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Enzymatic activity of bacteria. The variety of enzymes from inorganic catalysts. Ferments of bacteria. enzymatic activity

Understanding fermentation

Enzymes (enzymes) I call it the rosette or tied with the membranes of the bricks, over the catalytic activity. (Крім білків catalytic activity organisms can show actions of RNA (ribozymes) and antibodies (abzymes), however, the stench in a thousand times less effective, less ferment.) Smell stench about persh_ dzherelakh enzymes. Biohimii, yaka vivchak ferments, be called enzymology... On the diagrams and in the reaction, enzyme molecules mean - E... Recovini, the re-enactment of which catalyze ferments, is called substrates (S). products enzyme reactions mean - R... In addition, ferments can be obtained in bottles, which can be obtained in a homogeneous view in the same ways, as well as інші bottles. For enzymes, they are characterized by physical and chemical power, power to the little ones.

Specification of enzymes from inorganic catalysts:

a) accelerate the reaction in a meaningfully effective way;

b) over a high specificity of the work;

c) there is a regulation in physiological minds;

d) dіyut in soft minds.

budova ferments

Enzymes can be used as simple or folded (kon'yugovany) bottles, before the warehouse of which can include lipid, carbohydrates, metals, nitrogenous bases, old vitamins. In organism, enzymes can function as a function in the development of a cell, as well as in the presence of non-essential complexes, or it enters the storehouse of biological membranes.

Due to the specificity of enzymes active center. Active center - a very unique combination of proximity in the space of amino acid surplus, which will prevent:

a) recognition of the molecule to the substrate,

b) linking the substrate with the enzyme,

c) the catalytic conversion (in the case of a folding enzyme in the act of catalysis, it also takes care of the fate of the coenzyme, which enters the active center before the warehouse).

The active center is winnowed at the moment when the blocks turn off and accept its native (active) conformation. The structure of the active center can change during interaction with the substrate. Behind the figurative vislov of D. Koshland, the substrate goes to the active center, yak hand to the mittens.

One molecule of the enzyme, especially if it is stored in a decimal subunit, can be attached to more than one active center.

In the active center є dvі dilyanka. The first dilyanka is prompted for recognition and connection to the substrate. Vin is called a substratum-sounding dilyanka or an anchored maidan. Another dilyanka is called catalytic, its warehouse includes amino acid surpluses, which take part in the act of catalysis.

Enzymes are proteins that are strongly developed for molecular weight and folding. By applying the enzyme with a small molecule, ribonuclease, it can be stored in one subunit with a molecular weight of 13,700 Da. (Ribonuclease has an amino acid endurance. In 1969, ribonuclease was synthesized in B.Merrifild's laboratory in New York.) Bagato enzymes are stored in one sub-unit, for example, lactate dehydrogenase is two subtypes. Until the present hour, there are a number of multi-enzyme complexes, which are stored in dozens of different sub-units and decile types of coenzymes. For example, the pyruvate dehydrogenase complex is stored in 60 subunits of three types and five types of cofactors. The molecular weight of such a complex becomes 2.3 * 10 6 - 10 * 10 6 Da in the presence of dzherel to the enzyme. The enzyme molecule can be smaller than the substrate molecule. For example: molecules of enzymes amylase and ribonuclease are less, less molecules of substrates - starch and RNA.

The bilkov part of folding enzymes is catalytically inactive and is called apofenzyme... The connection of the apoenzyme with a non-alcoholic component is to be produced until the approval of a catalytically active enzyme (holoenzyme):

Bagato fermentations in their warehouses for metal, which may be viconuvati development functions:

a) take part in the involved substrate and the process of its catalytic transformation;

b) take the attached coenzyme to the enzyme molecule;

c) stabilize the tretin structure of the enzyme (for example, Ca 2+ in amylase);

d) vibrate with the substrate, fix the true substrate, for which enzyme.

A lot of coenzymes є obsolete vitamins, which is why the loss of speech exchange in case of vitamins deficiency is explained by a decrease in the activity of singing enzymes.

Deyaki ferments order with the active center to revenge allosteric (regulatory) center - dilyanka of bilkovo globules, posture to the active center, can sound the words, and regulate the enzymatic activity. The words of speech are called allosteric effectors (allosteric activators or ingibitors)... As a result of the linking of the effector to the allosteric center, a change in the structure of the bottle is observed, which leads to a change in the spacious growth of amino acid surpluses in the active center, as a result, to a change in the enzymatic activity.

Enzymes that are produced in one organism and catalyze the same chemical reaction, albeit with a different primary structure of the protein, are called isoenzymes. Ferments are developed one kind one after such physical and chemical authorities, Yak molecular weight, thermostability, Substrate specificity, electrophoretic looseness. The nature of the appearance of isoenzymes is versatile, but more often for all it is overwhelmed by the ideas in the structures of genes, which code isoenzymes or subunits. For example, the enzyme lactate dehydrogenase (LDH), which catalyzes the reverse reaction of oxidized lactate to pyruvate, may be subunits of two types M and H, the combination of these subunits is the basis for the formation of five Lizoenzymes. For the diagnosis of heart disease and liver disease, it is necessary to monitor the LDH isozyme spectrum in the blood, LDH 1 and LDH 2 actives in the heart muscle and blood cells, and LDH 4 and LDH m 5 - as early as in the summer.

Fig. 1 Budova LDH isozymes.

Vimіryuvannya enzymatic activity

The value of the activity of enzymes in the process of going well in the way of increasing the speed of reaction catalyzes. The frequency of enzymatic reactions is varied by decreasing the concentration of the substrate or increasing the concentration of the product per hour:

v = -ΔC S / Δτ, v = ΔC P / Δτ,

de ΔC S- change of molar concentration to the substrate (mol / l),

ΔC P- change of molar concentration to the reaction product (mol / l),

Δτ - hour (xv, sec).

Kinetic dosage is necessary to carry out at a saturated concentration of the substrate, in the case of a drop, the enzyme is not able to show maximum activity.

Single enzyme activity:

International Single Enzyme (U)- the amount of enzyme, which catalyzes the conversion of 1 micromol to the substrate for 1 quiline at a temperature of 25 ° C and the optimal pH of the middle.

In the CI system, one enzyme є katav (kat) the same amount of enzyme, which catalyzes the transformation of one molar substrate in 1 second. It’s not important pidrahuvati, scho:

1 U = (1 * 10 -6 M) / 60 s = 1.67 * 10 -8 M s-1 = 1.67 * 10 -8 cat = 16.7 ncat.

often visit active activity the preparation in the enzyme increased the activity of the preparation of the enzyme, expressed in (U), on the basis of the preparation in milligrams:

A beats = U / mass to the drug (mg)

With purified enzymes in the pitoma, the activity increases. For the growth of pet activity, one can judge about the efficiency of the stages of purification and purity of the enzyme preparation.

For the assessment of the activity of highly purified, homogeneous preparations in enzymes, the number of international units (U) to the enzyme per unit amount per enzyme (μmol) per unit rate molar activity(number of wraps). per physical wizard molar activity - the whole number of molecules to the substrate, which is transferred to one molecule of the enzyme for 1 quill or for 1 second. For example: for urease, accelerating the hydrolysis of sechovina, the molar activity becomes 30,000, trypsin - 102, glucose oxidase - 17,000 cycles per second.

the power of enzymes

4.1. Mechanism of the arts. Enzymes can change rapidly to catalyze reactions in the batch of products, in such a rank, the constant of effective reaction becomes permanent. Yak and all catalysts, ferments will not change the hour of reaching the price of rivnovagy. In a large number of enzymes, they accelerate reactions in 10 7 - 10 14 times. The efficiency of enzymatic catalysis is based on a strong decrease in the energy of activation of the reaction for the transformation of the substrate into the product through the transition plates.

4.2. specificity of the event... The specificity of the reaction with the substrate and the way through the enzymatic reaction begins with the apofenzyme. The specificity of the enzyme in the form of the conjugation of the exchange of speech in the organism.

It seems about enzymes, what a stink vuzka substrate specificity, There is a stench on the other side of a small number of substrates. Inodi you can talk about absolutely substrate specificity, for example, catalase catalyzing only one reaction - dispensing with water peroxide:

Large enzymes are characterized by common (broad, group) Substrate specificity If the stench catalize a group of similar reactions. For example, alcohol dehydrogenase catalyzes the transformation of alcohols into aldehyde, and the substrates can be methanol, ethanol, propanol and other alcohols. This is the fact that alcohol dehydrogenase can oxidize non-linear alcohols, as well as an alcohol group, which can be included in the store of folding molecules, winter cream, and the enzyme can catalyze the transformation of retinol into retinal. Naturally, enzymes, over a wide substrate specificity, catalyze the transformation of substrates with a good efficiency.

Ferments of nadіlenі also stereochemical specificity: Їх active center develops molecules of substrates in a spacious configuration. For example, the oxidation of L-amino acids is active only as well as L-amino acids and absolutely does not exist on their D-analogues. For oxide deamination of D-amino acids in living organisms є oxidation of D-amino acids, but not on L-amino acids. The very fact that the active center is connected with the singular stereoisomers to the substrate lies in the basis of the function of such enzymes, such as racemazi, which transform one stereoisomer into one another.

Specificity of the nobles of re-development However, one substrate from other enzymes can be transformed into products, which is developed for the structure and role in metabolism.

Guided butt: L-amino acid oxidase a diet on L-amino acids, converting them into alpha-keto acids with the solution of ammonia and peroxide water.

L-amino acid decarboxylase It is connected with these substrates, rather than catalyzing the reaction: decarboxylation from the formulations of biogenic amines and the form of carbon dioxide.

With just one butt є the possibility of converting glucose-6 phosphate from one of the other enzymes, one at a time from the various metabolic paths:

4.3. thermolability .

Yak and richly strong, when the temperature of the enzyme is adjusted, thermal denaturation is given, so that the native conformation of the enzyme is destroyed and the structure of the active center changes. Ferments of ssavts are repaired with a little denatured at temperatures of 40 o C.

At the zyazyka z vyshekazanim, enzyme preparations are bazhano zberigati at low temperatures. One of the best ways to save enzymes is lyophilization (drying at temperatures lower than -70 ° C in vacuum), transferred to a partially denatured mill for additional salts of ammonia and placing in a refrigerator.

4.4. Precipitation of fluidity reactions in terms of temperature. The variability of enzymatic reactions, such as any chemical reactions, lie at a temperature. When the temperature is adjusted by 10 ° C, the speed of the reaction increases 2-4 times according to the Van't Hoff rule. However, at temperatures of 40 ° C, at the same stage of denaturation of enzymes, it is possible to produce to a decrease in the total activity (Fig. 2):

Small. 2. The presence of liquid enzymatic reactions in terms of temperature.

4.5. The severity of the fluidity of the reaction in terms of pH. The abundance of the liquid enzymatic reaction in the form of pH is bell-shaped (Fig. 3). The pH value, at which the most rapid enzymatic reaction occurs, is called optimal (pH-optimum). The nature of the curves and the value of the pH optimum is due to the nature of the charge of the groups to the substrate and the charge of the groups to the enzyme (especially quiet, as it enters the active center). The optimum pH for higher enzymes is between 6.0 and 8.0 (Fig. 3).

Small. 3. The presence of liquid enzymatic reactions in terms of pH.

However, the єth vinyatka, for example, pepsin is most active at pH 1.5 - 2.0, and puddle phosphatase at pH 10.0 - 10.5 (Fig. 4)

Small. 4. Deposits of liquid enzymatic reactions (v) as the pH of the middle.

With extreme (even lower or even higher) pH values, the deterioration of the tertiary structure of the molecule is caused by the enzyme, which leads to the loss of enzymatic activity.


Similar information.


Enzymes are a special kind of proteins, and nature has introduced the role of catalysts in various chemical processes.

The whole term is constantly on the ear, however, far from all the reason, but also an enzyme, but also an enzyme, such as the functions of a viconious speech, as well as what enzymes are derived from enzymes and are derived from an enzyme. All at once and knowledge.

Without these words, no people, no creatures, could not overpower the hedgehog. And for the first time, until the enzymes were consumed, people went in for 5 thousand rockets, if our ancestors came to take milk in the "dishes" of slimes of food. In such minds, the milk is transformed into a sire by pouring the ferment into the ferment. The first step is only one application of the robot to the enzyme in the capacity of the catalyst, which will accelerate the biological processes. Christmas ferments are indispensable in industry, the stench is important for the production of sugar, margarines, yoghurts, beer, food, textiles, alcohol and concrete. In the presence of powder and oral powders, there is also a presence of corny speech - they additionally help to vivodit by playing at low temperatures.

History of the message

Enzyme in walnut means "leaven". And the cries of the people of the goiters were told by the Dutch to Jan Baptist Van-Helmont, who is alive in the 16th century. In my own hour, I’m stuck to alcohol wanderings, and in the course of the journey, I’m aware of an unimaginable speech that will accelerate the process. The Dutchman called it fermentum, which in the cross-section means "brodinnya". Then, perhaps three centuries later, the Frenchman Louie Pasteur, also sparingly behind the fermenting processes, drove to visnovka, but fermentation is not so important, like the speech of a lively clitine. And after a decade, the nimets Edward Buchner added the enzyme to others, and thus the speech does not live by organism. Vin also gave it its name - "zymaza". Even through the decal, the rocky name of Ville Kuehne proponed all the library catalysts for two groups: ferments and enzymes. Moreover, the other term “wine” proponates the name “leaven”, which expands the posture of living organisms. In less than 1897, rіk passed the edge to all the scientific superstrips: insulting terms (enzyme and enzyme) are viralized as absolute synonyms.

Structure: lantsyug z thousand amino acids

All ferments are in bites, but not all bins are ferments. Yak and інші proteins, prices are stored z. І scho tsіkavo, on the stem of the skin enzyme from one hundred to a million amino acids, strung, nem pearls on a string. Ale tsya thread is not buvaє rіvnoy - zzvychay curled up in hundreds of times. In such a rank, the structure is trivial and unique for the skin enzyme. Mіzh tim, the enzyme molecule - is of course great knowledge, and if the part of its structure is not large, so the title is an active center, take part in biochemical reactions.

Amino acid dermal acid of the best type cheery sound And the dermal enzyme has its own unique effect of amino acids. For the establishment of a large number of them, approximately 20 types of aminosubstances are vikorized. To find insignificant changes in the after-life of amino acids can drastically reduce zovnishniy viglyad and "talent" to the enzyme.

biochemistry

I would like to see a great number of reactions for the participation of enzymes in nature, but all the stinks can be classified into 6 categories. Apparently, the skin is of six reactions against the injected type of enzymes.

Reactions for the participation of enzymes:

  1. Oxidation and renewal.

Enzymes, which take part in cich reactions, are called Oxidoreductase. Yak butt can be guessed yak, alcohol dehydrogenase can be reimagined first alcohol in aldehyde.

  1. Reaction of the transferred group.

The enzymes that are used for the reaction are called transferase. Smell the smarter change of functional groups from one molecule to the last. So it is considered, for example, if alanine aminotransferase replaces alpha-amino group with alanine and aspartate. Transferase also replaces phosphate groups and ATP in small portions, and disaccharides are removed from excess glucose.

  1. Hydroliz.

Hydrolases, as they take part in the reaction, take a single ring, add the elements of the drive.

  1. The connection is abo the view of the subway link.

Tsei kind of reactions with a non-hydrolytic way to see for the participation of liazi.

  1. Isomerization of functional groups.

In many chemical reactions, the position of the functional group changes in the boundaries of the molecule, but the molecule itself is folded from the same number and types of atoms, which will bring up the cob of reaction. In other words, the substrate is a reaction product and isomers. This type of transformation can be given by injecting enzymes into isomerase.

  1. Osvita single link from usunennyam element of water.

Hydrolase the ring by adding elements to the molecule. Lіazi zdіysnyuyut zvorotnuyu reaction, vіdalyayuyu part of the functional groups. In such a rank, there is a simple connection.

Yak work in organizmі

Ferments to spice up practically everything chemistry reactions, Scho are seen in the clitines. The stench may be of vital importance for people, to persecute and accelerate metabolism.

Deyak from the number of words add to the ruinuvati large molecules on more other "shmatki", as the body can digest. Inshi navpaki tie other molecules. Ale fermentation, which seems to be a scientific language, may seem to be very selective. Tse means that the skin from the chicks of the words will welcome only the singing reaction. Molecules, which “clean” the enzyme, are called substrates. Substrates, in their own accord, release a link with a part of the enzyme, which is called the active center.

There are two principles to explain the specifics of the interaction of enzymes and substrates. The so-called “key-lock” model has an active loan center in the substratum of a strictly singing configuration. As a matter of fact, up to the іnshoi model, offense to the participants of the reaction, the active center and the substrate, to change their form, to do it.

Due to the bi principle, the result of the same thing was not attributed to the interaction - the reaction to the infusion of the enzyme is opposed to a lot of developed shvidshe. As a result of such interaction, new molecules are "populated", which are then added to the enzyme. And the speech-catalyst prodovzhu to viconuvati its robot, even after the fate of those particles.

Hyper- and hypoactivity

There are drops, if they do not show their functions with the wrong intensity. The overwhelming activity of the reaction is overwhelming in the formation of the reaction product and the deficiency of the substrate. The result is the loss of self-respect and serious ailments. The cause of the enzyme hyperactivity can be genetically damaged, as well as an excess of vitamins or, vicarious in the reaction.

Hypoactivity of enzymes can be a cause of death, if, for example, enzymes do not lead to toxins in the body or ATP deficiency. The reason for this will also be the possibility of being muddled geni, or navpaki, hypovitaminosis and deficiency of other living words. In addition, the temperature is lowered in the same way as the control function of the enzymes.

Catalyst and not only

You can often see about the corny of enzymes. Is there any way to talk about what kind of praise of our body can be found?

Enzymes are biological molecules, the life cycle of which is not meant to be within the framework of nationality and death. The stench just pours in the body until quietly, as long as it is not razchinyatsya. As a rule, the price is given for the infusion of other enzymes.

In the process of biochemical reaction, the stench does not form part of the final product. If the reaction is complete, the enzyme is overflowing with the substrate. Writing a speech is ready to start again before the robot, even on the other molecules. And so trivial style, but a need for the body.

The uniqueness of enzymes is in the fact that the skin is only one of them, the function is introduced. The biological reaction is considered only todi, if the enzyme is known to be the correct substrate for a new substrate. The quality of interaction can be correlated with the principle of a robotic key and a lock - as soon as you select the right elements, you can "spratsuvatisya". Another special feature: the stench can smell at low temperatures and at a normal pH, and in the role of catalysts, it is more stable, not even if it is chemistry.

Ferments yak catalysts accelerate the processes of metabolism and reactions.

As a rule, the processes are composed of sine stages, dermal wrinkle vimag of robotic enzyme. Without it, the cycle of revision, or acceleration, cannot be completed.

Mabut, with all the functions of enzymes of the best type - the role of a catalyst. This means that we combine chemical reagents in such a way that it is necessary to reduce energy vitrati, which is necessary for a more efficient formulation of the product. Without these words, chemical reactions would occur hundreds of times more. But at all the building of the business is not enough. All living organisms take revenge on the energy that is necessary for the continuation of life. ATP, or ATP, the battery is charged in its own way, I will take care of the power of the cell. Ale function of ATP is uncomfortable without enzymes. The I head enzyme, which is virobly ATP, is synthase. For the cutaneous glucose molecule, which transforms into energy, viroble synthase is close to 32-34 ATP molecules.

In addition, enzymes (lipase, amylase, protease) are actively used in medicine. Zokrema, serve as a component of enzymatic preparations, such as "Festal", "Mezim", "Panzinorm", "Pancreatin", which can freeze for the treatment of non-etched slunk. Ale deyakі enzimі zdatnі also inject on the blood-carrying system (razchinyayut thrombi), to heal the healing of gnіyn wounds. I can also use antibiotic therapy until enzymes are added.

The factor that allows you to start the activity of your business

Oskіlki enzym zdatnіy prizryuvati reacciiії in a lot of developments, thіѕ activity іsnаtаrаt so called by the number of revolutions. The term means the number of molecules to the substrate (reagent), which can transform 1 molecule to the enzyme for 1 quill. However, there are a number of factors that lead to the quickness of the reaction:

  1. Concentration of the substrate.

Increase the concentration of the substrate before the accelerated reaction. More molecules of active speech, less more reaction, some more active centers. However, it can be accelerated only to quiet times, as long as not all molecules of the enzyme are involved. On the other hand, we will not bring an increase in the concentration of the substrate to an accelerated reaction.

  1. Temperature.

Change the temperature adjustment until the reaction is accelerated. The whole rule of thumb is for large enzymatic reactions, ale only until quiet, as long as the temperature is not 40 degrees over Celsius. Writing a common sign of quickness of reaction, navpaki, start a quick decrease. As the temperature drops below the critical level, the frequency of enzymatic reactions will increase again. As soon as the temperature is over, the covalent bonds are ruined, and the catalytic activity of the enzyme is consumed at all times.

  1. Acidity.

The pH indicator is also added to the speed of enzymatic reactions. For the skin enzyme, there is an optimal level of acidity, with any reaction, it should pass the most adequately. The change in the pH value is determined by the activity of the enzyme, and hence, the speed of the reaction. As the snakes are too big, the substrate consumes the energy of the active nucleus, and the enzyme cannot catalyze the reaction. By updating the required pH, the activity of the enzyme is also updated.

Ferments present in human body, Can be divided into 2 groups:

  • metabolic;
  • equal.

Metabolic "work" over the neutralization of toxic speech, as well as the release of energy and energy. Well, і, wickedly, to accelerate biological processes in organizmі.

For the sake of being able to tell the same - there is a sense of the name. And here is the basic principle of selectivity: the singing type of enzymes is added only to one type of food. That for polіpshennya etching can go into a little trick. As organism is badly over-poisoned with a product, it means that it is necessary to add a product to a product, to take revenge on an enzyme, which is important to over-poison it.

Harchovy ferments are catalysts, which can be used to develop food products until they reach the body, in which the body of the building can eat corny speech from them. Travіnі enzimі buvayut decіlkoh types. In human organisms, there are different types of enzymes to be found on the small plates of the herbal tract.

Rotova empty

At the end of the day, alpha-amylase is injected. I will break down in carbohydrates, starch and glucose, which can be found in potatoes, fruits, vegetables and other food products.

slunk

Here pepsin breaks down proteins to peptides, and gelatinases - gelatin and collagen, which can be found in meat.

Pidshlunkova zalosa

On the whole stage "pratsuyut":

  • trypsin - as a result of splitting of bilks;
  • alpha-chymotrypsin - additional help to assimilate proteins;
  • elastazi - split deyakі vidi bіlkіv;
  • nucleases - add to the breakdown of nucleic acids;
  • steapsin - to acquire fatty їzhі;
  • amilaza - prompted for the cultivation of starch;
  • lipase - dissolves fat (lipid), which can be found in dairy products, mountains, oils and meat.

Small intestine

Above the grub pieces "chuckle":

  • peptidazi - split peptides from half to the level of amino acids;
  • saccharase - additional help to develop folded candies and starch;
  • maltase - I break down disaccharides to become monosaccharides (malt zukor);
  • lactase - breaks down lactose (glucose, which can be found in dairy products);
  • lipase - the assimilation of triglycerides, fatty acids;
  • erepsin - pouring into proteins;
  • isomaltase - "pratsyu" with maltose and isomaltose.

Tovsta gut

Here are the functions of enzymes:

  • kishkova palichka - caused by over-etching of lactose;
  • lactobacilli - infused into lactose and carbohydrates.

For the names of the names, there are:

  • diastasis - over-etching starch;
  • invertase - I will break down sucrose (table zukor);
  • glucoamylase - converts starch into glucose;
  • alpha-galactosidase - digestion of beans, seeds, soy products, root vegetables and leaves;
  • bromelain - enzyme new species bіlkіv, effective in case of higher levels of acidity in the middle, volodya with anti-fiery power;
  • papain - an enzyme, visions from syroa papaya, the splitting of other and great proteins, effective in a wide range of substrates and acidity.
  • cellulase - splitting cellulose, roslinn_ fibers (in the human body is not revealed);
  • endoproteases - cleaves peptide links;
  • bichacho zhovchi extract - an enzyme of food activity, stimulates intestinal motility;
    • that іnshih minerals;
  • xylanase - I will break down glucose from cereals.

Catalysts in products

Ferments may be of great importance for health, some of them add to the organism of splitting food components up to the camp, which is attached to victorian living rhymes. The intestines and pidshlunkov zloza circulate a wide range of enzymes. Ale krym tsyogo, rich korishnyh speeches, scho to drink etching, to take revenge also in deyaky products.

Fermented products є a practically ideal gherel of cinnamon bacteria, necessary for proper pickling. And at that hour, if the pharmacy probiotics "work" only in the upper part of the herbal system and often do not reach the intestines, the effect of enzymatic products is seen in the entire intestinal tract.

For example, apricots can be found in a sum of brown enzymes, including invertase, which is responsible for the breakdown of glucose and a quick energy boost.

Avocado can serve as a natural lipazi dzherel (spriyє more richly digested lipids). In organizmі tsya speech is viroblyaє pіdshlunkova zalosa. If you want to linger on your life, you can indulge yourself, for example, with a salad with avocado - delicious and cinnamon.

In addition, banana, mabut, the most expensive dzherelo calyu, wine also supplies amylase and maltase to the body. Amilaza can also be found in khlib, kartopl, cereals. Maltase is a splitting of maltose, the so-called malt zucru, which is a great number of representations in beer and corn syrup.

The first exotic fruit is pineapple to take revenge in its own collection of enzymes, including bromelain. And win, it’s a good thing for those who are pretending, that they’re wiping and anti-fiery powers.

Extremophiles and promises

Extremophiles - the chain of speech, building up life in extreme minds.

Alive organisms, as well as enzymes, which allow them to function, are known in geysers, when the temperature is close to the boiling point, and in ice, and also in the minds of extreme salinity (Death Valley in the USA). Besides, at the same time, it was known that for some pH levels, as it happened, it is also not a principle for an effective robot. Prescribers with a special interest in vivchayut ferments-extremophiles, like speech, which can be widely used in industry. If you want to and for the current year, they already know their stasis in the industry as biologically and ecologically pure speech. Until the end of the business, they are involved in the food industry, cosmetology, and the widespread chemistry.

Moreover, the "services" of enzymes in such vapadas are cheaper than synthetic analogs. In addition, the natural words of the building are biologically ruinuvatisya, so that they are safe for ecology. In nature, there are microorganisms, the development of enzymes based on amino acids, which then become components of a new biological lance. Ale tse, so bi moviti, als zvsim іnsha history.

Enzyme activity. pid enzyme activity The reason is the same, as it catalyzes the transformation of the singing amount to the substrate in one hour. For varying the activity of enzyme preparations, there are two alternative units: international (MO) and catav (cat). per international unit of activity The enzyme accepted the same amount, which catalyzes the conversion of 1 μmol of the substrate into the product for 1 hour in standard sinks (depending on the optimal ones). one katav means a quantity of the enzyme that catalyzes the transformation of 1 mole to the substrate in 1 s (1 cat = 6 ∙ 10 7 MO). In the bimolecular reaction A + B = C + D, for one enzyme activity, take the same amount, which catalyzes the conversion of 1 μmol A and B, or 2 μmol A (where B = A), for 1 hour.

Often, enzyme preparations are characterized by their active activity, as they represent the steps of the purification of the enzyme. pitoma activity - the whole number of units of activity of the enzyme, which falls on 1 mg of a bottle.

molecular activity (Number of revolutions to the enzyme) - the number of molecules of the substrate, which must be reconstituted by one molecule of the enzyme for 1 hour when the enzyme is again saturated with the substrate. The number of units of activity of the enzyme, given to the amount of the enzyme, is increased in micromol. The understanding of molecular activity can be used only for pure enzymes.

If there is a number of active centers in the enzyme molecule, an understanding is introduced activity of the catalytic center ... Vaughn is characterized by the number of molecules to the substrate, which can be transformed in 1 xv per one active center.

The activity of enzymes is very high among the most important minds, in the middle of the first order of magnitude the temperature and pH of the middle. The temperature adjustment in the 0-50 ° C interval should be adjusted to a smooth increase in enzymatic activity, which is linked to the accelerated processes of the formation of the enzyme-substrate complex and all the onset of catalysis. When the temperature on the skin is 10 ° C, the speed of the reaction is approximately reduced (Van't Hoff's rule). However, farther away the temperature rise (> 50 ° C) will lead to an increase in the amount of inactivated enzyme for the denaturation of the protein part, which will rotate in decreased activity. The skin enzyme is characterized by temperature optimum- the values ​​of the temperature, at which the most active activity is restored.

The severity of the activity of enzymes in terms of the pH value of the middle is very foldable. For skin enzyme characteristics optimum pH middle ground, Whenever there is wine, it shows maximum activity. With a visible value in that direction, the enzymatic activity decreases. The price will be explained by the change in the active center of the enzyme (changes in the ionization of functional groups), as well as the third structure of all the protein molecules, which can be used as a basis for the reduction in these centers. A large number of enzymes may have an optimum pH in the region of neutral values. However, it is an enzyme that exhibits maximum activity at pH 1.5 (pepsin) or 9.5 (arginase). When robotic with enzymes, it is necessary to adjust the pH to an additional type of buffer.

The activity of enzymes is strong up to significant amounts in the fallow area. іngіbіtorіv(Rechovin, partly to reduce the activity) і activator(Rechovin, to increase the activity). Their role is to identify cationic metals, deyaki anioni, carriers of phosphate groups, intravalent equivalents, specific proteins, industrial and chemical products of metabolism and inn.

Principles of enzymatic kinetics. The essence of the kinetic dosages of polyanga is at the value of the maximum efficiency of the enzymatic reaction ( V max) і constants Mikhaelis Do M. Enzymatic kinetics of vivchaє shvidkostі kіlkіsnyh re-transformation of some words in іnshі before dієyu enzymes. The speed of the enzymatic reaction is reduced by the decrease in the substrate, or by the increase in the product for one hour, or by the change in the concentration of one of the sum forms of the coenzyme.

inflow concentration of the enzyme on the speed of the reaction, it turns in the offensive: if the concentration of the substrate is post-lay (for removing the surplus of the substrate), then the speed of the reaction is proportional to the concentration of the enzyme. For those who are kinetic, use the enzyme concentration of 10  8 M active centers. The optimal value of the concentration of the enzyme is based on the graph of the presence of the activity of the enzyme from the concentration. The optimal value is to lie on the plateau of the discarded graph in the area of ​​the enzyme activity, it is not enough to lie in this concentration (Fig. 4.3).

Small. 4.3. The presence of the liquid enzymatic reaction

from concentration to enzyme

For vivchennya vpwu concentration of the substrate the frequency of the enzymatic reaction will be a kinetic curve, which shows a change in the concentration of the substrate (S 1) or the product (P 1) in the hour (Fig. 4.4) and increase the cob fluidity ( V 1) the reaction yak tangent kuta nahil to the point of being crooked at zero point.

Small. 4.4. Kinetic curves of enzymatic reactions

Having stayed kinetic curves for the highest values ​​of the concentration given to the substrate (S2, S 3, S 4, etc.) For the product (P 2, P 3, P 4, etc.) V 2, V 3 , V 4 and D.) Reactions, there will be a graph of fallowness of cob and liquid enzyme reactions due to the concentration of the substrate (with a constant concentration of the enzyme), such a small amount of hyperbole (Fig. 4.5).

Small. 4.5. Degree of corn cob fermentation reaction

from the concentration of the substrate

The kinetics of bagatoch enzymatic reactions is described by the words of Michaelis  Menten. With a constant concentration of the enzyme i low values ​​of the concentration of the substrate[S] pochatkova speed of reaction is directly proportional to [S] (Fig. 4.5). In general it is worth talking about the substratum for the enzyme, if half of the molecules of the enzyme are in the form of the enzyme-substrate complex and the speed of the reaction V = 1/2V max. According to the substrate, the reactions are of the 1st order (the speed of the reaction is directly proportional to the concentration of one reactant speech) or the 2nd order (the speed of the reaction is proportional to the addition of the concentration of the two reactants).

at high values concentration of the substrate[S] The speed of the reaction may not be stagnant at [S]: with a further increase [S], the speed of the reaction grows more and more, and as a result, it becomes permanent (maximum) (Fig. 4.5). When all the enzyme molecules are present in the form of an enzyme-substrate complex and V = V max. To the extent of the substrate, the reaction is of the 0th order (the speed of the reaction does not lie in the concentration of reactive speech).

In 1913, L. Mikhaelis and M. Menten propounded a simple model that would explain this kind of kinetics. According to the model, the establishment of a specific enzyme-substrate complex is a necessary intermediate stage of catalysis.

k 1 k 3

E + S ⇄ ES → E + P

Enzyme E is bound with the substrate S, forming the ES-complex. The constant speed of the process k 1. The share of the ES-complex is stored in two ways: vin can either dissociate into the enzyme E and the substrate S with the constant k 2, for a substitute reinterpretation, setting the product P і vіlny enzyme E, with a constant shvidkostі k 3. At the same time it is postulated that the product of the reaction does not overturn in the substrate. Tsia Umova will see to the cob stage of the reaction, while the concentration of the product is low.

The speed of the catalysis starts in stationary minds If the concentration of industrial products is used gradually, so as the concentration of industrial speech and end products changes. It’s not a big deal, if the speed of the ES-complex has been approved for the first time.

You can introduce a new constant K M - Michaelis constant(Mol / l), yaka dorіvnyu

Rivnyannya Mikhaelisa - Menten, Which turns to a large extent to the reduction of the enzymatic reaction and concentration of the substrate,

(4.2)

The process of determining the graph of the deposition rate of the fluidity of the reaction to the concentration of the substrate. at low substrate concentrations, If [S] is nabagato nizche K M, V = V max [S] / K M, that is, the speed of the reaction is directly proportional to the concentration of the substrate. at high concentrations of the substrate, If [S] nabagato vishche Do M, V = V max, that is, the reaction rate is maximum and does not lie in the concentration of the substrate.

Yaksho [S] = K M, then V = V max / 2.

In this rank, K M suitable for the concentration of the substrate, with a liquidity of the reaction of the warehouse, half of the maximum.

Michaelis constant (K M) and the maximum reaction rate ( V max) - important characteristics of fluidity at low concentrations of the substrate. V max is the value of the post-term for the skin enzyme, allowing the assessment of the effectiveness of the yogo performance.

The Michaelis constant shows the spore rate of the substrate to the enzyme (in times, if k 2 >> k 3): less than KM, more spore and quickness of reaction, and navpaki. Skin substrate is characterized by its own K M value for a given enzyme, and for these values ​​one can judge about the substrate specificity of the enzyme. Constant Michaelis is due to the nature of the substrate, temperature, pH, ionic strength and manifestation of ingibitoriv.

At the connection z tim, what is the value V max і К М without a middle graphical deposit of Michaelis - Menten (Fig. 4.5) є ambiguous, it goes up to the linearization of this ryvennya. For many people to transform into such a form, graphically, it is straight. There are many methods of linearization, the middle of the most often use the methods of Lineuver - Burke and Edi - Hofsti.

redefining Lainewera - Burka ma viglyad

(4.3)

There will be a graph of deposits 1 / V = f(1 / [S]) і take a straight line, the overflow between the ordinates yields the value 1 / V max; the tangent of the kuta goes straight to the abscis axis to the value -1 / K M / V max (fig. 4.6). Tsey graph allows you to make a big deal V max. As well as lower, the graph can also be used to display valuable information, as well as to control the activity of the enzyme.

Small. 4.6. The method of linearization of the rivnyannya Mikhaelis - Menten

(According to Lineuver - Burke)

method Edі - Hofsti of recordings on the re-enactment of Michaelis - Menten shlyakhom many of both parts on V max:

(4.4)

Graph in coordinates Vі V/ [S] is a straight line; V max, and the value V max / K M (Fig. 4.7). Wien allows you to just start Do M i V max, and you can also see it out of line, not in the front graph.

Small. 4.7. The method of linearization of the rivnyannya Mikhaelis - Menten

(By Edі - Hofsti)

Determination of enzyme activity. Diya of enzymes can be raised, or sometimes strangled with singing chemical words - Ingibitors ... For the nature of their own work, they are added to werewolves and non-negotiable ones. The basis of such a basis is the combination of an enzyme with an enzyme.

werewolves - tse dnannya, as non-covalently interacting with the enzyme, and when the activity of the enzyme is visible, the enzyme is renewed. The turnover of іngіbuvannya can be competitive, uncompetitive and uncompetitive.

butt competitive galvanizingє a series of structural analogs to the substrate, which can connect to the active center of the enzyme in a similar way, as the substrate, which does not convert the protein into the product; with the active center of the enzyme. As a result of the establishment of enzyme-ingibitor (EI) complexes, the concentration of ES-complexes decreases and, as a result, decreases the speed of the reaction. In other words, the competitive ingibitor reduces the speed of catalyzing by reducing the fraction of molecules to the enzyme, which called the substrate.

Vimіryuvannya of the variability of reactions at low concentrations allows the substrate to become more competitive than іngіbuvannya as uncompetitive. With a competitive іngіbuvannі on the graph of deposition 1 / V=f(1 / [S]) straighten all ordinates in one point 1 / V max directly in the presence of the Ingibitor, or, in the presence of the Ingibitor, the tangent of the kuta goes straight to the abscis axis, i.e. V max does not change, but K M grows, so that the change in the spore rate of the substrate to the enzyme in the presence of the Ingibitor is indicated (Fig. 4.8). Also, when a high concentration of the substrate in the minds of the competition for the active center, if the substrate is in the active center, the reaction can be used, and the speed of the reaction can begin to evolve. At the same time as Michaelis - Menten maє viglyad

(4.5)

de [I] - concentration of the ingibitor; K i - constant іngіbuvannya.

The constant іngіbuvannya characterizes the spore rate of the enzyme to the іngіbіtor and is the constant of the dissociation of the EI-complex:

(4.6)

In the presence of a competitive Ingibitor, the tangent of the kuta, straight up to the abscissa axis, increases by the value (1 + [I] / K i).

Small. 4.8. Competitive Ingibuvannya:

a - diagram; b - graphical rotation according to Lineuver - Burke

at noncompetitive inhibition The іngіbіtor takes into account the structure of the substrate and binds not to the active, but to the allosteric center of the enzyme. It is necessary to change the conformation of the active center of the enzyme, which is supervised to reduce the catalytic activity of the enzyme. Moreover, the ingibitor can be involved not only with the enzyme (E + I → EI), but also with the enzyme-substrate complex (ES + I → ESI). Offense forms EI and ESI are not active. The substrate and the ingibitor can be tied at once with a molecule of the enzyme, and even if it is not crooked. The action of a polyagus, which is non-competitive to the ingibitor, in a decrease in the number of wraps to the enzyme, and not in a reduced fraction, called the substrate of molecules to the enzyme. The Ingibitor does not convert ES-complexes, but it does not convert the substrate into a product. Vnaslidok tsyogo V max change, that is, in the presence of the Ingibitor, the straight line from the top of the ordinates will go to a larger point (Fig. 4.9). In the same world of growth and tangent kuta nahil straight up to the abscis axis, equal K M / V max I. Up to M on vidminu vid V max does not change, that uncompetitive ingibuvannya cannot be attributed to the increased concentration of the substrate.

Small. 4.9. Non-competitive Ingibuvannya:

a - diagram; b - graphical rotation according to Lineuver - Burke

Maximum speed of reaction V max I in the presence of a non-competitive Ingibitor is described by the equal

(4.7)

In vipad uncompetitive іngіbuvannya, If the ingibitor calls only with the ES-complex and does not call with the enzyme, on the graph of abandonment 1 / V = f(1 / [S]) straight parallel one to one and cross the y-axis and abscissa at different points (Fig. 4.10).

Small. 4.10. Uncompetitive Ingibuvannya:

a - diagram; b - graphical rotation according to Lineuver - Burke

non-negotiable ingibitories - the highly responsive to the development of the chemical nature, which can interconnect with the functionally important groups of the active center, setting up the micro-covalent links. Tse to produce to bezporotnoy loss of activity of the enzyme. At the link with the cym theory of Michaelis - Menten, it is based on stewed, but the attachment of the Ingibitor to the enzyme has a reversible character, in this vipad it does not stagnate.

The application of non-reversible ingibuvannya is the intermodulation of enzymes with the ions of important metals, which add up to sulfhydryl groups of cysteine ​​surplus enzyme and to create with a wide range of ferments - practically unavailable

The enzymatic activity of microorganisms in the bagat is also versatile. According to them, it is possible to establish not only the species and the type of belonging of the microbe, but also the significance of its options (so called biovari). The basic enzymatic power and quality are easily discernible.

The breakdown of carbohydrates (saccharolytic activity), i.e. When the acid is cleaved in the carbohydrate, it is an indicator of the change in the middle. This middle course is called "row row". Mikrobi, which does not ferment Danium into carbohydrates, grow in the middle, do not change. Evidently, gas will be installed for lighting the bulb in the middle with agar, or after the purchase of it in the "floats" in the middle of the middle. "Float" - a vuzka sklyana tube with a sealed tip, burnt up the mountain, put it in a test tube with the middle before sterilization.

In addition, the saccharolytic activity is vivchayut in the middle of Endo, EMC, Ploskirєva. Microorganisms, fermenting to acidity, are found in the middle of the milk tsukor (lactose), fix the colony - the acid of the change in the color of the obvious in the middle of the indicator. Colonies of microbes, which do not ferment lactose, without barn.

Milk with growth of microbes, fermenting lactose, burns out.

With the growth of microorganisms, where amylase is set up, in the middle of the starch with a small starch, the splitting occurs. You know about the price, having brought Lugol's line to the culture of the splinter, the color of the middle does not change. Non-cleavage of starch is even due to the size of the blue barn.

Proteolytic power (i.e., healthy splitting of beads, polypeptides, etc.) When growing on the gelatinous middle of the microbes, ferment the gelatin, the middle grows. The nature of the development, how to get caught up in small microbes, growth. Mikrobi, which dissolves casein (milk beetle), viklikayut peptonezatsiyu milk-vono poured into the eyes of milk syrovat. When peptones are split, indol, syrwater, amiak can be seen. Їх will be installed for the additional help of indicator papіrtsіv. Smell the filter with singing lines, hanging, dividing with vuzhny pigs up to 5 - 6 cm. Pislya incubation in thermostats will provide the result. Amiak wiklikak blue litmus papirtsya; if water is seen on papyrtsi, leaked with 20% strength to lead acetate and sodium hydrogen carbonate, the approval of lead sulphate - papyretsya chorniyu is taken; Indol viklikє pochvonіnnya papіrtsі, leaked out with a large amount of oxalic acid.



In addition to the meanings of the middle, the quality of microorganisms in the development of growing substrates can be used for the supplementary paper disks, leaked with chemical reagents (system of indicators of paper "SIB"). These disks are lowered into tubes with pre-juvenile culture, and after 3 years incubation in thermostats at 37 ° C, according to the change in the color of the disks, one can judge about the dispensed in carbohydrates, amino acids, bile acids, etc.

Hemolytic power (health of ruinuvati erythrocytes) vivchayut in the middle with blood. Ridky middle ground at the same time will be clear-cut, and on the middle middle ground near the colony there will be a clear-cut zone. When methemoglobin is approved, the middle is green.

CONSERVATION OF CROPS

Vidіlenі і vivchenі cultures (shtami), which represent value for science, or vyrobnіstva, take in museums of living cultures. The All-Union Museum is located in the Sovereign NDI Standardization and Control of Medical Biological Preparations. L.A. Tarasevich (GISK).

The head of the zberigannya is to educate the life of microorganisms and to get ahead of their ministry. For a wide demand, weaken or pinch the exchange in the microbial client.

One of the most thorough methods of trivial preservation of cultures is lyophilization - hanging in a vacuum from a frozen mill, allowing the setting of anabiosis. Visushuvannya to spend in special apparatuses. Take culture in sealed ampoules at a temperature of 4 ° C, more beautifully at -30-70 ° C.

Renovation of hanging crops.

Strongly heat the tip of the ampoule in the half of the pallet and push it up with a cotton swab, slightly soaking with cold water, microscopic stains appear on the slopes, through which it happens to seep into the middle of the ampoule. At the same time, passing through the rosіgrіtі land of thrusts, wіth wіth thе sterilization.

Do not forget that there is a vacuum in the sealed ampoule. As soon as you drink in it, you drink it all at once through the great opening, you can sprinkle it in the ampoule of culture and status of the Wikid.

If you let go by chance, I quickly smack and see the top of the ampoule with a pair of tweezers. Slightly scorch the openings with a sterile pasteurized pen, or add a syringe to the ampoule with a bottle (broth or isotonic). Remix ampoules and transfer to the middle. The growth of new crops in the first crops can be made.

Trivially zberigati culture It is also possible in native nitrogen (-196 ° C) in special attachments.

Methods of non-trivial preservation of cultures of the offensive: 1) subculture (periodical repetition in the middle of the middle) with intervals, so that the powers of microorganism, middle and minds of cultivation can be found. If I re-feed the culture, take it at 4 ° C; 2) saving a ball of butter. Grow the culture in 5-6 cm agar, pour sterile vaseline oil (a ball of oil about 2 cm) and store it vertically in the refrigerator. The term is taken from the small microorganisms of the development, to that from the test tubes they periodically hang the culture, to reconsider the life; 3) zberigannya at -20-70 ° C; 4) zberigannya in sealed test tubes. If necessary, take the material hanging on the middle.

Chapter 8. phages

Phages are viruses of bacteria and a number of other microorganisms. The singing minds have a stink of lizis (razchinennya) of their masters. The diya of phages is manifested in nature and vicarious in practice.

Fig. 42 Bacteriophages

History of the phage display and recovery. In 1898 N.F. Gamalia showed that the filtrate of siberian bacilli through the disease of new cultures of microorganisms, In 1915 R.F. , saving the quality of the recognition of microorganisms culture. The manifestation of lysis of microorganisms has been described, but the nature of it is not invented. The axis of honor of the vidkrittya bacteriophage should lie with the Canadian vcheny d "Erelle.

D "Erell (1917) vivchav filtrati vyporozhnen, which took home a sick person for dysentery and introducing into the test tubes with freshly seeded culture of the plant ailment plant. sick.

D "Erelle showed how the health of the filter was used during the last passages on new cultures of bacteria. more in number.

Vіdkritiy vіrus d "Erell calling bacteriophage - devouring bacteria (in Greek. Phagos - devouring), and the phenomenon - bacteriophages.

The corpuscular nature of the phage and its morphology is confirmed by the Bull electronic microscope.

Vіdkrittya d "Erellya privernulo uwagi lіkarіv, SSMSC zastosuvali phage for lіkuvannya i profіlaktiki number іnfektsіynih hvorob. The Danian hour phages widely vikoristovuyut in medichnіy praktitsі i at rіznih bіologіchnih doslіdzhennyah. Phages zaymayutsya bakterіologi, vіrusologi, bіohіmіki, genetics, bіofіziki, molekulyarnі bіologi, eksperimentalnі oncologists, faculty of genetic engineering and biotechnology, etc. Vivchennya phage triva, which is one of the most famous chapters of biology.

the power of phages

Phage morphology. Most of the phages are stored from the head and the caudal appendix, which means they can be separated from the head and spermatozoa. Nibilsh vivcheni T-phages of intestinal sticks). Їх growth is an empty cylinder (shearing), covered with a chohl and end with a basal plate with thorns and fibrils. Growth of phages, shape and size of the head, additional growth and growth of growth in small phages. For example, phages are seen with a large sprout, which does not speed up, phages with a short sprout, without an outgrowth and thread-like

Chemistry warehouse phage. Yak and all viruses, phages are composed of nucleic acids of the same type (DNA-phages are often formed) and protein. A nucleic acid molecule, twisted into a spiral, is located in the head of the phage. Phage shell (capsid) and sprout may be of a blue nature. A lytic enzyme takes place at the vilny end of the sprout, lysozyme or hyaluronidase.

Phage interaction with a sensitive cell go through the last stages. The entire cycle is borrowed in the old systems of bacterial phage from decilcochium up to 1-2 hours.

Stage I - the adsorption of phage particles on the surface receptors of the cell line to follow the auxiliary filaments of the tail outgrowth. Hundreds of phages can be adsorbed on one cell (for the lysis of the cell to finish one). The adsorption of phages is specific.

Stage II - penetration (ін'єкція) of nucleic acid and phage into cells of young phages is displayed in a different way. In T-phages of the intestinal stick, the spines of the basal plate stick to the cell wall. The haircut "punctured" the clitinnu stinka. The enzyme is found in the sprout, most often lysozyme, ruin cytoplasmic membrane. With a large chokhol, the growths speed up, and through the shearing canal, the nucleic acid of the phage is "injected" into the cell. Empty the bilkovo phage shell ("tin") will be left behind.

Stage III - reproduction of a nucleic acid and a phage in the middle of a cellin.

Stage IV - the folding and formation of the mature particles of the phage.

Fig. 43 Budov phage.

1 - head; 2 - DNA; 3 - rod; 4 - chokhol; 5 - basal plate; 6-thorns; 7 - fillet tails.

Fig. 44 Morphology of phages.

1 phage with a head, sprouting and speeding up like a head; 2 - head and sprout, without speedy health; 3 - head and short extension; 4 - tailless phages; 5 - filamentous phages.

Stage V-lysis of cellini and appearance of adult particles of phage from it. Call for reviewing the culture of navkolishnє center to enter a number of hundreds of new phages, old feuds of children. Such a lysis is called the middle lysis.

In the middle of the lysis from the middle of the lysis, the lysis is displayed only if the number of phages is adsorbed on the cells at once. The stench is coming in culture numerically open, through yaki vitika instead of klitini. In such a rank, during lysis, the phage does not multiply, and the number of this part does not grow.

Behind the character of the house, the microorganisms develop the virulent and intertwined phages.

Virulent phages wick the lysis of an infected cell at the entrance to the midst of a large number of phage particles, which are hostile to new cells. At the same time, the culture of microorganisms is lysed. Ridke the middle age is old enough to see the approval of phagolizates - the middle one, in which there is a large number of phages. When a virulent phage develops in bacteria, it grows in the middle of the disease, it is established either to see the disease of the succinct lysis, or to grow in the same way to see it - the colonies of the phage. Їх are called negative colonies (plaques). Colonies - small phages grow in size and structure.

Partial phages do not lyse all cells in the population. In part of them, the phages enter into symbiosis: the nucleic acid of the phage (its genome) will wake up in the chromosome of the cell, and I will name it about Phage. To see the confirmation of a single chromosome. Bacterial clitine with a whole lot of gin. The prophage, having become a part of the cellin genome, when multiplied, can be transmitted to an unlimited number of sites, i.e., to new cells. The phenomenon of symbiosis of microbial cells with a phage (prophage) is called lisogenous, and culture, in general, is called lysogenic. This is the name of the image of the prophage spontaneously leaving the chromosome of the cell, passing into the cytoplasm, transforming into an external phage. Those cultured cells, in which a branched phage has settled down, go (lyse), and they take over Lizogenia.

Scheme of the main stages of the interaction of the phage with the bacterial cell.

1 - injection of nucleic acid and phage into the clerk; 2-young, how to multiply

phages; 3 - maturity of phage; 4 - vision of phages.

Lizogeny of culture behind its main powers does not appear as out-of-life, even the stink of stink until it is re-infected with the same phage. With the development of lyzogeny, the culture of penetrating viprominuvannya (singing doses and exposure of X-ray, space exchanges), actions cheeky speeches In a number of other officials, the production of virulent phage and lysis and culture cells is significantly increasing.

Small phages can bring Skoda to microbiology. For example, those who produce vaccines, antibiotics and others biological speeches Lizogenia appears, because it is not safe for the transition of the phage to the branched one, so that it can cause the lysis of the virobny to follow.

The phage is a straining factor in the reduction of microorganisms. The prophage can change the power of the microbial culture, for example, the growth of the building up to toxicity, which helps to promote the middle of diphtheritic sticks, scarlet fever and inn. In addition, by changing into a virulent form and lyzing the cell, the phage can seize a part of the chromosome of the clergy-ruler and transfer the whole part of the chromosome to the cell, the phage will once again move to the prophage, and the cell is rejected by the new power.

The expansion of phages in nature is everywhere. Phages develop there, because there are microorganisms that are sensitive to them: near the water, runtі, stichny waters, Vidіlenikh people і tvarin і t. D. Mayzhe all kinds of bacteria є governors of phages specific to them.

The range of phages to physical and chemical factors in food, but not in vegetative forms and gentlemen. Phages are heated to 75 ° C, trivially hung, pH from 2.0 to 8.5. The stench is not sensitive to antibiotics, thymol, chloroform and a number of other words, which can affect the microflora. That is why the speech is vicious when seeing and sparing phages. Acid and disinfectant speech teeth for phages.

Practically storing phages

The stagnation of phages is based on their supreme specificity and building capacity, or to enter into symbiosis with them.

Phage prophylaxis and phage therapy-amelioration and detection of infections for other phages are based on the fact that they are developing in the organism of a sick ailment, the phage is known to him. In this hour, phages are widely stagnant in cases of infection and prevention of staphylococcal and streptococcal infections, such as those that do not come into being for antibiotics, as well as cholera, plagues and a number of proteicose infections, intestinal infections, intestinal infections.

Phage diagnostics includes: a) identification of visual cultures for additional species (diagnostic) phages. Culture leads to that phage, such as її lisis. For example, if the lysis of cholera phage wicks, then the culture of cholera wіbrіon. Suvora, the specificity of typical phages gives the ability to type variants in the middle species (phagovari). Fagotinization is of great importance in epidemiology, as it allows you to establish a number of nutritional conditions; b) the identification of an unidentified phage by test cultures of microbes. If the phage lyses the culture of the dysentery, then the dysentery phage; c) accelerating the method of diagnostics for an additional reaction, the increase in the titer of the RNTF phage does not increase the vision of the pure culture of the animal. Preliminary material (from a sick person or from the objects of the new middle) and indicator phage, the titer of which is strictly established, should be introduced into the broth.

Pomegranate phages grow widely in the presence of cardinal nutritional biology. From the help of the implantation genetic code, reached great successes in gennіy іngineering, їkh vicoristoyu for vivchennya plumpy growth, as a factor of diminution of microorganisms and in the last preliminaries. So as the lizogeny of culture on the basis of the "healthy" is sensitive to radioactivity, the stench to serve for the purpose of the mission of the owner of space ships from space exchanges: in case of improper lysis, the prophage transforms into the form of the virus.

Phage preparations

When phage preparations are violated, they creep with good strains of microorganisms and phages, which are allowed to rotate in reactors, so that they can be removed. great numbers phagolisates.

Phages are dispensed in viglyadi (ampoules and vials), in tablets and candles. Pigulka of phages, intended for sucking through the mouth, cover the acidic membrane, and preying phages from hydrochloric acid and slurry juice.

All phage preparations are subject to viscous control for the viscosity of third-party flora, lack of longevity and activity (titer), which can be detected on the basis of the release of the virus. Vibration control shall be carried out in the State NDI Standardization and Control of Medical Biological Preparations. L.A. Tarasevich. When a phage of diseases is issued with a label, it is indicated in which it is indicated: set, yogo, name of the phage, seria, control number and term of affinity. The skin packaging is secured by instructions for storing and harvesting the phage.

In bagatokh vipadkah, the reference molar amount of the enzyme is unavailable. It is accepted that the amount of enzyme is judged by the speed of reaction, as it was catalyzed in the singing minds of the word. The value of the activity of the enzyme is not a direct value of its number, since the speed of the enzymatic reaction is proportional to the concentration of the active enzyme.

For the decisions of the Committee on enzymes of the International Biochemical Union (1961), for the international unit of activity of the enzyme, the same amount is used, which catalyzes the transformation of 1 micromole to a substrate in one micromole at 30 ° C. Nutrient activity is in units of enzyme activity per 1 mg of a bottle or per 1 mg of a preparation.

According to the international system of calls (1972), a new international unit of activity for the enzyme is recommended - katav. By rolling a batch of enzyme, it is necessary to dissolve 1 mol of the substrate into the product in one second (mol / s).

The assignment of a number of units of activity to the enzyme up to cal- Tal to become µmol / xv - 60 µmol / s - 16.67 nmol / s. Again, the unit of activity of the enzyme is 16.67 ncat.

Normal functioning of organs and tissues of organisms є in the form of coordinated functions of all regulatory systems, including enzymes. It is possible to increase the change in the activity of one enzyme, or to bring about a breakdown of the metabolism. With any etiology of ailments, infectious or invasive, there are changes in the activity of enzyme systems, and in the whole sense of all ailments are seen as metabolic.

A lack of damage to the singing enzyme systems in the body has revealed a lot of ailments of food and people. So, in the form of anemia, viclikanі in the erythrocytes of pyruvate dehydrogenase, glucose-6-phosphate dehydrogenase, methemoglobin reductase. Often, the pathogenesis of a pathological process is not easy to do. Schob z'yasuvati, yaka, the enzyme system is ruined, followed by a lot of factors; necessary tissue biopsies, vibrations of diagnostic reactions, activators or enzymes.

The need to determine the activity of syrovatous enzymes is based on the pre-set, which changes in their activity represent the changes that appear in the singing organ. There are two types of ferment that can be found in the ferment: one is specific for the ferment, the role is specific;

With a number of pathologies (stroke), there may be a change in cell penetration and an increase in the number of cell lines, which can lead to the release of internal cell enzymes into the plasma. Low molecular weight enzymes emerge in cich vipads.

In the diagnosis of pathology around the organ, the activity of the enzyme characteristic of the given organ is ideal. However, it’s not a pity to go, there’s some metabolism in the other organs of the opposite. And all the same, it is possible to set up tissue or organ-specific enzymes, the activity of those visual functions of the singing tissues or organs. For example, adjusting the activity of acid phosphatase in the blood characterizes the appearance of prostate swelling; an increase in the activity of lactate dehydrogenase and creatinphosphokinase in the blood of a blood є by an even informative diagnostic test, which is an imaging of the heart muscle tissue. An increase in the activity of LDH ^ and LDH 2 isozymes in the blood is indicative of myocardial infarction, an increase in the activity of LDH and aspartate aminotransferase to indicate the outbreak of cells to the brain. The connection between the activity of enzymes and the pathological process is not possible at all, intelligence, ale and d

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