protein immunochemical |
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