CATALYSIS

AZUELO
FERRER
MEDIANA
CATALYSIS
The phenomenon in which
a small amount of
substance, called a
catalyst affects the rate
of chemical reaction
without itself being
affected.
CATALYSIS
Many everyday
products depend on
catalysts, thus,
playing a key role in
our lives; indeed, life
would not be possible
without them.
CATALYSIS
Industrial catalysis
has been responsible
for the vast growth of
chemicals
manufacture and
petroleum refining
worldwide.
HISTORY
The first period of catalysis dates back
to the dawn of civilization, at a date
lost in time when mankind began to
produce alcohol by fermentation. The
work done during the first period of
catalysis consists mainly of isolated
observations that were sporadically
documented without any effort made to
explain these phenomena.
HISTORY
The first period of catalysis
ended stridently when Jns
Jacob Berzelius
systematically investigated
the recorded observations
and classified them as
catalysis in 1835. The
conclusions drawn by
Berzelius were based upon
discussions and experimental
work with contemporary
scientists in Europe.
HISTORY
The second period was characterized by
systematic research and the discovery of
new catalytic processes. During this period
it became quite clear that catalysis was
applicable in most chemical processes and
that by implementing catalysis in an
industrial process there could be significant
financial gains. This new perception of
catalysis was clearly formulated by
Wilhelm Ostwald, who once wrote that
there is probably no chemical reaction
which cannot be influenced
catalytically.
HISTORY
The third period of catalysis begins sometime
during the end of the nineteenth century, when
the growth of academic knowledge translated
into industrial applications. At this point the
number of catalytic processes that had been
developed had grown into hundreds and the
economic potential of some of these processes
were highly feasible. There was also a general
growth in the demand for bulk chemicals and
therefore minimization of by-products, by
catalysis, had evident economic advantages. The
industrial production of bulk chemicals of this
period was at an all-time high during World War
1, when the demands on explosives based upon
nitric acid reached preposterous proportions.
HISTORY
The fourth period of catalysis began at the end of the
First World War, when the demand for explosives
diminished, and the industrial production shifted
towards the manufacturing of synthetic fuels and new
innovative processes such as Fisher- Tropsch, a
collection of chemical reactions that converts a
mixture of carbon monoxide and hydrogen into liquid
hydrocarbons. The most significant new process
innovation of this period was the FCC (Fluid Catalytic
Cracking) process, which enabled the Allied forces to
provide fuel to its fighters during World War Two. When
the war ended there was a notable change in the trend
of the catalytic industry and thus the end of the fourth
period of catalysis.
HISTORY
The fifth period, which lasted to some undefined point
at the beginning of the 1970s, was strongly
characterized by the petrochemical industry and
various catalytic processes for the manufacturing of
synthetic polymers. The dominating role of the
petrochemical industry was the result of the explosive
automotive market that had developed in Europe and
North America after World War Two. At some point
during the early 70s the world started to become aware
of the impacts that industry had on the environment,
partially sparked off by Rachel Carsons Silent Spring.
This new trend of thought gave birth to the discipline
of environmental catalysis. Environmental catalysis was
the first step towards the modern chemical industry
where catalysis is applied to almost every process,
including the production of fine chemicals for
pharmaceutical applications to the production of bulk
chemicals and exhaust gas catalysts.
HISTORY
The sixth period, which started
in the seventies, and that can
only be characterized by
continuous invention of new
catalytic processes, has not yet
clearly passed into a seventh
stage, the use of enzymatic bio-
catalysis.
IN GENERAL:
Catalysts generally react with one or more reactants to form
intermediates that subsequently give the final reaction
product, in the process regenerating the catalyst. The
following is a typical reaction scheme, where C represents
the catalyst, X and Y are reactants, and Z is the product of
the reaction of X and Y:
X + C XC (1)
Y + XC XYC (2)
XYC CZ (3)
CZ C + Z (4)
Although the catalyst is consumed by reaction 1, it is
subsequently produced by reaction 4, so for the overall
reaction:
X + Y Z
A CATALYST
can be:
HETEROGENEOUS
MOSTLY solids.
Mostly contain metals especially
those of Group VIII of the periodic
table, Pt being a prime example.
Physically, these catalysts
resemble sponges; small and
numerous pores.
HETEROGENEOUS
PALLADIUM PLATINUM
HOMOGENEOUS
MOSTLY acids, bases or organic amines.
Others consist of metals particularly transition
metals ex, Fe or Rh in the form of salt or
organometallic compound or a metal carbon
monoxide (metal carbonyl) compound.
This is most often the liquid phase, although
gas phase examples are known. Ozone in
the stratosphere, for example, is converted
into oxygen via the catalytic action of chlorine
atoms formed as a result of the photochemical
destruction of chlorofluorocarbon refrigerants.
HOMOGENEOUS
ENZYMES
also known as
ORGANOCATALYSTS
Enzymes are
"biological catalysts."
"Biological" means the
substance in question
is produced or is
derived from some
living organism.
Enzymes, as a subclass of
catalysts, are very specific in
nature. Each enzyme can act to
catalyze only very select
chemical reactions and only
with very select substances.
ENZYMES AS CATALYST
WHAT ARE ENZYMES AND
WHAT DO THEY DO?
Enzymes are proteins with highly specialized
catalytic functions, produced by all living
organisms.
Enzymes are responsible for many essential
biochemical reactions in microorganisms,
plants, animals, and human beings.
Enzymes are essential for all metabolic
processes, but are not alive.
Although like all other proteins, enzymes
are composed of amino acids, they differ
in function in that they have the unique
ability to facilitate biochemical reactions
without undergoing change themselves.
This catalytic capability is what makes
enzymes unique.
ENZYMES AS CATALYST
Enzymes are natural protein molecules that
act as highly efficient catalysts in biochemical
reactions, that is, they help a chemical
reaction take place quickly and efficiently.
Enzymes not only work efficiently and rapidly,
they are also biodegradable. Enzymes are
highly efficient in increasing the reaction rate
of biochemical processes that otherwise
proceed very slowly, or in some cases, not at
all.
ENZYMES AS CATALYST
An enzyme has been described as a "key"
which can "unlock" complex compounds. An
enzyme, as the key, must have a certain
structure or multi-dimensional shape that
matches a specific section of the "substrate"
(a substrate is the compound or substance
which undergoes the change). Once these two
components come together, certain chemical
bonds within the substrate molecule change
much as a lock is released, and just like the
key in this illustration, the enzyme is free to
execute its duty once again.
ENZYMES AS CATALYST
The Nature of Enzyme
Catalysis
Specific acid or base catalysis
- Enzymes are able to deprotonate or protonate a
substrate.
General acid or base catalysis
- It is similar from the specific acid or base catalysis, the
reaction rate can be increased by adding or removing a
proton.
Charge Neutralization
- When a substrate is charged when it is bound to the
enzyme, other residues of the opposite charge around
the enzyme can help to maintain the binding.
Nucleophilic catalysis
- Many enzymes binds substrates with covalent bonding.
Enzymes always are nucleophilic. Substrates are
electrophilic. Therefore, the enzymes attacks the
electrophilic center of substrates. This reaction is very
rapid.
The Nature of Enzyme
Catalysis
Electrophilic catalysis
- The enzyme reaction can be catalyzed by removing the
electron.
Bond strain
- There are different types of binding in the enzyme-catalyzed
reaction present such as hydrogen bonds, hydrophobic interactions,
and electrostatic interactions. When substrates bind on the active
site of enzymes, their structures may not be exactly
complementary to the site. These different types of binding energy
contribute the binding. Further, it helps the substrates bind
enzyme more tightly.
The Nature of Enzyme
Catalysis
MECHANISM
SOURCES OF
INDUSTRIAL
ENZYMES
PLANTS ANIMALS MICROBIAL/
BACTERIA
Malted grains
or tubers
(Amylase)
Pineapple
Bromelin
(Protease)
Fig Tree Ficin
(Protease)
Papaya Papain
(Protease)
Liver Catalase
(Peroxide
Breakdown)
Calf Stomach
Rennet/ Chymosin
(Milk Clotting)
Hog Stomach Pepsin
(Protease)
Hog Pancreas
Pancreatic Enzymes
(Several)
Digestive Tract
Trypain (Protease)
Amylase
Protease
Fungi (Molds
and Yeast)
amylase
Pectinase
Cellulase
Isomerase
Lactase (many
types of each)
Beta-glucanase
Hemicellulase
Amylase
catalyzes the
digestion of
starch into
small segments
of multiple
sugars and into
individual
soluble sugars.
Protease (or
Proteinase)
split up proteins
into their
component
amino
acid building
blocks.
Lipase
split up animal
and vegetable
fats and oils into
their component
part: glycerol
and fatty acids.
Cellulase
breaks down the
complex molecule
of cellulose into
more digestible
components of
single and multiple
sugars.
Beta-glucanase
(or Gumase)
digest one
type of
vegetable
gum into
sugars and/or
dextrins.
Pectinase
digests pectin
and similar
carbohydrates
of plant
origin.
PRODUCTION
OF ENZYME
CATALYST
Isolation of Microorganisms,
Strain Development and
Preparation of Inoculum
Microorganisms are isolated
on culture media following
the microbiological
techniques.
(a) production of enzyme in high
amount and other metabolites in low
amount,
(b) completion of fermentation
process in short time, and
(c) utilization by the microorganism
of low cost culture medium.
Aim for isolating a suitable
microorganism lies in:
Strains of
microorganisms are
developed by using
mutagenic chemicals
and ultraviolet light.
Isolation of Microorganisms,
Strain Development and
Preparation of Inoculum
Inoculum of enzyme producing
strains developed after
treatment of mutagens is
prepared by multiplying its
spores and mycelia on liquid
broth.
Isolation of Microorganisms,
Strain Development and
Preparation of Inoculum
Medium Formulation and
Preparation
Culture medium is formulated
in such a way that should
provide all nutrients supporting
for enzyme production in high
amount but not for good
microbial growth.
Medium Formulation and
Preparation
An ideal medium must have a
cheap source of carbon,
nitrogen, amino acids, growth
promoters, trace elements and
little amount of salts. Care must
be taken to maintain pH during
fermentation.
Medium Formulation and
Preparation
For a specific microbe pH,
temperature and formulation of
culture medium is optimized
prior to inoculation. Production
of enzymes increases with the
concentration of culture
medium.
Sterilization and
Inoculation of Medium,
Maintenance of Culture
and Fluid Filtration
Medium is sterilized batch-
wise in a large size
fermenter.
After medium is sterilized,
inoculation with sufficient
amount of inoculum is done to
start fermentation process.
Sterilization and
Inoculation of Medium,
Maintenance of Culture
and Fluid Filtration
Fermentation process is the
same as antibiotic production.
Sterilization and
Inoculation of Medium,
Maintenance of Culture
and Fluid Filtration
When fermentation is over
broth is kept at 5C to avoid
contamination. Fungal broth is
directly filtered or centrifuged
after pH adjustment.
Sterilization and
Inoculation of Medium,
Maintenance of Culture
and Fluid Filtration
Purification of
Enzymes
Enzyme purification is a
complex process but the
main steps of
purification are:
1. Preparation of
concentrated solution by
vacuum evaporation at
low temperature or by
ultrafiltration
Purification of
Enzymes
2. Clarification of
concentrated enzyme by
a polishing filtration to
remove other microbe
Purification of
Enzymes
3. Addition of
preservatives or
stabilizers
Purification of
Enzymes
4. Precipitation of
enzymes with
acetone, alcohols or
organic salts.
Purification of
Enzymes
5. Drying the
precipitate
Purification of
Enzymes
6. Packaging
Purification of
Enzymes
ENZYME EFFICIENCY
Enzymes work as a catalyst by
lowering the Gibbs free energy
of activation of the enzyme-
substrate complex. On the next
slide, are two figures showing a
basic enzymatic reaction with
and without a catalyst.
ENZYME EFFICIENCY
Looking at a simple enzymatic
reaction:
ENZYME EFFICIENCY
German biochemist Leonor
Michaelis and Canadian
biochemist Maud Menten derived
an equation later known as the
"Michaelis-Menten Equation",
shown below.
V
0
=V
max
[S]/K
M
+[S]
ENZYME EFFICIENCY
For K
M
we know that V
0
= V
Max
/2
V
Max
/2 = (V
max
[S])/(K
M
+ [S])
(K
M
+ [S])(V
Max
/2) = (V
max
[S])
(K
M
+ [S]) = (V
max
[S]) / (V
Max
/2)
K
M
+ [S] = 2[S]
K
M
= [S]
ENZYME EFFICIENCY
The Michaelis constant can be thought of
as the rate at which the substrate
becomes unbound to the enzyme, which
can either be in the events of substrate-
enzyme complex becoming the product,
or the substrate becomes unbound to the
enzyme. K
M
can be shown as an equation.
K
M
=k1+k2k1
ENZYME EFFICIENCY
Graphing V
0
vs [S] :
ENZYME EFFICIENCY
V
max
is the maximum rate the
reaction can run at, regardless of
[S], meaning that even if you add
more substrate, the reaction would
not go any faster. That is because
at V
max
all of the active sites on the
enzyme are occupied.
ENZYME EFFICIENCY
After all the explanations on various
forms of enzyme kinetic equations, we
arrive at our conclusion of catalytic
efficiency. Referring back to the earlier
reaction, we have:
ENZYME EFFICIENCY
k
2
is an irreversible reaction as oppose to an
equilibrium expression, when compared to
k
-1
and k
1
, k
2
is also known as k
cat
, the catalytic
efficiency of enzyme. V
0
is the measured reaction
rate, which is the product formation over time,
so we can conclude that an equation would end
up looking like the following:
v0=d[P] dt=k2[E]
0
Where [E]
0
is the total enzyme concentration.
ENZYME EFFICIENCY
V
Max
is observed when all of the enzyme-
substrate complex disappear and turn into
products, so we can make the following
assumption:
VMax=k2[E]
0
and after rearrangement, we have this equation:
kcat=k2=VMax[E]
0
ENZYME EFFICIENCY
That is the equation for calculating
catalytic efficiency, to be used
after we obtain data from
experiments and after using the
Michaelis-Menten Equation. With a
larger k
cat
, the enzyme is efficient
because less enzyme is needed.
ENZYME EFFICIENCY
FACTORS
AFFECTING THE
EFFICIENCY OF
ENZYMES
1. Enzyme
Concentration
The amount of enzyme present in a reaction is
measured by the activity it catalyzes. The
relationship between activity and
concentration is affected by many factors such
as temperature, pH, etc. An enzyme assay
must be designed so that the observed activity
is proportional to the amount of enzyme
present in order that the enzyme
concentration is the only limiting factor. It is
satisfied only when the reaction is zero order.
1. Enzyme
Concentration
Table I: Reaction Orders with Respect to Substrate Concentration
Order Rate Equation Comments
zero rate = k rate is independent of
substrate concentration
first rate = k[S] rate is proportional to
the first power of
substrate concentration
second rate = k[S][S]=k[S]
2
rate is proportional to
the square of the
substrate concentration
second rate = k[S
1
][S
2
] rate is proportional to
the first power of each
of two reactants
1. Enzyme
Concentration
2. Substrate
Concentration
more likely the driver of the entire reaction.
Can be interpreted and explained using the Michaelis-Menten
Equation
Michaelis constants have been determined for many of the
commonly used enzymes. The size of Km tells us several things
about a particular enzyme.
A small Km indicates that the enzyme requires only a small
amount of substrate to become saturated. Hence, the maximum
velocity is reached at relatively low substrate concentrations.
A large Km indicates the need for high substrate concentrations to
achieve maximum reaction velocity.
The substrate with the lowest Km upon which the enzyme acts as
a catalyst is frequently assumed to be enzyme's natural substrate,
though this is not true for all enzymes.
3.Inhibitors, Poisons
and Promoters
Catalyst INHIBITORS - substances that
reduce the action of catalysts (if reversible
reaction)
ex. Sildenafil (Viagra), Methotrexate,
penicillin
3.Inhibitors, Poisons
and Promoters
Catalyst POISONS - substances that
reduce the action of catalysts (if
irreversible reaction)
ex. Mercury and Lead compounds
3.Inhibitors, Poisons
and Promoters
PROMOTERS/ACTIVATORS- are
substances that increase the catalytic
activity, even though they are not catalysts
by themselves.
ex. MAGNESIUM ion (Mg2+) for Phosphatase
and ZINC ion (Zn2+) for carbonic anhydrase
3.Inhibitors, Poisons
and Promoters
Temperature
Like most chemical reactions, the rate of an
enzyme-catalyzed reaction increases as the
temperature is raised. A ten degree Centigrade rise
in temperature will increase the activity of most
enzymes by 50 to 100%. Variations in reaction
temperature as small as 1 or 2 degrees may
introduce changes of 10 to 20% in the results.
Over a period of time, enzymes will be deactivated
at even moderate temperatures. Storage of enzymes
at 5C or below is generally the most suitable. Some
enzymes lose their activity when frozen.
pH
Enzymes are affected by changes in pH. The most
favorable pH value - the point where the enzyme
is most active - is known as the optimum pH.
Extremely high or low pH values generally result
in complete loss of activity for most enzymes. pH
is also a factor in the stability of enzymes. As
with activity, for each enzyme there is also a
region of pH optimal stability.
pH
FOOD/FOOD
INGREDIENT
Sugar syrups from
starch
Meat Tenderizing
DAIRY APPLICATIONS
Cheeses
Cheese flavors
Lactose-free dairy
products
BAKING
APPLICATIONS
Bromate Replacer
BEVERAGE
APPLICATIONS
Low Calorie Beers
HOUSEHOLD & PERSONAL
CARE APPLICATIONS
Lower Temperature
& No Phosphate
Clothes Washing
Milder Dishwashing
Detergents
Textiles
Processing
Leather
Tanning with
Enzymes:
Dehairing,
Bating
INDUSTRIAL
APPLICATIONS
THANK YOU! :D