DL-Aspartic acid
[CAS# 617-45-8]

Identification

• Classification: Biochemical >> Amino acids and their derivatives >> Alpha--amino acid
• Name: DL-Aspartic acid
• Synonyms: DL-2-Aminobutanedioic acid; DL-Aminosuccinic acid
• Molecular Formula: C₄H₇NO₄
• Molecular Weight: 133.10
• Protein Sequence: D
• CAS Registry Number: 617-45-8
• EC Number: 210-513-3
• SMILES: C(C(C(=O)O)N)C(=O)O

Properties

• Melting point: 300 °C
• Water solubility: SOLUBLE

Safety Data

• Hazard Symbols: GHS07 Warning
• Risk Statements: H315-H319-H335
• Safety Statements: P233-P260-P261-P264-P271-P280-P302+P352-P304-P304+P340-P305+P351+P338-P312-P321-P332+P313-P337+P313-P340-P362-P403-P403+P233-P405-P501

Hazard Classification

Hazard	Class	Category Code	Hazard Statement
Eye irritation	Eye Irrit.	2	H319
Skin irritation	Skin Irrit.	2	H315

Discovery and Applications

DL-Aspartic acid is a synthetic form of aspartic acid, an amino acid involved in various metabolic processes. It consists of two stereoisomers, D-aspartic acid and L-aspartic acid, which are mirror images of each other. While L-aspartic acid is naturally occurring and found in proteins, D-aspartic acid plays a role in the regulation of hormone production, particularly in the nervous and reproductive systems. The DL form, a racemic mixture, combines both isomers and is used in various research and industrial applications.

Aspartic acid was first isolated from asparagus juice in 1827 by the chemists Plisson and Henry. The development of synthetic methods allowed for the production of DL-aspartic acid, which provided a mixture of both the biologically active L-form and the less common D-form. The distinction between the two isomers was crucial in the understanding of their individual roles in biochemistry and physiology. L-aspartic acid is incorporated into proteins and participates in the citric acid cycle, while D-aspartic acid is involved in neurological and endocrine functions.

DL-Aspartic acid is used in the food industry as a precursor in the production of sweeteners like aspartame. Aspartame, a widely used artificial sweetener, is synthesized from L-aspartic acid and L-phenylalanine. The demand for synthetic aspartic acid increased as artificial sweeteners became more prevalent in food and beverage products. The DL form can be used as a starting material for the selective production of L-aspartic acid during industrial processes, ensuring the availability of this key ingredient.

In biochemical research, DL-aspartic acid is employed as a standard in amino acid analysis and in studies exploring the behavior of racemic mixtures. Since the two isomers of aspartic acid can have different effects on biological systems, the DL form serves as a control in experiments investigating their roles. This racemic mixture is also useful in studying enzyme specificity, as many enzymes selectively recognize one isomer over the other.

Another important application of DL-aspartic acid is in the pharmaceutical industry. It can be used in the synthesis of drugs and biologically active molecules. Additionally, D-aspartic acid, which is present in the DL mixture, has been studied for its potential role in enhancing testosterone levels, leading to interest in its use in supplements aimed at supporting male reproductive health. While the L-isomer is more commonly associated with metabolic functions, D-aspartic acid's potential impact on hormone regulation has attracted attention in the field of sports nutrition and endocrinology.

Safety considerations regarding DL-aspartic acid are minimal, as it is generally regarded as safe when consumed in normal dietary amounts. However, supplements containing high doses of D-aspartic acid have prompted research into their long-term effects, particularly in relation to hormone regulation.

In summary, DL-aspartic acid is a versatile compound with applications in food production, pharmaceutical development, and biochemical research. Its discovery and synthesis allowed for advances in understanding the roles of stereoisomers in biological systems, and it continues to be a valuable tool in both industrial and scientific contexts.

References

1979. The isolation, characterization and partial sequence of a peptide rich in glutamic acid and aspartic acid (HGA-2 peptide) from calf thymus non-histone chromosomal protein HMG 2. The Biochemical Journal, 179(2).
URL: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1186617

1990. Channel kinetics determine the time course of NMDA receptor-mediated synaptic currents. Nature, 346(6284).
DOI: 10.1038/346565a0

1979. Effect of ATP translocation on citrulline and oxaloacetate synthesis by isolated rat liver mitochondria. Archives of Biochemistry and Biophysics, 195(2).
DOI: 10.1016/0003-9861(79)90340-0