BIOLOGICAL CATALYSIS

1. Biological Catalyst
Dr.Gurumeet C Wadhawa ,Assistant Professor, Department
of Chemistry.
Rayat Shikshan sansthas Veer Wajekar ASC
College,Phunde,Uran

2. Introduction
▪ A catalyst is a substance which alters to promote the reaction,
and a substance especially an enzyme, that initiates or modifies
the rate of a chemical reaction in a living body is termed as
biocatalyst.
▪ They are enzymes or microbes that initiate or accelerate
chemical reactions

3. ENZYMES:
• Enzymes are chemical substances
which are mostly proteins.
• Enzymes catalyze nearly all the
biochemical reactions in the living
cells.
• They have unique three dimensional
shapes that fits the shape of
reactants
• Enzymes are typically derived from
plants, micro-organisms (yeast,
bacteria or fungi) or animal tissue (e.g.
protease from pancreas).

4. Production Of
Enzyme
• Commercial sources of enzymes are obtained from three
primary sources, i.e. animal tissue, plants and microbes.
• These naturally occurring enzymes are quite often not readily
available in sufficient quantities for food applications or
industrial use.
• However, by isolating microbial strains that produce the
desired enzyme and optimizing the conditions for growth,
commercial quantities can be obtained.

5. Production Of
Enzyme(Cont.)
• This artificial method of producing enzyme was earlier
known as Fermentation.
• Today, this fermentation process is carried out in a
contained vessel. Once fermentation is completed, the
microorganisms are destroyed; the enzymes are isolated,
and further processed for commercial use.
• Enzyme manufacturers produce enzymes in accordance
with all applicable governmental regulations, including the
appropriate federal agencies such as FDA(Food & Drug
Administration, Chemical industries, research laboratories)

6. Types of Biocatalyst
• Oxidoreductases: catalyze oxidation/reduction reactions.
For example, alcohol dehydrogenase converts primary alcohols to aldehydes.
In this reaction, ethanol is converted to acetaldehyde, and the cofactor, NAD,
is converted to NADH. In other words, ethanol is oxidized, and NAD is reduced.
• Transferases: transfer a functional group. alanine aminotransferase
shuffles the alpha-amino group between alanine and aspartate.

7. Types of
Biocatalyst(Cont.)
• Hydrolases: catalyze the hydrolysis of various bonds
For example, phosphatases break the
oxygen-phosphorus bond of phosphate esters.
• Lyases: Formation or removal of a double bond with group transfer.
For example, Dehydratases remove water,
as in fumarase (fumarate hydratase).

8. Types of
Biocatalyst(Cont.)
• Isomerases: catalyze isomerization
changes within a single
molecule(Rearrangements) .For example,
triose phosphate isomerase, carry out these
rearrangements.
• Ligases: removing the elements of water
from two functional groups to form a single
bond.

9. Types of
Biocatalyst(Cont.)
• Kinase: This enzyme in the body attaches a
phosphate group to a high energy bond. It is
a very important enzyme required for ATP
production and activation of certain
enzymes.

10. Some Important Enzymes of
Human Body
Digestive Enzymes
Digestive enzymes are secreted by the body that helps in
digestion of food. The names of enzymes that help in digestion are:
Amylase: This enzyme helps in breaking down carbohydrates.
It is found in saliva, pancreas and intestinal juices.
Proteases: It helps in digestion of proteins.
It is present in the stomach, pancreatic and intestinal juices.
Lipases: Lipases assist in digestion of fats.
It is seen in the stomach, pancreatic juice and food fats.

11. Reaction for breakdown of
Carbohydrates , Protein and Fat

12. Factor affecting
catalytic activity of
enzyme
1.Enzyme Concentration: Product
Concentration increases
with the increase of enzyme concentration.

13. Factor affecting
catalytic activity of
enzyme
2.Substrate Concentration: It has been shown
experimentally that if the amount of the
enzyme is kept constant and the substrate
concentration is then gradually increased,
the reaction velocity will increase until it
reaches a maximum. After this point,
increases in substrate concentration will
not increase the velocity (delta A/delta T).
This is represented graphically in Figure .

14. Factor affecting
catalytic activity of
enzyme
3.Effects of Inhibitors on Enzyme Activity:
Enzyme inhibitors are substances which
alter the catalytic action of the enzyme and
consequently slow down, or in some cases,
stop catalysis. There are three common
types of enzyme inhibition - competitive,
non-competitive and substrate inhibition.

15. Factor affecting
catalytic activity of
enzyme
4. Temperature Effects: 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.

16. Factor affecting
catalytic activity of
enzyme
5.Effects of 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. This is graphically illustrated
in Figure.

17. DNA replication
• DNA replication is a biological process
that occurs in all living organisms .
• Biocatalysts are the most important
aspect in molecular biology(DNA
replication, cloning) e.g. Polymerases (to
polymerize), Restrictases(to cut the
DNA strands) ,DNA ligases( to bind the
DNA strands).

18. Application in Medical
Field.
1.Diagnostic Purpose 2.Therapeutic purpose

19. Industrial Application of
Enzyme Biocatalysis:
• Enzymes are the most proficient catalysts,
offering much more competitive processes
compared to chemical catalysts.
• The number of industrial applications for
enzymes has exploded in recent years,
mainly owing to advances in protein
engineering technology and environmental
and economic necessities.

20. Biocatalysts in industrial
biotechnology
• Fine and bulk chemical industries:
Enzymes provide a more powerful way of producing
enantiomerical pure compounds mainly through high
chemoselectivity, regioselectivity, and streoselectivity. Some
examples showing the contribution of biocatalysis to fine and bulk
chemical fields are described here.

21. Examples:

22. Pharmaceutical industry
• The pharmaceutical substances have become increasingly
complex, and public and environmental quests for green
technologies have increased. Therefore, the industry is
seeking low-cost, safer, and greener biocatalytic processes as
alternatives to traditional chemical catalysis
• Specific reactions that can be replaced with biocalaysis have
been identified in the synthesis of pharmaceuticals, including
chiral amine synthesis, stereo and regio-specific hydroxylation
of complex molecules, and other redox reactions.

23. Examples:

24. Food industry
• most uses of biocatalysis have focused on
hydrolytic reactions for debranching, improving the
solubility, and clarification.
• A recent trend in the food industry is to develop
functional foods such as prebiotics, low-calorie
sweeteners, and rare sugars.

25. EXAMPLES

26. Cosmetic industry
• Recently,the cosmetic industry has faced a challenge because
of increasing consumer demands for natural and eco-friendly
cosmetics.
• Arbutin is the most common skin-lightener, and is known to
inhibit melanogenesis without causing melano-cytotoxicity
• As an enzymatic approach to producing arbutin, various
enzymes have been used, including α-amylase, α-glucosidase,
transglucosidase, sucrose phosphorylase, and dextransucrase

27. Textile industry
• For the development of cleaner processes, the use of
enzymes is rapidly growing. Typical examples include
the staining of jeans using cellulase from Trichoderma
viride , and a bio-carbonization process in the case of
wool .
• Cellulase and protease are used in the polishing step
for clear dyeing, the improvement of color and surface
vividness, and resistance to wrinkles.

28. Demerits of
Biocatalysts:
• Enzymes require narrow operation parameters.
• Enzymes display their highest catalytic activity in water.
• Enzymes may cause allergies.
• Often low specific activity.
• Instability at extreme temperatures and pH values.
• Availability for selected reactions only - long development
time for new enzymes.

29. Possibilities
• Over the past decades, enzyme-based processes have continuously
substituted traditional chemical processes in many areas, especially
fine chemical and pharmaceutical industries. Owing to the
development of new technologies in enzyme engineering as well as
economic pressure and public concern about environmental pollution,
such replacement will be more accelerated.
• Therefore, it would be a great chance for researchers to explore new
applications and technologies in enzyme engineering.
• Current trend in enzyme engineering based on the focused-directed
evolution in conjunction with computational methods will continue
and even accelerate.

30. References:
•BIBLIOGRAPHY: Outlines of Biochemistry- Eric Conn, Paul Stumf WEBLIOGRAPHY:
•http://www.lsbu.ac.uk
•http://www.worldofteaching.com
•http://www.enzymes.me.uk
•http://www.enzymetechnicalassoc.org
•http://www.media.wiley.com
•http://www.sc.ehu.es
•https://bodytomy.com/enzymes-in-body
•https://www.cliffsnotes.com/study-guides/biology/biochemistry-i/enzymes/six-types-of-enzyme-catalysts
•Tanja Gulder, Baran Group Meeting 07/11/2009: http://www.scripps.edu/baran/images/grpmtgpdf/Gulder_Jul_09.pdf
•Choi J-M, et al, Industrial applications of enzyme biocatalysis: Current status and future aspects, Biotechnol Adv (2015),
http://dx.doi.org/10.1016/j.biotechadv.2015.02.014
•Bennett, T. P., and Frieden, E.: Modern Topics in Biochemistry, pg. 43-45, Macmillan, London (1969).
•Holum, J.: Elements of General and Biological Chemistry, 2nd ed., 377, Wiley, NY (1968).
•Martinek, R.: Practical Clinical Enzymology: J. Am. Med. Tech., 31, 162 (1969).
•Harrow, B., and Mazur, A.: Textbook of Biochemistry, 109, Saunders, Philadelphia (1958).
•Pfeiffer, J.: Enzymes, the Physics and Chemistry of Life, pg 171-173, Simon and Schuster, NY (1954)

31. THANK YOU