CHAPTER ONE
INTRODUCTION AND LITERATURE REVIEW
1.1 Enzyme
Enzymes
are large biological molecules responsible for thousands of chemical
inter-conversions that sustain life (Smith, 1997). All known
enzymes
are proteins. They are high molecular weight compounds made up principally of
chains of amino acids linked together by peptide bonds, they are denatured at
high temperature and precipitated with salts, solvents and other reagents. They
have molecular weights ranging from 10,000 to 2,000,000 units.
Enzymes
do not cause reactions to take place, but rather they enhance the rate of
reactions that would
have been slower without their presence and still
remains unused and unchanged.
Many
enzymes
require the presence of other compounds - cofactors - before their catalytic
activity can be exerted. This entire active complex is referred to as the
holoenzyme; i.e. apoenzyme (protein portion) plus the cofactor (coenzyme,
prosthetic group or metal-ionactivator) is called the holoenzyme (Alexopoulos
et
al., 1996)
The living cell is the site of tremendous biochemical activity called
metabolism. It is the process of chemical and physical change which goes on
continually in the living organism involving the build-up of new tissues,
replacement of old tissue, conversion of food to energy, disposal of waste
materials, reproduction - all the activities that we characterize as
"life."Thephenomenon of enzyme catalysis makes possible biochemical
reactions necessary for all life processes. Catalysis is defined as the
acceleration of a chemical reaction by some substance which itself undergoes no
permanent chemical change. Synthetic molecules called artificial
enzymes
also display enzyme like catalysis (Grovesm, 1997).
The catalysts of biochemical reactions are
enzymes
and are responsible for bringing about almost all of the chemical reactions in
living organisms. Without enzymes, these reactions take place at a rate far too
slow for the pace of metabolism(Bairoch, 2000).
Enzymes
actually work by lowering the activation energy of a reaction. This is achieved
when it creates an alternative pathway which is faster for the reaction hence
speeding it up such that products are formed faster. Enzyme catalysed reactions
are million times faster than uncatalysed reactions, they alter the rates but
not the equilibrium constant of the reaction being catalysed (Ashokkumar
et
al., 2001). A few RNA molecules called ribozymes also catalyse reactions,
with an important example being some parts of ribosome (Lilley, 2005).
1.1.1 Types of enzymes
Metabolic enzymes: These have been called
the spark of life, the energy of life and the vitality of life. These
descriptions are not without merit. Metabolic enzymes catalyse and regulate
every biochemical reaction that occurs within the human body, making them
essential to cellular function and health (Sangeetha
et al.,2005).
Digestive
enzymes
turn the food we eat into energy and unlock this energy for use in the body.
Our bodies naturally produce both digestive and metabolic enzymes as they are
needed. They either speed up or slow down the chemical reactions within the
cells for detoxification and energy production. The enable us to see, hear, and
move and think. Every organ, every tissue and all 100 trillion cells in our
body depend upon the reaction of metabolicenzymes and enjoy their energy
factor. Without these metabolic
enzymes,
cellular life would beimpossible.
Food enzymes:These are introduced to
the body through the raw foods we eat and throughconsumption of supplemental
enzyme products. Raw foods naturally contain
enzymes
providing asource of digestive enzymes when ingested(Hossain
et al.,
1984). However, raw food manifests only enough enzymesto digest that particular
food, not enough to be stored in the body for later use (the exceptionsbeing
pineapple and papaya, the sources of the enzymes bromelain and papain). The
cooking andprocessing of food destroys all of its enzymes. Since most of the
foods we eat are cooked orprocessed in some way and since the raw foods we do
eat contain only enough
enzymes
toprocess that particular food (Persike
et al., 2002) our bodies must
produce the majority of the digestive enzymes werequire, unless we use
supplemental
enzymes
to aid in the digestive process. A variety ofsupplemental enzymes are available
through different sources. It is important to understand thedifferences between
the enzyme types and ensure that one is using an enzyme product which willmeet
one’s particular needs.
Plant based enzymes:These are the most
popular choice of enzymes. They are grown in a laboratorysetting and extracted
from
Aspergillus species. The enzymes harvested from
Aspergillusspecies
are called plantbased, microbial and fungal. Of all the choices, plant based
enzymes are the most active. Thismeans they can break down more fat, protein
and carbohydrates in the broadest pH range than any other sources (Ashokkumar
et
al., 2001).
1.1.2 Characteristics of enzymes
Protein nature:Enzyme is a protein. The main
components of an enzyme is protein.
Temperature: Enzymes
are sensitive to temperature. Many work best at temperatures close to body
temperatures and most lose their ability to catalyse if they are heated above
60 or 70o C. (Ashokkumar
et al., 2001).
Acidity and alkalinity:Many
enzymes
work best at a particular pH and stop working if the pH becomes too
acidic or alkaline.
Catalytic effect:It acts as catalyst, enzyme functions in
accelerating chemical reaction, but the enzyme itself does not change after the
reaction ends.
Specificity:It functions specifically. The enzyme only
catalyzes one kind of substrate and cannot function for many substrates. The
term is called one enzyme one substrate.
Reversibility: It means the enzyme does not determine the
direction of reaction, but it only functions in accelerating reaction rate
until it reaches equilibrium. The enzyme also functions in substance synthesis
and substance breaking down reaction.
Small quantity:It is required, in small amount. A small
amount of enzyme is able to catalyze a chemical reaction (Nason, 1968).
CHAPTER ONE
INTRODUCTION AND LITERATURE REVIEW
1.1 Enzyme
Enzymes
are large biological molecules responsible for thousands of chemical
inter-conversions that sustain life (Smith, 1997). All known
enzymes
are proteins. They are high molecular weight compounds made up principally of
chains of amino acids linked together by peptide bonds, they are denatured at
high temperature and precipitated with salts, solvents and other reagents. They
have molecular weights ranging from 10,000 to 2,000,000 units.
Enzymes
do not cause reactions to take place, but rather they enhance the rate of
reactions that would
have been slower without their presence and still
remains unused and unchanged.
Many
enzymes
require the presence of other compounds - cofactors - before their catalytic
activity can be exerted. This entire active complex is referred to as the
holoenzyme; i.e. apoenzyme (protein portion) plus the cofactor (coenzyme,
prosthetic group or metal-ionactivator) is called the holoenzyme (Alexopoulos
et
al., 1996)
The living cell is the site of tremendous biochemical activity called
metabolism. It is the process of chemical and physical change which goes on
continually in the living organism involving the build-up of new tissues,
replacement of old tissue, conversion of food to energy, disposal of waste
materials, reproduction - all the activities that we characterize as
"life."Thephenomenon of enzyme catalysis makes possible biochemical
reactions necessary for all life processes. Catalysis is defined as the
acceleration of a chemical reaction by some substance which itself undergoes no
permanent chemical change. Synthetic molecules called artificial
enzymes
also display enzyme like catalysis (Grovesm, 1997).
The catalysts of biochemical reactions are
enzymes
and are responsible for bringing about almost all of the chemical reactions in
living organisms. Without enzymes, these reactions take place at a rate far too
slow for the pace of metabolism(Bairoch, 2000).
Enzymes
actually work by lowering the activation energy of a reaction. This is achieved
when it creates an alternative pathway which is faster for the reaction hence
speeding it up such that products are formed faster. Enzyme catalysed reactions
are million times faster than uncatalysed reactions, they alter the rates but
not the equilibrium constant of the reaction being catalysed (Ashokkumar
et
al., 2001). A few RNA molecules called ribozymes also catalyse reactions,
with an important example being some parts of ribosome (Lilley, 2005).
1.1.1 Types of enzymes
Metabolic enzymes: These have been called
the spark of life, the energy of life and the vitality of life. These
descriptions are not without merit. Metabolic enzymes catalyse and regulate
every biochemical reaction that occurs within the human body, making them
essential to cellular function and health (Sangeetha
et al.,2005).
Digestive
enzymes
turn the food we eat into energy and unlock this energy for use in the body.
Our bodies naturally produce both digestive and metabolic enzymes as they are
needed. They either speed up or slow down the chemical reactions within the
cells for detoxification and energy production. The enable us to see, hear, and
move and think. Every organ, every tissue and all 100 trillion cells in our
body depend upon the reaction of metabolicenzymes and enjoy their energy
factor. Without these metabolic
enzymes,
cellular life would beimpossible.
Food enzymes:These are introduced to
the body through the raw foods we eat and throughconsumption of supplemental
enzyme products. Raw foods naturally contain
enzymes
providing asource of digestive enzymes when ingested(Hossain
et al.,
1984). However, raw food manifests only enough enzymesto digest that particular
food, not enough to be stored in the body for later use (the exceptionsbeing
pineapple and papaya, the sources of the enzymes bromelain and papain). The
cooking andprocessing of food destroys all of its enzymes. Since most of the
foods we eat are cooked orprocessed in some way and since the raw foods we do
eat contain only enough
enzymes
toprocess that particular food (Persike
et al., 2002) our bodies must
produce the majority of the digestive enzymes werequire, unless we use
supplemental
enzymes
to aid in the digestive process. A variety ofsupplemental enzymes are available
through different sources. It is important to understand thedifferences between
the enzyme types and ensure that one is using an enzyme product which willmeet
one’s particular needs.
Plant based enzymes:These are the most
popular choice of enzymes. They are grown in a laboratorysetting and extracted
from
Aspergillus species. The enzymes harvested from
Aspergillusspecies
are called plantbased, microbial and fungal. Of all the choices, plant based
enzymes are the most active. Thismeans they can break down more fat, protein
and carbohydrates in the broadest pH range than any other sources (Ashokkumar
et
al., 2001).
1.1.2 Characteristics of enzymes
Protein nature:Enzyme is a protein. The main
components of an enzyme is protein.
Temperature: Enzymes
are sensitive to temperature. Many work best at temperatures close to body
temperatures and most lose their ability to catalyse if they are heated above
60 or 70o C. (Ashokkumar
et al., 2001).
Acidity and alkalinity:Many
enzymes
work best at a particular pH and stop working if the pH becomes too
acidic or alkaline.
Catalytic effect:It acts as catalyst, enzyme functions in
accelerating chemical reaction, but the enzyme itself does not change after the
reaction ends.
Specificity:It functions specifically. The enzyme only
catalyzes one kind of substrate and cannot function for many substrates. The
term is called one enzyme one substrate.
Reversibility: It means the enzyme does not determine the
direction of reaction, but it only functions in accelerating reaction rate
until it reaches equilibrium. The enzyme also functions in substance synthesis
and substance breaking down reaction.
Small quantity:It is required, in small amount. A small
amount of enzyme is able to catalyze a chemical reaction (Nason, 1968).