Enzymatic determination of free glutamic acid in dried soups and in minced sausages: NMKL collaborative study

Tapani Hattula, Harriet Wallin

Research output: Contribution to journalArticleScientificpeer-review

5 Citations (Scopus)

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 languageEnglish
Pages (from-to)921 - 925
Number of pages5
JournalJournal of the Association of Official Analytical Chemists
Volume74
Issue number6
Publication statusPublished - 1991
MoE publication typeA1 Journal article-refereed

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soups
sausages
glutamic acid
Glutamic Acid
glutamates
NAD (coenzyme)
acid
meat
chloride
enzyme
sampling
NAD(P)H dehydrogenase (quinone)
glutamate dehydrogenase
Dihydrolipoamide Dehydrogenase
Formazans
cauliflower
Glutamate Dehydrogenase
Meat Products
meat products
reproducibility

Cite this

@article{9bf851bb3d554b84a52bbb699e6cf7c4,
title = "Enzymatic determination of free glutamic acid in dried soups and in minced sausages: NMKL collaborative study",
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{\%}.",
author = "Tapani Hattula and Harriet Wallin",
note = "Project code: ELI4533",
year = "1991",
language = "English",
volume = "74",
pages = "921 -- 925",
journal = "Journal of AOAC International",
issn = "1060-3271",
publisher = "AOAC International",
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Enzymatic determination of free glutamic acid in dried soups and in minced sausages : NMKL collaborative study. / Hattula, Tapani; Wallin, Harriet.

In: Journal of the Association of Official Analytical Chemists, Vol. 74, No. 6, 1991, p. 921 - 925.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Enzymatic determination of free glutamic acid in dried soups and in minced sausages

T2 - NMKL collaborative study

AU - Hattula, Tapani

AU - Wallin, Harriet

N1 - Project code: ELI4533

PY - 1991

Y1 - 1991

N2 - 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%.

AB - 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%.

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JO - Journal of AOAC International

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