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Immunochemical Quantification of Heat Denaturation of Bovine Meat Soluble Proteins
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ABSTRACTImmunoquantification 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.
Title: Immunochemical Quantification of Heat Denaturation of Bovine Meat Soluble Proteins
Description:
ABSTRACTImmunoquantification 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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