What is Biochemistry

• Biochemistry is the application of

chemistry to the study of biological
processes at the cellular and molecular
level.
• It emerged as a distinct discipline
around the beginning of the 20th
century when scientists combined
chemistry and biology to investigate the
chemistry of living systems by:
 Studying the structure-details in next
lecture
 Chemical reactions and Interaction of
molecules in living organisms
Aspects covered in Biochemistry
  Studying structure
• The chemistry of living organisms is organized around
carbon, which accounts for more than half the dry weight of
cells.
• Carbon can form single bonds with hydrogen atoms, and
both single and double bonds with oxygen and nitrogen
atoms.
• Of greatest significance in biology, is the ability of carbon
atoms to form very stable single bonds with up to four other
carbon atoms.
• Covalently linked carbon atoms in biomolecules can form
linear chains, branched chains, and cyclic structures. It seems
likely that the bonding versatility of carbon, with itself and
with other elements, was a major factor in the selection of
carbon compounds for the molecular machinery of cells
during the origin and evolution of living organisms. No other
chemical element can form molecules of such widely
different sizes, shapes, and composition.
Structure of DNA and cell wall: An example of structural study in
Biochemistry
  Chemical reactions inside a living
organism
• Photosynthesis: The conversion of CO2 and H2O to glucose.

• Respiration: The conversion of glucose to CO2 and H2O in the presence of oxygen with release
of energy.

Activity-Brain storming

• What factor causes these reactions to take place?

 I, You, We?
 Air?
 Water?
 Light?
 Fuel?
Enzymes
What are enzymes?
• Much of the history of biochemistry is the history of enzyme research. Biological
catalysis was first recognized and described in the late 1700s. Buchner discovered
that yeast extracts could ferment sugar to alcohol, proving that fermentation was
promoted by molecules that continued to function when removed from cells.
Name “enzyme” was given to these molecules at a later stage.

• ENZYMES are responsible to carry the chemical reactions which take pace inside
living bodies. Enzymes are similar to catalysts, which speed up the chemical
reactions outside a living body.

• Except for some of the originally studied enzymes such as pepsin (act on
proteins), rennin (coagulation of milk), and trypsin (act on proteins), most
enzyme names end in “-ase". Such as urease, oxidorecductase.
 Structure/properties of enzyme
• Mostly enzymes are proteins. Like all proteins, they are also made of “amino acids”.
• Their catalytic activity depends on the integrity of their native protein
conformation.
• Enzymes have an “active site”-a site where the reactions takes place.
• If an enzyme is denatured or dissociated, catalytic activity is usually lost.
• Structure and shape of enzyme is important to maintain catalytic activity of an
enzyme.
• Factors such as temperature, pH can destroy or accelerate enzymes activity. Every
enzyme works under its own specific condition.
• Enzymes remain un changed after the reaction-reusable
Classification of enzymes
Few examples
 How enzyme works?
• Enzymes work in form of a lock and key model.

Enzyme Enzyme-Substrate complex = Products (P)

How enzyme works?
 How enzyme works?

 Some enzymes require an additional component for their activity. The additional
component can be either:
• a cofactor—either one or more inorganic ions, such as Fe2+ Mg2+ Mn2+ for their
activity
• a co enzyme—complex organic or metalloorganic molecule. Most are derived from
vitamins, organic nutrients required in small amounts in the diet.

 Some enzymes require both a coenzyme and one or more metal ions for activity.

 A coenzyme or metal ion that is very tightly or even covalently bound to the
enzyme protein is called a prosthetic group. A complete, catalytically active
enzyme together with its bound coenzyme and/or metal ions is called a
holoenzyme. The protein part of such an enzyme is called the apoenzyme or
apoprotein.
How enzyme works?
 Factors affecting enzyme activity
• Temperature: Like most chemical reactions, the rate of an enzyme catalyzed reaction
increases as the temperature is increased. A 10° C rise in the temperature will
increase the activity of most enzymes by 50-100%. Variation in the reaction
temperature, as small as 1-2° C, may introduce a 10-20% increase in the reaction rate.
Most enzymes are adversely affected by a temperature above 40° C. They are rapidly
denatured, i.e. lose catalytic activities. Enzymes lose their activity at extremely low
temperatures as well. This may account for storing enzymes at 5° C or below without
affecting the enzymatic activity permanently.

• PH: Enzymes are affected by changes in the pH. The most favorable pH, at which an
enzyme exhibits its maximum activity, is known as the optimum pH for the enzyme.
Extremely high or low pH values generally result in complete loss of enzymatic
activity. The optimum pH value varies greatly from enzyme to enzyme.
 Factors affecting enzyme activity

• Concentration of Substrate: Increase in the substrate concentration

gradually increases the velocity of enzyme reaction within the limited range of
substrate levels. Three distinct phases of the reaction are observed in the graph.
 Factors affecting enzyme activity
• Inhibitors and activators: Many molecules affect the rates of enzyme catalyzed
reactions. Some molecules bind to the enzyme or the substrate or the enzyme-
substrate complex and lower the reaction rate. These are known as inhibitor
molecules. Similarly, some bind to the enzyme molecule and consequently increase the
reaction rate. These are known as activator molecules.
• Concentration of Enzyme: As the concentration of the enzyme is increased, the
velocity of the reaction proportionately increases
Factors affecting enzyme activity
 The application of enzymes industrial level:

There re three main advantages of using enzymes in industrial

processes.

1. They are specific in their action and are therefore less likely to
produce unwanted by-products.
2. They are biodegradable and therefore cause les environmental
pollution.
3. They work in mild conditions, i.e. low temperatures, neutral pH and
normal atmospheric pressure, and are therefore energy-saving.

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