Optically pure alpha-amino acids production by the "Hydantoinase Process"

Area of Science:

• Biotechnology
• Organic Chemistry
• Enzymology

Background:

• Optically pure D- and L-amino acids are vital chiral building blocks in pharmaceuticals, agriculture, and food industries.
• Their specific biological activity is determined by structure, chirality, and purity.
• Traditional chemical synthesis yields racemic mixtures and is environmentally unfavorable.

Purpose of the Study:

• To review the industrial production of optically pure amino acids.
• To highlight the advantages of enzymatic synthesis, particularly the Hydantoinase Process.
• To discuss the evolution of this process towards industrial applications.

Main Methods:

• The Hydantoinase Process involves a cascade of enzymatic reactions.
• Stereoselective hydrolysis of D,L-5-monosubstituted hydantoin by hydantoinase.
• Enantioselective hydrolysis of N-carbamoyl alpha-amino acids by N-carbamoylase.
• Simultaneous racemization of remaining hydantoin by hydantoin racemase.

Main Results:

• The Hydantoinase Process enables the stereoselective production of optically pure amino acids.
• This enzymatic method offers higher yields and enantioselectivity compared to chemical synthesis.
• The process is more environmentally sustainable.

Conclusions:

• The Hydantoinase Process is a key enzymatic strategy for industrial production of optically pure amino acids.
• Advancements include using isolated enzymes, microbial systems, and recombinant technologies.
• This approach provides an efficient and green route for obtaining essential chiral compounds.