Abstract
An enzymatic method for the determination of free glutamic acid in meat
products and dried soups was collaboratively studied in 11 laboratories.
In the presence of the enzyme glutamate dehydrogenase, L-glutamic acid
is oxidatively deaminated by nicotinamide adenine dinucleotide (NAD) to
2-oxoglutarate. In a reaction catalyzed by diaphorase, the NADH thus
formed converts 2-(p-iodophenyl)-3-(p-nitrophenyl)-5-phenyltetrazolium
chloride to a formazan, which is measured in the visible range at 492
nm. Fourteen samples (7 samples of minced sausage and 7 samples of dried
cauliflower soup) with glutamate contents varying between 0.4 and 16
g/kg were included in the study. Materials were distributed to
participants as blind duplicates and as split level pairs. The mean
relative standard deviation (RSDR) for reproducibility for the dried
soup material containing glutamate between 7 and 16 g/kg was 4.6%. RSDR
values for samples of minced sausage containing glutamate at lower
levels (0.4-1.3 g/kg) were between 12 and 16%.
Original language | English |
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Pages (from-to) | 921-925 |
Journal | Journal of the Association of Official Analytical Chemists |
Volume | 74 |
Issue number | 6 |
Publication status | Published - 1991 |
MoE publication type | A1 Journal article-refereed |