Gas chromatography of tryptophan together with other amino acids in hydrochloric acid hydrolysates

V. Fábián, M. Pintér-Szakács, I. Molnár-Perl

Research output: Contribution to journalArticle

19 Citations (Scopus)

Abstract

The classical hydrolysis of proteins with hydrochloric acid using tryptamine [3-(2-aminoethyl)indole] as additive revealed that tryptophan can be measured without destruction together with other amino acids by gas chromatography. An extensive study was made to establish the optimum conditions for protein hydrolysis (time and temperature of hydrolysis, amount of tryptamine) and for the derivatization of amino acids. The amino acid contents (including tryptophan) of standard proteins such as lysozyme, bovine and human albumin, human γ-globulin, casein and α-chymotrypsin and protein matrices (meat and fish meals, sunflower) were determined, after hydrochloric acid hydrolysis (4 h, 145°C) in the presence of tryptamine, as N,O,(S)-trifluoroacetyl isobutyl esters with SE-30 as the stationary phase. The reproducibility of the measurements was 4.6% (relative standard deviation) or less.

Original languageEnglish
Pages (from-to)193-199
Number of pages7
JournalJournal of Chromatography A
Volume520
Issue numberC
DOIs
Publication statusPublished - Nov 9 1990

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Hydrochloric Acid
Tryptophan
Gas chromatography
Gas Chromatography
Hydrolysis
Amino Acids
Proteins
Silicone Elastomers
Meats
Helianthus
Globulins
Chymotrypsin
Muramidase
Caseins
Meat
Fish
Meals
Albumins
Fishes
Esters

ASJC Scopus subject areas

  • Analytical Chemistry
  • Clinical Biochemistry
  • Molecular Medicine

Cite this

Gas chromatography of tryptophan together with other amino acids in hydrochloric acid hydrolysates. / Fábián, V.; Pintér-Szakács, M.; Molnár-Perl, I.

In: Journal of Chromatography A, Vol. 520, No. C, 09.11.1990, p. 193-199.

Research output: Contribution to journalArticle

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