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Organic substances known as amino acids serve as the building blocks of proteins and are essential to many biological processes in living things. Amino acids are utilized in the pharmaceutical, food additive, animal feed, and cosmetics industries. There are multiple processes involved in the industrial preparation of amino acids. Amino acids can first be made through fermentation or chemical synthesis. While fermentation uses microorganisms like bacteria or fungi to digest sugars or other organic substrates into amino acids, chemical synthesis uses sophisticated chemical reactions to create amino acids from basic organic components.
Amino acids are organic molecules whose functional groups are amino (-NH2) and carboxyl (-COOH) and are the basic building blocks of proteins. They are divided into types according to the type of side chains (essential amino acids, non-essential amino acids). There are a variety of functions for amino acids in life, from protein synthesis to metabolic function and controlling physiological processes. Aside from their key functions in the maintenance of life, amino acids are also ubiquitously employed in food, medicine, cosmetics and industry, a key focus of contemporary biotechnology and chemical companies.
Amino acids are organic compounds composed of carbon, hydrogen, oxygen, and nitrogen atoms, and some amino acids also contain sulfur atoms. The central carbon atom in an amino acid is bonded to hydrogen atoms, amino groups (NH2), carboxyl groups (COOH), and side chains (R groups) that distinguish one amino acid from another. It is this unique side chain that gives each amino acid its unique properties and allows the diversity of proteins in nature to exist.
There are 20 standard amino acids commonly found in proteins, each with its own specific side chain that determines its chemical properties and functions. These amino acids can be divided into different categories based on the characteristics of their side chains. There are two main categories: nonpolar amino acids, whose hydrophobic side chains do not interact easily with water, and polar amino acids, whose hydrophilic side chains interact well with water. In addition, amino acids can be further classified as acidic, basic, or neutral, based on the charge of the side chain.
Polar amino acids are essential for maintaining protein solubility in water and promoting interactions with other molecules. These amino acids often participate in hydrogen bonds and play a key role in protein folding and stability. Examples of polar amino acids include serine, threonine, cysteine, tyrosine, asparagine, glutamine, and histidine.
Acidic amino acids, such as aspartic acid and glutamic acid, have side chains that can release hydrogen ions (protons) in solution, making them negatively charged at physiological pH. They play crucial roles in biological systems, such as serving as metabolic intermediates, participating in protein synthesis, and maintaining intracellular pH balance.
Nonpolar amino acids are important for forming the core of globular proteins and stabilizing protein structure through hydrophobic interactions. Examples of nonpolar amino acids include glycine, alanine, valine, leucine, isoleucine, proline, methionine, and phenylalanine.
Basic amino acids, such as lysine, arginine, and histidine, have side chains that can accept hydrogen ions, resulting in a positive charge at physiological pH. These charged amino acids play important roles in enzymatic reactions, protein-protein interactions, and maintaining the overall charge balance within the protein structure.
In nature, over 500 types of amino acids have been identified, but only 20 are considered standard amino acids, which are directly involved in protein synthesis. These amino acids, also known as proteinogenic amino acids, are encoded by the genetic code and are found in almost all living organisms. Additionally, there are non-standard amino acids, such as hydroxyproline and selenocysteine, which are not encoded by the genetic code but play critical roles in specific biological functions. Amino acids are not only foundational to biology but also have extensive applications in food, medicine, and chemical industries. Understanding the types and functions of amino acids aids in advancing life sciences and related technologies.
Based on this, BOC Sciences offers a wide range of amino acids, including natural, standardized, modified and rare amino acids, in both small and large quantities. This supply flexibility enables BOC Sciences to meet orders of all sizes, from research laboratories requiring small quantities for experiments to large production facilities requiring large quantities for manufacturing processes.
| Name | CAS | Catalog | Price |
| L-Arginine hydrochloride | 1119-34-2 | BAT-008148 | Inquiry |
| L-Cysteine Hydrochloride | 52-89-1 | BAT-008076 | Inquiry |
| L-Glutamic Acid Hydrochloride | 138-15-8 | BAT-004723 | Inquiry |
| L-Tyrosine hydrochloride | 16870-43-2 | BAT-004042 | Inquiry |
| L-Aspartic acid | 56-84-8 | BAT-014297 | Inquiry |
| 3-Fluoro-D-phenylalanine | 110117-84-5 | BAT-007834 | Inquiry |
| 2,4-Difluoro-L-Phenylalanine | 31105-93-8 | BAT-014113 | Inquiry |
| Acetyl-β-alanine | 3025-95-4 | BAT-007554 | Inquiry |
| N-Acetyl-DL-aspartic acid | 2545-40-6 | BAT-007715 | Inquiry |
| Phthaloyl-β-alanine | 3339-73-9 | BAT-007602 | Inquiry |
Chiral amino acids refer to amino acids with a chiral center, meaning they exhibit mirror-image isomers in space that cannot be superimposed by rotation or translation. The chirality of amino acids arises from their α-carbon atom, which is bonded to an amino group (-NH₂), a carboxyl group (-COOH), a hydrogen atom, and a side chain (R group). Except for glycine, all amino acids have a chiral center. The most common forms of chiral amino acids are the L-isomers and D-isomers. L-amino acids are the primary form used in protein synthesis within living organisms, whereas D-amino acids are found in certain bacteria and antibiotics. In chiral amino acids, the α-carbon is bonded to four different groups, resulting in two distinct spatial arrangements, analogous to the left and right hands. These mirror-image isomers cannot overlap. To accurately describe these two isomers, the R and S nomenclature is used to represent their different spatial configurations.
The production of amino acids mainly occurs through biological synthesis and chemical synthesis. In biological synthesis, amino acids are synthesized by cells through complex metabolic pathways, typically starting from simple carbon sources like glucose and undergoing a series of enzyme-catalyzed reactions. Plants and microorganisms can synthesize all essential amino acids, while humans and animals must obtain some essential amino acids through their diet. Chemical synthesis, on the other hand, is commonly used in industrial processes, where simple compounds are converted into amino acids through chemical reactions, such as the Strecker reaction or reductive amination. Modern technologies also employ genetic engineering to modify microorganisms for the efficient production of specific amino acids, which are widely used in food, pharmaceuticals, and industrial applications.
The chemical synthesis of amino acids is achieved through organic chemical reactions, with commonly used methods including the Strecker synthesis and reductive amination. Additionally, asymmetric synthesis, which employs chiral catalysts to achieve selective synthesis of specific enantiomers, has become a research hotspot in recent years. This approach is particularly suitable for the preparation of high-value non-natural amino acids, such as pharmaceutical intermediates and specialized functional materials.
In 1850, Strecker first used acetaldehyde, ammonia and HCN to react to obtain α-cyanamide, and then hydrolyzed it to obtain α-amino acids. After Zelinsk's improvement, ammonium chloride and potassium cyanide were used instead of hydrocyanic acid and ammonia, thus avoiding the direct use of hydrogen cyanide or ammonium cyanide, and the same product was obtained after the reaction. When reacting with ammonium chloride, primary amines are generated; or when reacting with primary or secondary amines, substituted amino acids are generated. When reacting with ketones, α,α-disubstituted amino acids are obtained.
Erlenmeyer synthesis is also called Erlenmeyer-Plöchl synthesis. It refers to the generation of dihydrooxazolone (azlactone) intermediates by α-amidoacetic acid in the presence of acetic acid or acetic anhydride, sodium acetate (or potassium carbonate). Since the methylene group on the intermediate oxazolone ring is affected by the adjacent carbonyl group, H has a certain acidity, and condenses with aldehyde under the action of alkali, and then reduces and hydrolyzes to obtain α-amino acids. For example, the synthesis of α-phenylalanine: First, glycine reacts with benzoyl chloride to generate benzoylglycine (commonly known as hippuric acid), and then benzoylglycine is cyclized under the action of acetic anhydride, and a water molecule is removed to generate oxazolone (or dihydrooxazolone). The methylene H on the heterocyclic ring has a certain acidity, and condenses with benzaldehyde under alkaline conditions, and then catalytic hydrogenation is carried out, and finally hydrolysis is carried out to obtain the target product α-phenylalanine.
In the presence of alkaline, phase transfer catalysts [such as triethylbenzylammonium chloride (TEBA)], Schiff bases generated by aldehydes and amines can undergo alkylation reactions with alkyl halides (such as RCl, RBr, etc.) to produce amino acids. This method can be used to synthesize alanine, phenylalanine, methionine, tryptophan, aspartic acid, leucine, orthovaline, valine, norleucine, etc. For example: R=H, R′=Bn, phenylalanine can be synthesized; R′=CH3, glycine can be synthesized.
With the application of gene editing technology and comprehensive synthetic biology, the production of amino acids by fermentation is becoming increasingly advantageous. Compared with chemical synthesis, fermentation has many advantages, including higher efficiency, lower production costs and environmental sustainability. At present, the main strains used for amino acid fermentation are Corynebacterium glutamicum, Brevibacterium flavum, Brevibacterium lactofermentum, Bacillus brevis, and Sesinobacterium marcescens. The key steps of amino acid fermentation include:
Amino acid modification involves functionalizing natural amino acids through chemical or enzymatic reactions to enhance their stability, bioactivity, or broaden their application scope. These modifications include derivatization reactions such as acetylation, methylation, and phosphorylation, which regulate amino acid metabolic behavior in organisms. Additionally, crosslinking reactions use bifunctional reagents to connect amino acids with polymers or proteins, enabling the design of drug delivery systems or biomaterials. For instance, PEGylation significantly improves the water solubility and circulation time of amino acid-based drugs, offering broader applications in biomedicine.
Amino acid labeling is a method of introducing specific tags into amino acids through chemical or biotechnological means, primarily including isotope labeling and fluorescent labeling. Isotope labeling uses radioactive isotopes (e.g., tritium, carbon-14) or stable isotopes (e.g., deuterium, carbon-13) to label amino acids, widely applied in metabolic tracing, protein dynamics research, and structural analysis. Labeling methods include chemical synthesis and fermentation labeling, with the latter producing high-purity amino acids by culturing microorganisms with labeled substrates. Fluorescent labeling introduces fluorophores into amino acid side chains, enabling real-time monitoring of protein dynamics, and is commonly used in cell imaging, protein-protein interaction studies, and drug screening.
Amino acid resolution techniques are used to separate racemic mixtures into D- and L-amino acids. Traditional methods include chemical resolution by forming separable diastereomeric salts with chiral reagents. Modern technologies rely on chiral chromatography and enzymatic resolution. For example, the resolution of L-lysine can utilize specific aminoacylases, offering high efficiency and selectivity.
Because of their special qualities and purposes, amino acids are not only the building blocks of proteins in living things but also essential components of many industrial uses. Aside from their biological roles, amino acids are utilized in biotechnology, medicines, cosmetics, food and beverage production, and agriculture. The fact that amino acids can be used as raw materials for chemical synthesis and bioprocessing further demonstrates their adaptability in industrial applications. Amino acids are building blocks of many other compounds, such as peptides, derivatives of amino acids, and amino alcohols. Amino acids can be fermented to produce high-value molecules including bioactive peptides, sweeteners, and taste compounds utilizing microorganisms or enzyme biocatalysts. These bio-based chemicals offer environmentally friendly alternatives to traditional petrochemical-derived products, contributing to sustainable industrial practices.
The food and beverage business is one area where amino acids are widely used in industry. A wide range of food products use amino acids as nutritional supplements, flavor enhancers, and food additives. For instance, the sodium salt of glutamic acid known as monosodium glutamate (MSG) is frequently employed as a flavor enhancer to improve the flavor of a variety of processed foods. In order to enhance the nutritional condition of cattle overall and encourage growth, amino acids like methionine and lysine are also given to animal feed. Moreover, sports nutrition supplements include amino acids like citrulline and arginine to improve muscle repair and athletic performance.
Amino acids are crucial building elements for a variety of medications and treatments in the pharmaceutical industry. Peptide medications, which are used to treat a wide range of illnesses and ailments, are made up of chains of amino acids. For instance, the peptide hormone insulin, which is made up of amino acids, is crucial for the control of diabetes. Moreover, amino acids are needed in the manufacture of medications used in chemotherapy, antivirals, and antibiotics. Amino acids are also added to medicinal formulations to increase stability, solubility, and bioavailability.
Because amino acids have skin-repairing, anti-aging, and moisturizing qualities, they are frequently found in cosmetics and personal hygiene products. Amino acids that support skin hydration and suppleness, like arginine, proline, and serine, are frequently used in skin care products. The synthesis of collagen, which is necessary for the firmness and suppleness of skin, is also aided by these amino acids. Amino acids are also used to strengthen and repair damaged hair strands in hair care products. A vital component of hair care products that supports hair health and growth is keratin, a protein abundant in amino acids.
Amino acids are utilized in agriculture as plant growth regulators and fertilizers to raise crop yields and quality. Amino acid fertilizers improve nutrient uptake and utilization by giving plants the nutrients they need in an easily absorbed form. Additionally, they promote the growth of roots, flowers, and fruits in a variety of crops. As natural chelators, amino acids like glutamine and glycine aid in the more effective uptake of micronutrients by plants, including iron, zinc, and copper. Furthermore, amino acids are added to animal feed additives to enhance nutritional digestion and support healthy animal growth.
Amino acids are used in a wide range of biotechnological activities, such as enzyme synthesis, protein engineering, and the creation of biofuels. The basic building blocks of genetic engineering methods, amino acids are utilized to alter and create recombinant proteins with particular characteristics and roles. Enzymes generated from amino acids are essential to several biocatalytic processes utilized in the bioremediation, medicine manufacturing, and biofuel generation industries. Bio-based polymers, biodegradable polymers, and other sustainable products are also made with amino acids.
