Introduction:

The cell is the structural and functional unit of life—the basic building block of living systems.
Cells have the capability to effectively utilize biocatalysts, known as enzymes, which have
outstanding catalytic efficiency and both substrate and reaction specificity. Enzymes have
amazing catalytic power and their high level of specificity for their substrate makes them suitable
for biological reactions. They are crucial for cellular metabolism. Each and every chemical
reaction that takes place in plants, micro-organisms and animals proceeds at a quantifiable rate as
a direct result of enzymatic catalysis. Most of the history of biochemistry is directly or indirectly
related to the history of enzyme research. Catalysis in biological systems was initially reported in
the early 1800s based on research into the digestion of meat. In this report the catalytic activity
of secretions from the stomach, the conversion of starch into sugar by saliva, and various plant
extracts were reported.

Chemical Nature of Enzymes

Having laid the foundation of the enzymic conversion of compounds, several enzymes were
isolated from living cells. The true nature of enzymes was established by James Sumner in 1926
when he extracted and crystallized an enzyme, urease from jack beans. He also determined its
chemical nature and composition. It is now well known that all enzymes, without exception, are
proteins having a three-dimensional structure. About 150 enzymes have been prepared in pure
crystalline form. Many of them contain a non-protein component, called prosthetic group, which
may be covalently or non-covalently linked with the enzyme molecule. Enzymes therefore are
defined as biological catalysts, a kind of protein molecules formed by the living cells which
catalyze a particular reaction or a group of closely related reactions.

Properties of enzymes

All enzymes are synthesized within the cells and can pass through cell membranes under certain
condition. An essential property of these catalysts is speeding up the rate of chemical reactions
and while doing so they remain unchanged without loss of catalytic activity. Many enzymes
produced by the cell carry out metabolic reaction within the cell are hence called endoenzymes.
Some enzymes are liberated by the cell and catalyze reaction in the vicinity of the cell. These are
calledexoenzymes.

Many enzymes contain a non-protein component which could be either an organic compound or
a metal ion. The non-protein component is called a coenzyme, while the metal ion forms a
cofactor. The enzyme and the prosthetic group together form a holoenzyme. If the cofactor is
dissociated from the enzyme molecule, it loses its catalytic function and is called apoenzyme.
The substance on which the enzyme acts is called substrate. Most enzymes have specific
substrates whose specificity is determined by the protein or apoenzyme. The specificity of
enzymes towards their substrates is important because it exerts biological control over metabolic
function some of the properties that can be attributed to enzymes are:

1. Enzymes are present in the cell in small amount only.

2. During the course of catalytic activity, their chemical nature is not altered irreversibly, hence
they can participate in many individual reactions over and over again.
3. The chemical equilibrium of an enzyme catalyzed reaction remains unchanged. Usually
enzymes favour a chemical reaction by accelerating it. However, they can reaction in a reverse
direction provided it is favoured by an increase in the ratio of products to reactants.

Biological washing powders • Contain: - lipase: greasy stains - protease: eggs, blood

• Advantage: they work at lower temperatures, so less water heating is needed, and clothes don´t shrink.

Food industry

• Fruit juices: are extracted using pectinase. It breaks down pectin and is much easier to squeeze juice
from the fruit. It also makes the juice clear rather than cloudy. • Biscuits: - isomerase: converts glucose to
fructose, which is sweeter so less needs to be used in slimmers biscuits. - protease: softens
glutens, making the roller of biscuits easier
Germination of seeds • Amylase is found in seeds. • When the seed begins to germinate, it catalyses the
break down of insoluble starch to soluble maltose. • The maltose is used by the growing embryo : -as an
energy source - to make cellulose for new cell walls.

Overview
An enzyme is a type of protein found within a cell. Enzymes create chemical reactions
in the body. They actually speed up the rate of a chemical reaction to help support life.

The enzymes in your body help to perform very important tasks. These include
building muscle, destroying toxins, and breaking down food particles during
digestion.

An enzyme’s shape is tied to its function. Heat, disease, or harsh chemical conditions
can damage enzymes and change their shape. When this happens, an enzyme doesn’t
work anymore. This affects the body processes the enzyme helped support.

Enzymes are produced naturally in the body.

For example, enzymes are required for proper digestive system function. Digestive
enzymes are mostly produced in the pancreas, stomach, and small intestine. But even
your salivary glands produce digestive enzymes to start breaking down food
molecules while you’re still chewing. You can also take enzymes in pill form if
you’re having certain digestive problems.

Types of enzymes
There are three main types of digestive enzymes. They’re categorized based on the
reactions they help catalyze:

 Amylase breaks down starches and carbohydrates into sugars.

 Protease breaks down proteins into amino acids.
  Lipase breaks down lipids, which are fats and oils, into glycerol and fatty
acids.

Why are enzymes important for

digestion?
Enzymes are essential for healthy digestion and a healthy body. They work with other
chemicals in the body, such as stomach acid and bile, to help break down food into
molecules for a wide range of bodily functions.

Carbohydrates, for instance, are needed for energy, while protein is necessary to build
and repair muscle, among other functions. But they must be converted into forms that
can be absorbed and utilized by your body.

How enzymes work in your digestive system

Amylase is produced in the salivary glands, pancreas, and small intestine. One type of
amylase, called ptyalin, is made in the salivary glands and starts to act on starches
while food is still in your mouth. It remains active even after you swallow.

Pancreatic amylase is made in the pancreas and delivered to the small intestine. Here
it continues to break down starch molecules to sugars, which are ultimately digested
into glucose by other enzymes. This is then absorbed into the body’s blood circulation
through the wall of the small intestine.

Protease is produced in the stomach, pancreas, and small intestine. Most of the
chemical reactions occur in the stomach and small intestine. In the stomach, pepsin is
the main digestive enzyme attacking proteins. Several other pancreatic enzymes go to
work when protein molecules reach the small intestine.
Lipase is produced in the pancreas and small intestine. A type of lipase is also found
in breast milk to help a baby more easily digest fat molecules when nursing. Lipids
play many roles, including long-term energy storage and supporting cellular health.

What affects enzymes?

Enzymes work best at your normal body temperature. The average body temperature
is 98.6°F (37°C), but normal body temperatures can range from 97°F to 99°F (36.1°C
to 37.2°C).

If you run a fever and your temperature increases too much, the structure of enzymes
breaks down. They no longer function properly. Restoring your body temperature to
its optimal range will help restore enzyme health.

Certain health conditions, such as pancreatitis, which is inflammation of the pancreas,

hurts your pancreas and can also reduce the number and effectiveness of certain
digestive enzymes.

The pH level of your stomach or intestines can also affect enzyme activity.

A low pH means something is very acidic. A high pH means it’s basic, also known as
alkaline. Enzymes work best in a fairly narrow pH range. If the environment
surrounding an enzyme becomes too acidic or too basic, the enzyme’s shape and
function will suffer.

Chemicals called inhibitors can also interfere with an enzyme’s ability to cause a
chemical reaction.
Inhibitors can occur naturally. They can also be manufactured and produced as
medications. Antibiotics are a good example. They inhibit or prevent certain enzymes
from helping bacterial infections spread.

Your diet can also influence your body’s enzyme activity. That’s because many foods
contain digestive enzymes that help share the burden of the naturally occurring
enzymes in your body.

For example, bananas contain amylase. So even though a banana is packed with carbs,
it also comes with amylase to help you digest it so you can use those carbs for energy
later.

Eating enzyme-rich foods can boost enzyme activity in your body. Just keep in mind
the calories and other nutritional information about the foods in your diet.

In addition to your diet habits, your body’s overall state of health will also affect how
well it produces, stores, and releases enzymes and how efficiently its enzymes
function. This will vary from one person to the next.

References:

https://www.healthline.com/health/why-are-enzymes-important#what-affects-enzymes

http://www.uvm.edu/~dstratto/bcor011_handouts/Vayda_lecture_notes/12%20Enzyme