A Very Detailed Introduction for Biocatalysis

Biocatalysis refers to the process of chemical conversion using enzymes or biological organisms (cells, organelles, tissues, etc.) as a catalyst. This process is also called biotransformation.

Basic content definition

The organisms commonly used in biocatalysis are mainly microorganisms, and their essence is to catalyze the enzymes in the microbial cells to promote the process of biotransformation.

Advantages and disadvantages

Advantage

The action conditions are mild, and are basically completed in an environment such as normal temperature, neutrality, and water;

Unique and efficient substrate selectivity (because the enzymes in the catalytic process are specific, i.e. one enzyme can only catalyze the reaction of a specific substrate, but one substrate may be catalyzed by multiple enzymes);

The synthesis of chiral active pharmaceutical ingredients has unique advantages.

Disadvantage

Biocatalystsare often unstable in the reaction medium;
There are too few biocatalysts currently available for industrial applications;
The biocatalyst development cycle is longer.

Enzyme

Enzyme characteristics

Biocatalysts can catalyze a specific chemical reaction of a protein, RNA or a complex thereof, which can speed up the reaction by reducing the activation energy of the reaction, but does not change the equilibrium point of the reaction. The chemical nature of most enzymes is protein. It has the characteristics of high catalytic efficiency, strong specificity and mild action conditions.

The essence of enzyme catalysis: reducing the activation energy of chemical reactions;

High efficiency: the catalytic efficiency of the enzyme is higher than that of the inorganic catalyst, so that the reaction rate is faster;

Specificity: An enzyme can only catalyze one or a type of substrate, such as a protease that only catalyzes the hydrolysis of a protein into a polypeptide;

Diversity: There are many types of enzymes, about 4,000 kinds;

Mildness: means that the chemical reaction catalyzed by the enzyme is generally carried out under milder conditions;

Activity regulate: including inhibitor and activator regulation, feedback inhibition regulation, covalent modification regulation, and allosteric regulation;

Relevance: The catalytic properties of some enzymes are related to cofactors;

Variability; since most enzymes are proteins (a few are RNA), they are destroyed by high temperatures, strong acids, strong bases, and the like.

In general, the optimum temperature of the enzyme in the animal is between 35 and 40 ° C, and the optimum temperature of the enzyme in the plant is between 40 and 50 ° C; the optimum temperature of the enzyme in the bacteria and fungi is different, and the enzyme is obtained. The optimum temperature can be as high as 70 °C. The optimum pH of the enzymes in animals is mostly between 6.5 and 8.0, but there are exceptions. For example, the optimum pH of pepsin is 1.5, and the optimum pH of enzymes in plants is mostly between 4.5 and 6.5.

These properties of the enzyme enable the intricate metabolism of the cells to proceed in an orderly manner, allowing the metabolism of the substance to adapt to normal physiological functions. If an enzyme deficiency is caused by genetic defects, or the activity of the enzyme is weakened by other reasons, the reaction catalyzed by the enzyme may be abnormal, the metabolism of the substance may be disordered, and even the disease may be caused. Therefore, the relationship between enzymes and medicine is very close.

Digestive enzymes

Macromolecules such as protein, starch, and fat in food cannot be directly absorbed by the digestive tract. They must be digested and converted from macromolecular substances into easily absorbed small molecules to be absorbed by the digestive tract. The digestion of food is closely related to the enzymes in the digestive juice. Enzymes are a class of organic substances produced by living cells that have catalytic capabilities, also known as biocatalysts. Under certain conditions (such as suitable temperature, pH), digestive enzymes can break down complex macromolecular substances into simple small molecules.

Comparison

The same point: changing the chemical reaction rate, it is almost not consumed; it only catalyzes the existing chemical reaction; accelerates the chemical reaction rate, shortens the equilibrium time, but does not change the equilibrium point; reduces the activation energy, accelerates the chemical reaction rate; Poisoning.

The difference: inorganic catalysts are generally much longer than enzymes and are not easily poisoned. The stability of the enzyme is not as good as that of the inorganic catalyst, and the cost is much higher. But enzymes have terrible efficiency. Generally, the enzyme can be catalyzed at a rate of more than one million times that of the inorganic catalyst. Therefore, enzymes are generally used in high-tech fields such as medical pharmacy, relying on the demand for quality products.

Enzyme classification

According to the nature of the reaction catalyzed by the enzyme, the enzymes are divided into six categories:

Oxidoreductase promotes oxidation or reduction of the substrate.

Transferases promote the exchange or transfer of certain chemical groups between molecules of different substances.

Hydrolases promote hydrolysis.

Lyases catalyze the addition of a group or a de-grouping reaction from a double bond of a substrate molecule, i.e., promote the splitting of one compound into two compounds, or the synthesis of a compound from two compounds.

Isomerases promote the mutual conversion of isomers, that is, catalyze the rearrangement reaction inside the substrate molecules.

The ligase promotes the binding of two molecules to each other, while the high-energy phosphate bond in the ATP molecule (or other nucleoside triphosphate) cleaves, that is, catalyzes the intermolecular association reaction.

According to the principle of uniform classification of enzymes published by the International Biochemical Association, on the basis of the above six categories, in each of the major types of enzymes, according to the characteristics of the groups or bonds acting on the substrate, it is divided into several sub-categories; Precisely indicating the nature of the substrate or reactant, each subclass is subdivided into several groups (sub-subclasses); each group contains several enzymes directly.

Enzyme production

The enzyme can be produced synthetically or biologically. The cost of synthetic enzymes is significantly reduced, but the types of enzymes that can be artificially synthesized are very limited. Only organisms with biological activity can produce enzymes, but enzymes can work outside the body. Enzyme acquisition is currently obtained by extracting cultured organisms.

Catalyst poisoning

The case where the catalyst is degraded or even ineffective due to contamination or contact with an inaccessible substance during the reaction is called catalyst poisoning. The poisoned catalyst can no longer function.

Bio-catalyst

Summary

Biocatalyst technology is an integral part of chemical biotechnology and is increasingly important as a means or tool for chemical synthesis. Consumer demand for new products The industry is demanding higher revenues and lower costs. The government and the administration have promoted the application of biocatalysts by strengthening management pressures and the emergence of new technologies and scientific inventions. (Analysis of the real purpose of mainstream funds, find the best profit opportunities!)

Despite the production of high fructose corn syrup, sweetener production, and anticancer drugs, biocatalysts have yet to show their potential, and work is urgently needed by industry, non-profit organizations, government agencies, and academic institutions and national laboratories. Some of the goals set out in the plan are to exploit its potential to analyze technical barriers and issues that need to be addressed. At the same time, in order to implement this plan, the report also put forward implementation recommendations.

Objective: The biocatalyst planning goal includes reducing the consumption of materials, water and energy and pollution sources to 30% over the next 20 years. For biocatalysts, the following specific targets are: to develop biocatalysts that are better, faster and cheaper than existing chemical catalysts; to develop a series of biocatalysts that can catalyze in a wider range of reactions, as much as possible Increased versatility; improved temperature stability, reactivity and solvent compatibility; development of molecular modeling work, rapid design of new enzymes from scratch; creation of better tools or tools for biocatalyst development; Conduct social interest education in the utilization and creation of biocatalysts.

Technical obstacles to be overcome:

Little knowledge of enzymes and biocatalyst mechanisms; little knowledge of secondary metabolic pathways (including pathway interactions); few methods for organisms to engineer; many enzymes are expensive to produce and biocatalyst applications.

Implementation approach: Raise awareness of the value and effectiveness of research and development of new and efficient biocatalysts; develop research performance indicators that have achieved results; establish an executive preparatory committee to monitor and promote the development and use of biocatalysts; distribute guidelines to appropriate trade Organizational and professional societies; raising awareness of the value of biocatalysts that bring commercial benefits to industry leaders and certain local institutions; and scientists and funding agencies through basic research to promote understanding of the opportunities and challenges of biocatalyst development.

Through more than 50 expert studies, it is agreed that the continuous promotion of biocatalyst development is an important goal of the chemical-related industry. It requires extensive and coordinated work to understand the creation of a new generation of environmentally friendly and profitable biocatalysts. Opportunities and challenges. Consumers, industrialists, environmental workers and scientists should pay attention to this.

Chemical industry profile

The chemical industry is both a diversified and very complex industry. The entire chemical industry mainly includes industrial sectors, academic institutions and various national and local laboratories. These three components all carry out basic research, applied research and development to varying degrees. Different companies, organizations and institutions work differently according to their different ideas and purposes. The industrial sector conducts more research and development, while the academic sector focuses on basic research. Sometimes the industrial sector can conduct its own basic research. And universities and government laboratories often carry out competitive research and development or explore industrial applications.

Environmental issues are of the utmost importance in the chemical industry. Reducing environmental pollution is a matter of great concern to everyone. Therefore, we must develop a new "green chemistry" to make chemistry friendly to the environment, reduce waste generation, reduce energy use, and use renewable resources. Therefore, the main goal of chemical industry research is to develop processes and products that reduce waste, CO2 emissions and energy use. The chemical industry and its enterprises must consider sustainable fossil-based or biological regeneration resources.

Chemical biotechnology is the rapid application of biotechnology to chemical production. It is closely related to green chemistry and uses renewable raw materials. Bio-technical applications can afford new products, new manufacturing methods, and improved production economics, reducing energy consumption and reducing environmental impact.

New source

Biocatalysts traditionally rely on culture screening methods that actually lose most of the microbial resources. Scientists have developed a new approach because most of the microbes in the community cannot be cultured. This method can develop the genome of these microorganisms for biotechnology without pre-cultivation. This exciting field of research is called metagenomics. The metagenomic genome refers to the sum of all biological genetic material in a specific environment and determines the life phenomenon of the biological group.

There are two strategies for screening new biocatalysts or genes from libraries constructed from metagenomic DNA: activity-based screening and sequence-based screening. Either way, you must first construct a DNA library with a suitable vector and host. To construct a small fragment (<10kb) library, you can use a conventional cloning vector, but this library is difficult to detect large gene clusters and operons. With restrictions, researchers began to build large fragment gene libraries. Commonly used vectors are cosmids (allowing inserts of 25 to 35 kb in length) and BAC (about 200 kb). E. coli is still the most commonly used host strain.

Activity-based screening begins by identifying clones that express the desired characteristics and then characterizing these clones by sequence and biochemical analysis, which can quickly find proteins and natural products that can be used in industry, agriculture, and medicine. Another approach based on sequence screening is to sequence metagenomic clones, whether it is all or random sequencing is an effective means of discovering new genes.

Activity-based screening begins by identifying clones that express the desired characteristics and then characterizing these clones by sequence and biochemical analysis, which can quickly find proteins and natural products that can be used in industry, agriculture, and medicine. Another approach based on sequence screening is to sequence metagenomic clones, whether it is all or random sequencing is an effective means of discovering new genes.

The two screening methods have their own advantages and disadvantages, complement each other, and the two can be combined to obtain the maximum harvest from the natural molecular library.

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