17398-16-2

Usage

Uses

Used in Fragrance and Flavor Industry:
Pyrazine, ethyltrimethyl(8CI,9CI) is used as a fragrance and flavoring agent for its pleasant, tobacco-like scent. It is incorporated into various products to enhance their aroma and taste.
Used in Dye Manufacturing:
Pyrazine, ethyltrimethyl(8CI,9CI) is used as a solvent in the manufacturing of dyes. Its properties allow for efficient dye production and improved product quality.
Used in Resin Production:
In the resin industry, Pyrazine, ethyltrimethyl(8CI,9CI) serves as a solvent, aiding in the manufacturing process and contributing to the final product's characteristics.
Used in Pharmaceutical Industry:
Pyrazine, ethyltrimethyl(8CI,9CI) is utilized as a solvent in the production of pharmaceuticals, facilitating the manufacturing process and potentially enhancing the effectiveness of the final product.
Used as a Precursor in Organic Synthesis:
Pyrazine, ethyltrimethyl(8CI,9CI) is used as a precursor in the synthesis of various organic compounds, enabling the creation of a wide range of chemical products.
Safety Precautions:
It is important to handle Pyrazine, ethyltrimethyl(8CI,9CI) with caution, as it can be harmful if inhaled or ingested, and may cause skin and eye irritation upon contact. Proper safety measures should be taken during its use and storage to minimize potential risks.

InChI:InChI=1/C9H14N2/c1-5-9-8(4)10-6(2)7(3)11-9/h5H2,1-4H3

Upstream product

• 68303-35-5 2-chloro-3,5,6-trimethylpyrazine 
• 74-96-4 ethyl bromide 
• 103404-72-4 LysLeu*acetate 
• 78-98-8 2-oxopropanal 
• 106325-92-2 Lys-Cys 
• 56-87-1 L-lysine 
• 56-86-0 L-glutamic acid 
• 63-91-2 L-phenylalanine 
• 492-62-6 alpha-D-glucopyranose 
• 56-40-6 glycine 

Relevant academic research and scientific papers

Impact of the N-terminal amino acid on the formation of pyrazines from peptides in maillard model systems

Only a minor part of Maillard reaction studies in the literature focused on the reaction between carbohydrates and peptides. Therefore, in continuation of a previous study in which the influence of the peptide C-terminal amino acid was investigated, this study focused on the influence of the peptide N-terminal amino acid on the production of pyrazines in model reactions of glucose, methylglyoxal, or glyoxal. Nine different dipeptides and three tripeptides were selected. It was shown that the structure of the N-terminal amino acid is determinative for the overall pyrazine production. Especially, the production of 2,5(6)-dimethylpyrazine and trimethylpyrazine was low in the case of proline, valine, or leucine at the N-terminus, whereas it was very high for glycine, alanine, or serine. In contrast to the alkyl-substituted pyrazines, unsubstituted pyrazine was always produced more in the case of experiments with free amino acids. It is clear that different mechanisms must be responsible for this observation. This study clearly illustrates the capability of peptides to produce flavor compounds such as pyrazines.

Formation of pyrazines in maillard model systems of lysine-containing dipeptides

Whereas most studies concerning the Maillard reaction have focused on free amino acids, little information is available on the impact of peptides and proteins on this important reaction in food chemistry. Therefore, the formation of flavor compounds from the model reactions of glucose, methylglyoxal, or glyoxal with eight dipeptides with lysine at the N-terminus was studied in comparison with the corresponding free amino acids by means of stir bar sorptive extraction (SBSE) followed by GC-MS analysis. The reaction mixtures of the dipeptides containing glucose, methylglyoxal, and glyoxal produced 27, 18, and 2 different pyrazines, respectively. Generally, the pyrazines were produced more in the case of dipeptides as compared to free amino acids. For reactions with glucose and methylglyoxal, this difference was mainly caused by the large amounts of 2,5(6)-dimethylpyrazine and trimethylpyrazine produced from the reactions with dipeptides. For reactions with glyoxal, the difference in pyrazine production was rather small and mostly unsubstituted pyrazine was formed. A reaction mechanism for pyrazine formation from dipeptides was proposed and evaluated. This study clearly illustrates the capability of peptides to produce flavor compounds that can differ from those obtained from the corresponding reactions with free amino acids.

Pyrazine biosynthesis in corynebacterium glutamicum

The volatile compounds released by Corynebacterium glutamicum were collected by use of the CLSA technique (closed-loop stripping apparatus) and analysed by GC-MS. The headspace extracts contained several acyloins and pyrazines that were identified by their synthesis or comparison to commercial standards. Feeding experiments with [2H7]acetoin resulted in the incorporation of labelling into trimethylpyrazine and tetramethylpyrazine. Several deletion mutants targeting genes of the primary metabolism, were constructed to elucidate the biosynthetic pathway to pyrazines in detail. A deletion mutant of the ketol-acid reductoisomerase was not able to convert the acetoin precursor (S)2-acetolactate into the pathway intermediate (R)-2,3-dihydroxy-3-methylbutanoate to the branched amino acids. This mutant requires valine, leucine, and isoleucine for growth and produces significantly higher amounts and more different compounds of the acyloin and pyrazine classes. Gene deletion of the acetolactate synthase (AS) resulted in a mutant that is not able to convert pyruvate into (5)-2-acetolactate. This mutant also requires branched amino acids and produces only very small amounts of pyrazines likely from valine via the valine biosynthetic pathway operating in reverse order. A ΔASΔKR double mutant was constructed that does not produce any pyrazines at all. These results open up a detailed biosynthetic model for the formation of alkylated pyrazines via acyloins.