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The Secret of Active Enzymes: Why does biocatalysis play an important role in kinetic resolution?
In chemistry, active enzymes dominate many important biochemical reactions, which are often called enzyme-catalyzed reactions. The existence of these enzymes not only improves the efficiency of reactions, but also provides a wide variety of enzymes, making these chemical processes very critical in various fields. Especially in organic synthesis, biocatalytic technology has gradually replaced traditional chemical synthesis methods with its high selectivity and specificity.
Biocatalysis can be carried out under mild conditions, which makes chemical reactions more environmentally friendly and energy-saving.
Basic concepts of dynamic resolution
Kinetic resolution, especially using the effect of enzymes, means using the different reaction rates displayed by enzymes and catalysts in reactions to distinguish two enantiomers or enantiomers. Different reaction rates leave an excess of one isomer behind after the reaction, resulting in a more abundant product.
Biocatalytic technology to promote organic synthesis
Biocatalysis has become an important tool in organic synthesis, especially when it is necessary to prepare chiral molecules. This technology can be achieved through the following aspects:
- High selectivity: Biocatalysis targets specific substrates, is very effective and does not easily produce by-products.
- Environmental protection: Biocatalysis is usually carried out at normal temperature and pressure, which greatly reduces energy consumption.
- Diversity: There are many types of enzymes that can catalyze a variety of chemical reactions.
For chemists, being able to obtain high-purity, highly-selective products through biocatalysis is undoubtedly an innovation in chemical reactions.
Historical trajectory
Active enzymes have a long history of application. The earliest kinetic resolution came from Louis Pasteur. He discovered that when water-soluble mirror-image tartaric acid reacted with Penicillium, an asymmetric transformation occurred, ultimately leaving a large amount of L-tartaric acid behind.
Based on this, chemists began to explore the resolution mechanism under different reaction conditions. In 1899, Markwald and Mackenzie reported the kinetic resolution technology for the synthesis of chiral molecules. They successfully produced chiral esters selectively in esterification reactions, laying the foundation for more subsequent synthetic reactions.
Theoretical basis of kinetic resolution
The theory of kinetic resolution relies on different reaction rates and the energy transitions behind them. For mirror image isomers, there are differences in activation energies during the conversion process, which makes the reaction rates of the two different under the same conditions. Ideally, kinetic resolution can be efficiently performed if one isomer reacts much faster than the other.
Even in high-energy transition states, the energy difference between enantiomers is still a key factor affecting their reaction rates.
Future development direction
With the advancement of science and technology, the application of biocatalysis will become more and more widespread. From drug synthesis to environmentally friendly chemistry, biocatalysis will play a more important role in future organic synthesis.
For the chemical community, biocatalysis provides a new opportunity to explore more efficient and environmentally friendly synthesis methods. Where will chemical reactions go in the future? Will this completely change our understanding of chemistry?< /p>
