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Myoglobin Analysis for Determination of Beef, Pork, Horse, Sheep, and Kangaroo Meat in Blended Cooked Products
Author(s) -
JANSSEN F.W.,
HÄGELE G.H.,
VOORPOSTEL A.M.B.,
BAAIJ J.A.
Publication year - 1990
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.1990.tb03560.x
Subject(s) - myoglobin , electroblotting , chemistry , food science , urea , nitrocellulose , isoelectric focusing , horse , chromatography , polyacrylamide gel electrophoresis , biochemistry , biology , enzyme , paleontology , membrane
This method allows the concurrent detection of several types of animal muscle meat in comminuted, cooked meat products. Meat proteins were dissolved in a solvent containing 8M urea and dithioerythritol and separated by electrofocusing on an ultra‐thin polyacrylamide gel, containing urea. The proteins were then transferred to nitrocellulose by electroblotting and the blot was incubated with anti‐human myoglobin serum, a linking antibody, peroxidase‐antiperoxidase (PAP) immune complex, and enzyme‐substrate. Detection of less than 10% pork, horse and sheep meat was possible in a beef‐based meat product which had been heated to an internal temperature of 120°C for 5 min. The method is not suitable for detection of chicken and turkey meats.
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