Enzymes are protein catalysts that speed up the rate of biochemical reactions but do not change the structure of the final product. Like a catalyst, without being used up, the enzymes control the speed and specificity of the reaction, but unlike catalysts, only living cells generate enzymes.
The rate of biochemical reaction often influences enzymes like catalysts, so that they can take place at a relatively low temperature. The enzymes are thus known to lower the energy of activation. In certain cases, the biological response is initiated by enzymes.
The term enzyme is derived from the Greek word enzymes, meaning 'in yeast' since the enzyme activity in living organisms was first discovered by the yeast cells. The enzyme term was invented by W. Kuhne in 1878.
Physically, enzymes act as colloids or as high-molecular-weight compounds.
At a temperature below the boiling point of the water, enzymes are killed or inactivated.
Most enzymes in the liquid medium are inactivated at 60 degrees Celsius.
Extracting dried enzymes can withstand temperatures of 100 degrees Celsius to 120 degrees Celsius or even higher. Enzymes are, therefore, thermos-labile.
The optimum activity of each enzyme is always at a particular temperature, which typically varies from 25 degrees Celsius to 45 degrees Celsius. At 37 degrees Celsius, enzyme action is strongest and as temperatures rise above 60 degrees Celsius, enzymes become inactive.
Catalytic Properties: Biological catalysts are enzymes. The greater amounts of compounds are catalyzed by a small number of enzymes. This means that enzymes are highly capable of turning giant amounts of the substrate into a substance. Enzymes improve the reaction rate and remain unaffected by the reaction they catalyze.
Enzyme specificity: Enzymes are extremely variable in nature, which means that a specific enzyme can catalyze a specific reaction. For example, only sucrose hydrolysis can be catalyzed by Enzyme sucrase.
Enzymes initiate the biochemical reaction rate and accelerate it.
The activity of enzymes depends on the medium acidity of the (pH specific). At a particular pH, each catalyst is most active. PH 2 for pepsin, pH 8.5 for trypsin, for example. At near neutral pH, most intracellular enzymes act.
The reaction in either direction can be accelerated by enzymes.
Both enzymes have active sites involved in biochemical reactions.
Enzymes, often soluble in water, dilute glycerol, NaCl, and dilute alcohol, are very unstable compounds.
At the optimum temperature, enzymes work aggressively.
In nature, all enzymes are proteins, but all proteins may not be enzymes.
Enzymes lower the molecule's activation energy so that the biochemical reaction can take place at the normal temperature of the body, which is 37 degrees Celsius.
Proteins are all enzymes, but all proteins are not enzymes. However, there are several conjugated enzymes bound to the protein portion of the enzyme with a non-protein moiety, which is called the Apo enzyme. The portion of the non-protein is known as the cofactor. If the co-factor, like potassium calcium, magnesium, manganese, is of an inorganic type, it is known as the prosthetic group. In general, the prosthetic group is closely bound to the protein portion of the enzyme and it is difficult to separate it with a simple technique such as diffusion. The enzyme is called a holoenzyme with the prosthetic group and the Apo enzyme.
If organic moulds such as NADP, NAD, FAD, etc. are co-factor attached to an enzyme protein, it is called a coenzyme. In general, a coenzyme is loosely bound to the Apoenzyme and can be isolated easily from the prosthetic group. Often, coenzymes are heat tolerant.
Mechanism of Enzyme Action
The behaviour of the enzyme is greatly influenced by the reaction conditions; unique temperature and pH conditions are needed for most enzymes. The lock and key model will better describe the mechanism of enzyme action and its selectivity.
By providing a surface for the substrate, an enzyme brings down the activation energy of the reaction. The mechanism of enzyme action has been a matter of research ever since their identification. The enzyme provides the substrate with a surface for the response to take place. A complex (intermediate) forms the substrate, which then supplies the substance and the enzyme. There is a complex configuration of the substrate that is connected to the enzyme and can only fit into a specific enzyme similar to that of a lock that has a particular key.
The activity of enzymes in the biological system and their selective nature have led to many biological catalysts being produced. Scientists are now working on several artificial enzymes being synthesized. In the coming days, the analysis of bio-reactions and their catalysts will serve as the basis for making wonders.
Question 1: Explain the Properties of Enzymes.
Ans: Enzymes are incredibly capable biological molecules - they work on cellular reactions and speed up the rates at which they occur. Cellular processes would stop at a pace that would make life difficult without these biological catalysts, at least in the way we know it today. Enzymes-
act as biological catalysts, accelerating the reaction rate.
turn a single source of energy into a much more useful form of energy.
do not function alone and usually need cofactors called helper molecules
are highly specific, which means that they bind to and catalyze a single reaction or a group of closely related reactions to a specific substrate.
are primarily proteins, but some molecules of RNA may also serve as catalysts.
are not exhausted and remain at the end of the reaction unchanged.
Question 2: Explain the Most Important Properties of an Enzyme?
Ans - The most important properties of an enzyme are:
1. Enzymes have an extraordinary ability to catalyze. In very small amounts, they are involved. To transform a large quantity of substrate, a small amount of enzyme is enough. The enzymes after the reaction remain unchanged.
2. Specificity -
Enzymes in their behaviour are very unique. Particular enzymes function exclusively on unique substrates. Enzymes are unique to a specific form of reaction as well.
3. Reversibility -
Most of the reactions catalyzed by enzymes are reversible. The reversibility of the reaction is based on the cell's requirements. There are distinct forward and reverse reaction enzymes in some situations. Some reactions catalyzed by enzymes are not reversible.
4. Sensitiveness to heat and temperature and pH -
Enzymes are very heat- and temperature-sensitive. Thermolabile, they are. At the typical temperature, the optimum activity of Associate in Nursing protein is. The right temperature is considered the optimal temperature for the utmost operation. At very low temperatures, enzymes would be inactive; this is the explanation for the refrigerator preserving food and vegetables.