Biocatalytic technology is a technology that utilizes enzymes or microbial cells or plant and animal cells as biocatalysts to catalyze reactions. Enzymes as biocatalysts have many advantages over chemical catalysts: enzyme-catalyzed reactions are generally carried out at room temperature, under normal pressure, and under near-neutral conditions, so there is less investment, less energy consumption, and high operational safety; biocatalysts have extremely high catalytic efficiency and reaction speed, which can be 107 to 1013 times higher than that of chemical-catalyzed reactions.
Definition
Broadly speaking, it refers to all kinds of activities produced by organisms for their own metabolism and maintenance of their biology.
Industrial biocatalyst is a general term for free or immobilized enzymes or living cells. It includes free enzymes extracted from living organisms, mainly microbial cells or processed by immobilization technology, collectively referred to above; it also includes free, overall microbial-based living cells and immobilized living cells, collectively referred to. The process in which an enzyme catalyst is used to catalyze a particular type of reaction or a particular type of reactant (often referred to as substrate or matrix in enzyme reactions) is referred to as; and the process in which a whole microorganism is used in a series of cascade reactions is referred to as. Dead cells or stem cell preparations also have a catalytic effect, but their cells are no longer metabolically capable, often unable to regenerate coenzymes or cofactors (components of enzymes), and can only carry out simple enzyme reactions, which is an impure enzyme catalyst.

Advantages
Catalysts can be categorized into biocatalysts and with non-biological catalysts.
Compared with non-biological catalysts, biocatalysts have great advantages, can be reacted at room temperature and pressure, fast reaction rate, catalytic effect of specialization, lower price and other advantages, but the disadvantage is susceptible to inactivation by heat, destruction by certain chemicals and heterogeneous bacteria, poor stability, and higher requirements for temperature and pH range during the reaction. Used as an immobilized enzyme or immobilized cells, the service life should generally be not less than 30 batches or 3 months of continuous use, otherwise it is difficult to pass the economic.

Enzymes are biocatalysts

Living organisms use them to accelerate chemical reactions in the body. Without enzymes, many chemical reactions in living organisms would proceed so slowly that it would be difficult to sustain life. Enzymes work best at a temperature of about 37°C (the temperature of the human body). If the temperature is higher than 50°C or 60°C, the enzyme is destroyed and can no longer function. Therefore, biological detergents that use enzymes to break down stains on clothing are most effective when used at low temperatures.
Enzymes are proteins or RNAs produced by living cells that have a high degree of specificity and catalytic efficacy for their substrates.The catalytic effect of enzymes depends on the integrity of the primary and spatial structure of the enzyme molecule. If the enzyme molecule is denatured or subunit depolymerization can lead to the loss of enzyme activity. Enzymes are biomolecules with a molecular mass of at least 10,000 and up to a million.
Enzymes are an extremely important class of biocatalysts. Thanks to enzymes, chemical reactions in living organisms can be carried out efficiently and specifically under very mild conditions.

With the in-depth study and development of the structure and function of enzyme molecules and the kinetics of enzymatic reactions, the discipline of enzymology has been gradually formed.

The chemical nature of enzyme is protein (protein) or RNA (Ribonucleic Acid), so it also has a primary, secondary, tertiary, and even quaternary structure. According to the difference of its molecular composition, it can be divided into simple enzyme and bound enzyme. Those containing only proteins are called simple enzymes; conjugated enzymes consist of enzyme proteins and cofactors. For example, most hydrolases are composed of proteins alone; flavin mononucleotidase is composed of enzyme proteins and cofactors. In conjugated enzymes, the enzyme protein is the protein portion and the cofactor is the non-protein portion, and only when the two are combined to form the whole enzyme does it have catalytic activity.
Enzymes have significant characteristics different from general catalysts: they are highly specific to the substrate and have high catalytic efficiency. Enzymes are adjustable and unstable.

Functions

Catalytic Role
Enzymes are a class of biological catalysts that govern many catalytic processes such as metabolism, nutrition and energy conversion in organisms, and most of the reactions closely related to life processes are enzyme-catalyzed reactions.
These properties of enzymes enable the intricate processes of material metabolism within the cell to proceed in an orderly manner, so that material metabolism and normal physiological functions are adapted to each other. If an enzyme is defective due to genetic defects, or the activity of the enzyme is weakened due to other reasons, it can lead to abnormal reactions catalyzed by the enzyme, resulting in material metabolism disorders, and even diseases, therefore, enzymes have a very close relationship with medicine.

Enzymes enable the body to digest and absorb the food we eat, and maintain all the functions of internal organs, including: cell repair, anti-inflammatory detoxification, metabolism, improve immunity, generate energy, and promote blood circulation. Such as rice in the mouth when chewing, the longer the chewing time, the more pronounced sweetness, is due to the starch in the rice in the oral secretion of salivary amylase, hydrolyzed into maltose. Therefore, eating more chewing can make food and saliva fully mixed, conducive to digestion. In addition, the human body has pepsin, trypsin and other hydrolyzing enzymes. The human body from the food intake of protein, must be in the role of pepsin, hydrolyzed into amino acids, and then in the role of other enzymes, select the human body needs more than 20 kinds of amino acids, according to a certain order to re-integrate into the human body needs a variety of proteins.

Catalytic mechanism
The catalytic mechanism of enzyme is basically the same as that of general chemical catalysts, which also combines with reactant (substrate of enzyme) to form a complex first, and improves the speed of chemical reaction by lowering the activation energy of the reaction. Under constant temperature, the energy contained in each reactant molecule of a chemical reaction system is lower in the average value although it differs a lot, which is the initial state of the reaction.
The reaction S (substrate) → P (product) is possible because a significant portion of the S molecules have been activated to become activated (transition state) molecules, and the more activated molecules there are, the faster the reaction rate. The activation energy of a chemical reaction at a given temperature is the amount of energy (in kilocalories) required to make all of the molecules in 1 mole of a substance into activated molecules.
The enzyme (E) acts by temporarily combining with S to form a new compound, ES, which is in a much lower activated state (transition state) than the activated molecules of the reactants in that chemical reaction without a catalyst contain. the ES then reacts to produce P, and at the same time releases E. E can combine with another molecule of S to repeat the cycle again. Reducing the activation energy required for the entire reaction allows more molecules to react per unit of time, and the rate of reaction can be accelerated. If, in the absence of a catalyst, the reaction of hydrogen peroxide decomposition to water and oxygen (2H2O2 → 2H2O + O2) requires an activation energy of 18 kcal per mole (1 kcal = 4.187 joules), catalysis of the reaction by catalase requires an activation energy of only 2 kcal per mole, a rate of reaction that increases by a factor of approximately 1011.

Enzyme (E) and substrate (S) form an enzyme-substrate complex (ES)

Directed binding of the active center of the enzyme to the substrate to generate the ES complex is the first step in enzyme catalysis. The energy for directed binding comes from a variety of non-covalent bonds, such as ionic, hydrogen, and hydrophobic bonds, and also van der Waals forces, formed during the interaction of the functional group of the enzyme active center with the substrate. The energy generated when they bind is called binding energy. It is easy to understand that each enzyme is selective in binding to its own substrate.
If the enzyme is only complementary to the substrate to generate an ES complex, and cannot further drive the substrate into the transition state, then enzyme catalysis cannot occur. This is because the formation of the ES complex with the substrate requires the formation of more non-covalent bonds between the enzyme and the substrate molecules to produce a complex that is complementary to the transition state of the enzyme and the substrate in order to complete the catalytic effect of the enzyme. In fact, the substrate molecules are transformed from the original ground state to the transition state during the process of generating more non-covalent bonds as described above. That is, the substrate molecule becomes an activated molecule, providing the conditions for the combination and arrangement of groups, the generation of instantaneous unstable charges, and other transformations necessary for the substrate molecule to carry out the chemical reaction. So the transition state is not a stable chemical substance, unlike the intermediate products of a reaction process. As far as the transition state of a molecule is concerned, it has an equal probability of transforming into a product (P) or into a substrate (S).
When an enzyme generates an ES complex with a substrate and further forms a transition state, the process has released more binding energy, which is now known to offset some of the activation energy required for the activation of the reactant molecules, thus making molecules that were previously below the threshold of the activation energy activated, and thus accelerating the rate of the chemical reaction.
Enzymes and catalysts in general speed up chemical reactions by the mechanism of lowering the activation energy of the reaction.
The catalytic specificity of an enzyme is manifested in both its selectivity for substrates and the specificity of the reaction it catalyzes. The majority of chemical reactions in the body are catalyzed by a specific enzyme, except for individual spontaneous reactions, and an enzyme can find its own substrate from thousands of reactants, which is the specificity of the enzyme. According to the difference in the degree of catalytic specificity of an enzyme, it is divided into three categories: absolute specificity, relative specificity and stereospecificity. An enzyme catalyzes the reaction of only one substrate called absolute specificity, such as urease can only hydrolyze urea to decompose into carbon dioxide and ammonia; if an enzyme can catalyze the reaction of a class of compounds or a class of chemical bonds is called relative specificity, such as esterases can catalyze the hydrolysis of triglycerides, but also hydrolyze other ester bonds. Enzymes with stereoisomeric specificity have strict requirements for the stereo configuration of the substrate molecule, e.g., L-lactate dehydrogenase catalyzes the dehydrogenation of L-lactate only and has no effect on D-lactate.
The catalytic activity of some enzymes can be affected by many factors, such as the regulation of allozymes by alloys, the regulation of some enzymes by covalent modifications, the regulation of enzyme activity by hormones and neurohumoral fluids through second messengers, and the regulation of intracellular enzyme content (which alters the rate of enzyme synthesis and catabolism) by inducing agents or blocking agents.
It should be noted that the catalytic reaction of an enzyme is often a combination of multiple catalytic mechanisms, which is an important reason for the high efficiency of enzyme-promoted reactions.
Applications
Disease Diagnosis
With the in-depth study of enzymes and more and more understanding, complex enzymes enriched with highly concentrated SOD play an increasingly significant role in the regulation of diseases. Normal human body enzyme activity is more stable, when some organs and tissues of the body are damaged or disease occurs, some enzymes are released into the blood, urine or body fluids. Such as acute pancreatitis, serum and urine amylase activity significantly higher; hepatitis and other causes of liver damage, hepatocyte necrosis or permeability enhancement, a large number of transaminases released into the blood, so that the serum transaminases rise; myocardial infarction, serum lactate dehydrogenase and phosphocreatine kinase significantly higher. When organophosphorus pesticide poisoning, cholinesterase activity is inhibited, serum cholinesterase activity decreased; certain hepatobiliary diseases, especially biliary obstruction, serum r-glutamyltransferase increased and so on. Therefore, with the help of blood, urine or body fluid enzyme activity measurement, can understand or determine the occurrence and development of certain diseases.
Clinical treatment
Enzyme therapy has been gradually recognized, a variety of enzyme preparations in the clinical application of more and more common. For example, trypsin and chymotrypsin can catalyze the decomposition of proteins, and this principle has been used in surgical dilatation, purification of septic wounds and treatment of thoracic and abdominal plasma membrane adhesions. In the treatment of thrombophlebitis, myocardial infarction, pulmonary infarction and diffuse intravascular coagulation, fibrinolytic enzyme, streptokinase, urokinase, etc. can be applied to dissolve blood clots and prevent the formation of thrombus.
Some compound natural enzymes, with high units of SOD enzymes as the main formula, can be used not only in the adjuvant treatment of important organs such as brain, heart, liver, kidney, etc., but also in the use of tumors with remarkable results. In addition, the principle of competitive inhibition of enzymes is also used to synthesize some chemical drugs for the treatment of antibacterial, bactericidal and anti-tumor. Such as enzyme spleen tonic and kidney tonic in infertility and other problems, also have a better regulation. And sulfonamides and many antimicrobials can inhibit the enzymes necessary for the growth of certain bacteria, so they have antibacterial and bactericidal effects; many antitumor drugs can inhibit enzymes related to nucleic acid or protein synthesis in the cell, thus inhibiting the differentiation and proliferation of tumor cells to fight against the growth of tumors; thioredoxin can inhibit iodine enzyme, thus affecting the synthesis of thyroxine, and thus it can be used to treat hyperthyroidism and so on.
Update! 2024 The 2nd Advanced Enzyme Engineering and Enzyme Technology Application Conference/October 18-20
Production Life
The yeast used in brewing industry is produced by the relevant microorganisms, and the enzyme will convert starch etc. into alcohol through the process of hydrolysis, oxidation, etc.; the production of soy sauce and vinegar is also completed under the action of enzyme; the nutritional value of feeds treated with amylase and cellulase is improved; the addition of enzyme to the laundry detergent can improve the efficiency of the detergent, and make the original not easy to remove sweat stains, etc., easy to remove. removed, etc. ……
Due to the wide application of enzymes, the extraction and synthesis of enzymes has become an important research topic. At this time, enzymes can be extracted from living organisms, such as pineapple skin can be extracted from pineapple protease. However, since the content of enzymes in living organisms is very low, a large number of enzymes in industry are produced by fermentation of microorganisms. It is generally necessary to select and breed the required strains of bacteria under suitable conditions and allow them to multiply to obtain large quantities of enzyme preparations. In addition, the synthetic synthesis of enzymes is being studied. All in all, with the improvement of scientific level, the application of enzymes will have a very broad prospect.
Main effects
Relationship between enzymes and certain diseases
Diseases caused by enzyme deficiencies are mostly congenital or hereditary, such as albinism due to tyrosine hydroxylase deficiency, serotonin or primaquine-sensitive patients due to 6-phosphoglucose dehydrogenase deficiency. Many toxic diseases are almost always caused by the inhibition of certain enzymes. For example, when commonly used organophosphorus pesticides (e.g., trichlorfon, dichlorvos, 1059, and Rogaine) are poisoned, the enzymes are inactivated because they bind to an -OH on the serine, an essential group in the active center of cholinesterase. Cholinesterase can catalyze the hydrolysis of acetylcholine into choline and acetic acid. When cholinesterase is inhibited and deactivated, the hydrolysis of acetylcholine is inhibited, resulting in the accumulation of acetylcholine and a series of poisoning symptoms, such as muscular tremor, pupil narrowing, excessive sweating, and slow heartbeat. Certain metal ions cause poisoning in human body, because metal ions (such as Hg2+) can combine with the necessary groups of the active center of certain enzymes (such as -SH of cysteine) and make the enzymes inactive.

Contact Us Now!

If you need Price, please fill in your contact information in the form below, we will usually contact you within 24 hours. You could also email me info@longchangchemical.com during working hours ( 8:30 am to 6:00 pm UTC+8 Mon.~Sat. ) or use the website live chat to get prompt reply.

Compound Glucoamylase	9032-08-0
Pullulanase	9075-68-7
Xylanase	37278-89-0
Cellulase	9012-54-8
Naringinase	9068-31-9
β-Amylase	9000-91-3
Glucose oxidase	9001-37-0
alpha-Amylase	9000-90-2
Pectinase	9032-75-1
Peroxidase	9003-99-0
Lipase	9001-62-1
Catalase	9001-05-2
TANNASE	9025-71-2
Elastase	39445-21-1
Urease	9002-13-5
DEXTRANASE	9025-70-1
L-Lactic dehydrogenase	9001-60-9
Dehydrogenase malate	9001-64-3
Cholesterol oxidase	9028-76-6