Introduction to Biochemical

Engineering
Department of Chemistry-KYU
2018

CHE 324

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 Kissa R.A

(Ind. Chem, MSc. Chem. Eng.)

Industrialist-Pharmaceuticals
Renewable energy
Catalysis-Photocatalysis (MOFs)

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 Course content
• Basic concepts of enzymes: Chemical nature of
enzymes, enzyme partners, enzyme
classification, enzyme kinetics
• Production and purification of enzymes;
enzymatic: enzyme immobilization
• Application of enzymes

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 References
• Lehninger, A.L ‘Principles of biochemistry’
Butterworth publishers New York 1993)
• Lee JM, ‘Biochemical Engineering’, Prentice
Hall (1992)
• Bailey and ollis, ‘Biochemical Engineering
fundamentals’, McGraw Hill (1996)

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 Introduction
Biochemical Engineering

Biology Chemical Engineering

Biochemical Engineering is a marriage between Biology and

Chemical Engineering Where the principles and techniques
of chemical engineering are applied to enhance the product
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formation fromLecture
biological
1
systems 5
 Biology (Bios = life; logos = study) is
defined as the branch of science
dealing with the study of the living
things

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 Major differences between living
and non-living things

• Locomotion
• Growth
• Respiration
• Reproduction
• Metabolism

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 Other features of living things
• A high degree of chemical complexity microscopic
organization.
• System for extracting, transforming and using energy
from the environment.
• A capacity for precise self replication and self assembly.
• Mechanism for sensing and responding to the
alteration in their surroundings.
• Defined functions for each of their components and
regulated interactions among them
• A history of evolutionary change

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 Living

Cells

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 Basic concept of Enzymes
• Biocatalysts synthesized by living cells
• Protein in nature, colloidal, thermolabile and
specific in action
• Kuhne used the word enzyme to indicate
catalysis in biological systems.

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 Chemical nature of enzymes
• Invariably proteins (except ribozymes): They are
high molecular weight compounds made up
principally of chains of amino acids linked
together by peptide bonds.
• Functional unit of enzyme is known as
holoenzyme
• Holenzyme is made up of apoenzyme (protein
part) and coenzyme (non-protein organic part)
• Holoenzyme(active enzyme)Apoenzyme
(protein part)+Coenzyme (non-protein part)
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 Enzyme vs catalyst
Catalyst • Enzyme
• Work • Works efficiently at 37 oC
efficiently at
high • Catalysis with higher velocity
temperatures • E.g CO2  H 2 O     H 2 CO3
carbonic anhydrase

and high • In absence of the enzyme 200

pressures molecules of carbonic acid was
• Slow catalysis formed in an hour, in presence of
enzyme carbonic anhydrase
600,000 molecules/sec was
formed, reaction rate accelerated
by 10 million times

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 Enzyme active site
• The part of the enzyme where the substrate
binds is called the active site(since that’s
where the catalytic “action” happens).
• An enzyme attracts reactant molecules
(substrates) to its active site, catalyzes the
chemical reaction by which products are
formed, and then allows the products to
dissociate (separate from the enzyme
surface).

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 Enzyme partners
• Co-enzymes; organic molecules that bind
loosely to the active site of enzymes and
participate in catalysis e.g NAD (nicotine
adenine dinucelotide) FAD (flavine adenine
dinucelotide) etc,
• Co-factors; inorganic substances required to
increase the rate of catalysis e.g. metal-ions;
these include K+, Fe++, Fe+++, Cu++, Co++, Zn++,
Mn++, Mg++, Ca++, and Mo+++

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Prosthetic groups – organic or metal ion
substance which are firmly attached to proteins
or enzymes by covalent bond. e.g peroxidase
and catalase in haem is a prosthetic group.

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 Classification of enzymes
• Enzymes are classified based on their catalytic
behavior and they include:
• Oxidoreductases
• Transeferases
• Hydrolases
• Lyases
• Isomerases
• ligases

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• Oxidoreductases; involved in oxido-reduction
reactions e.g. succinate dehydrogenase
(reduces FAD to FADH2 and oxidises
succinate in TCA cycle occurs in
mitochondria)
• Transeferases; catalyses the transfer of the
functional group e.g. hexokinase this
phosphorylates hexoses (six-carbon sugars-
glucose-substrate), forming hexose phosphate
(product)

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• Hydrolases; brings hydrolysis of various
compounds e.g lipase, protease, amylase,
cellulase, etc
• Lyases; addition to double bond such as C=C,
C=O, C=N and removal of water e.g. aconitase
(removal of water molecule from citrate in
TCA cycle in mitochondria)

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• Isomerases ( A-B-C → B-A-C) e.g
phosphohexose isomerase
that interconverts glucose-6-phosphate (G6P)
and fructose-6-phosphate (F6P)

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• Ligases; formation of bonds with ATP cleavage.
Enzymes catalyzing syhthetic reactions where
two moecules are joined together and ATP is
used e.g. DNA ligase.

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 Enzyme kinetics

• Enzymes accelerate reactions by lowering free

energy of activation
• Enzymes do this by binding the transition
state of the reaction better that the substrate.
• Catalytic activity; turnover number is defined
as the maximum number of moles of
substrate that can be converted to product
per mole of catalytic site per second

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 Factors affecting the enzyme activity
(class discussants-15 minutes)

• Temperature
• pH
• Substrate/product concentration
• Etc

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 END OF Lecture one
Thank you

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