Imperial Cleaning

Courses in UTM

Such substances are called inhibitors, which may be competitive, non-competitive or un-competitive inhibitors. Wetting, Spreading Ally, Javed:

6.0 Nuclear Materials

All these theories will be applied later by looking at a few bioprocess case studies. The usual practices in industry such as the plant design, instrumentation control, costing and scaling up, as well as the knowledge in CGMP, GLP, ISO are also introduced in this course. This course covers historical aspect of plant and animal tissue culture, biology of cultured cells, design and layout of the cell culture laboratory, equipments and handling of the tissue culture.

Aseptic technique, general safety, culture vessels and media preparation and sterilization will be discussed. Other topics will include cultivation of plant and animal cells and tissues and some important applications. Laboratory sessions will be included to provide students experiences in handling and cultivation of plant and animal tissues. Introduces students to techniques in gene manipulation, protein expression, genomic cloning, cDNA, site directed mutagenesis, PCR and microarray. It will emphasize on the basic concepts in genomic and proteomic studies, DNA sequences as well as application of genetic therapies.

Upon completion, students should be able to define concepts and theories on molecular biology techniques and some application of techniques used in molecular biology. Laboratory hands-on will be carried out on selective topics. This course will emphasize on the study of both beneficial and detrimental effects of micro-organisms in food.

Initially this course will introduce the types of micro-organisms found in food, factors that affect their survival and growth in foods, and effects of microbial growth in foods.

Discussion focuses on microorganisms related to food spoilage and food preservation. Disease-causing micro-organisms are studied in the context of food safety. General principles of food preservation, contamination and food deterioration will be discussed in greater details. Pathogenic microorganisms and useful microbes in food will be differentiated for the industrial application. Halal issues are also addressed in relation to food safety.

This course emphasizes on the application of microorganism, plant and animal cell culture at various type of industry. The mechanism and processes of microbes at industrial level will be explained, which include production of primary and secondary metabolites by microbes, plant and animal cell culture using fermentation technology in commercial scale.

These also include antibiotic production, brewing process in beverages industry, food production, microbial spoilage of food and factors influencing. Microbes and biogeochemical cycle such as nitrogen cycle, sulfur and phosphate, immobilization technology and its uses in industry are also discussed. Current issue related with industrial microbiology will be highlighted.

This course is the first part of the Final Year Project. Each student will be assigned a topic and a supervisor at the beginning of Semester 1 of year 3. The students will also be trained to make a literature survey. At the end of the semester, each student is required to write a satisfactory progress report to be allowed to take SQBU in the following semester.

The evaluation of this course will be based on the progress report, evaluation by supervisor, and a possible oral presentation as required. In this course, fundamental knowledge of protein structure: Different techniques of extraction and purification using will be described. The efficiency of the protein purification technique is then evaluated in order to maximize protein recovery and purity.

This course elaborates the principles and application of plant and animal cell and tissue culture. The potential and the usage of tissue culture in biotechnology, research and industry involve transformation techniques, in vitro breeding, genetic engineering and germplasm conservation. The course will also provide knowledge in protoplast fusion, embryo rescue, haploid, and somaclonal variation. Upon completion, students should be able to explain some useful techniques in improving the quality of animal and plant including their health and development.

Discussion on the physiology of microorganisms, primary metabolic pathways, microbial metabolic diversity and secondary metabolism in microorganisms. The secondary metabolites with important application to health, industries and the environment will be described. In addition, microbial transformation of synthetic and naturally occurring recalcitrant molecules will be explained and outlined. Heavy metals biotransformation will also be included.

The biorefinery technology course will emphasize on the global issue of value added product from biomass. The benefit of chemical, enzymatic and microbial pretreatment will be identified. The criteria of biofuel and biomaterials from several substrates through several processes will be explained. The selection and criteria of microoganisms which involved in biorefinery will be identified. Student will have an exposure on the utilization of green technology and global model of biorefinery.

This course provides students with principle knowledge on waste management of different types of industrial wastes. Highlight will be given on the types of waste and their characteristics, pollution prevention technology and pollution reduction in various types of industry and industrial estate, including resource management in both regional and local areas.

Due to unplanned developmental activities as well as ever-increasing population, which have caused enormous strain on the environmental resources, societies across the world face several problems of environmental degradation.

However, it is imperative to maintain a balance between the capacity of the environment and the quantum of sustainable utilization. This is only possible by understanding the environment in its totality and the principles of its scientific management.

This course will be initiated by highlighting some of the key differences between the discovery and development of small molecules and biopharmaceuticals. Discussion includes the advancement of recombinant DNA technology in the exploitation of drug targets for the production of pharmaceuticals that provide health benefits. The second part of this course provides a brief overview of each class of macromolecules with respect to physiological role and clinical application.

The final part focuses on the future and advances that will enhance the ability to develop new and already identified macromolecules into safe and effective biopharmaceuticals. This part also describes gene and cell therapies, strategies that are needed when traditional drug therapy is not suitable or effective. The course will emphasize on fermentation technology and bioreactor design for microbial, plant and animal cell cultures.

The student will be exposed to the economics of fermentation technology, strain development and improvement, development of cost-effective medium for large scale fermentation. The physiology of microbial growth and product formation in batch, continuous and fed-batch cultures will be explained. The students will have knowledge on the differences between batch and continuous sterilization process. The kinetic of air sterilization and theory of fibrous filter will be explained.

The fluid rheologyand the bioreactor design for free and immobilised cell culture will be included in this course. The relationship between KLa and scaling up process will be explained. This course provides a body of knowledge relevant to the principles of enzymology and techniques employed in the utilization of enzymes. This course presents a basic introduction to the principles by which enzymes catalyze reactions and provide knowledge of the theory as well as applications of modern approaches to enzyme technology.

Students will also be introduced to the economic and commercial considerations concerning the viability of enzyme technologies. Generally, this course serves to provide an awareness of the current and possible future applications of enzyme technologies. Students are given practical experiences on basic techniques in enzyme technology such as protein extraction and purification.

Variety of protein purification techniques will be introduced besides the technique of enzyme immobilization for industrial applications. This course will introduce students to research methodology so as to develop understanding of the research process as applied to biological sciences.

Qualitative and quantitative research methods and approaches to solve problems are examined. An appropriate research methodology and analysis of a particular research problem is proposed and justified. The written proposal is evaluated based on the logical consistency of the written material and evaluate the outcome of a research project in terms of useable knowledge; and to design, defend and evaluate research proposals.

This course provides an introduction to bioethical principles used to make decisions when confronted with ethical issues involving the application and usage of biotechnology. The goal is to develop a framework for the appreciation and understanding of ethical dilemmas within the biotechnological, pharmaceutical and medical fields.

This course begins with a brief overview of ethics, and then moves to develop and consider the moral values and principles relevant to biotechnology and bioethics. The course hopes to develop moral wisdom knowledge about ethics and the ability to think ethically and moral virtue a stronger commitment to act morally. Students will also be introduced to fundamental bioethical review systems, including the theory of peer review and moral and ethical responsibilities of scientists.

This course covers the principles and methodology for Bioinformatics. It focuses on the application of computational methods and tools to study biological problems. This course will introduce the principles, scope, application and limitations of computational tools in bioinformatics. This course covers the principle and application of biotechnology in industry as well as current issues involved in molecular biotechnology.

The course will introduce genetic engineering basically from the perspective of advantages, strategies and the products. Some of the biotechnology products can be commercialized will be discussed as well. Production of transgenic plants and transgenic animals will be discussed in greater details especially on molecular techniques involved.

Subsequently the course deals with an introduction to eugenics, human genetic engineering and human cloning, techniques in gene therapy with its application. This course will also include an introduction to intellectual property, permission for usage, protection as well as benefits and relationship between biotechnology and intellectual property and current issues involved in biotechnology from various field. At the end of the semester, each student is required to present their findings and submit a report to the faculty on a certified date.

Evaluation of the course is based on oral presentation and submitted report. This course will present an overview of the fundamental principles and applications of biosensors. More specifically it will cover the following subjects: What is a sensor? How does a sensor become biological in nature? The history of biosensors. What are the components of a biosensor? What are the types of transducers used in biosensors? What are bioreceptor molecules? How are bioreceptor molecules attached to the transducers, i.

What are the most important factors that govern the performance of a biosensor? In what areas have biosensors been applied? This course covers definition and duties of environmental biotechnology, scope of use and the integrated approach of biological system in environmental biotechnology aspect. Fundamental aspect of microbes and metabolism will be part of the discussion prior to a more detailed explanation on the biological involvement in the control of pollution and bioremediation of pollutant in various types of environments.

Therefore, students will be introduced to the nature of biowastes, biological waste treatment and its important parameter affecting the process. The use of plant in environmental application will also be included.

This subject provides a basic knowledge of bioremediation and biodegradation. The process by which microorganism are stimulated to rapidly degrade hazardous organic contaminants to environmentally safe levels in soils, subsurface materials, water, sludges and residues is discussed.

Students are required to undergo Industrial Training LI in selected local industries or government bodies for 10 weeks. At the end of their training, students are required to submit a written report on their work. To be eligible for Industrial Training, a student must have obtained the following: Students will not be permitted to undergo Industrial Training, if i their total credit count is less than 40, or ii they were on Probationary Standing KS twice consecutively.

This course aims to strengthenand enhance the knowledge on principles of chemistry before students proceed to more specialized and higher level chemistry courses.

The first part of this course exposes students to fundamentals of atoms and molecules and chemical bonding, which are known to be the main sources of chemical processes.

The formation of chemical bonding, structure of molecules and properties of compounds are discussed. The second part of this course concentrates on stoichiometry and the relation between reacted species in chemical reactions. The last part of this course emphasizes on the fundamental knowledge of organic chemistry and introduces students to the concept of green chemistry. The course provides students with the understanding of the role of chemists and the relationship between chemistry and society so that they can make reasoned judgements on issues that are affected by the processes and products of chemistry.

The students will be introduced to the role of the chemist in researching, analyzing and developing chemistry knowledge and products for the purpose of benefiting mankind and for sustaining the world. The course also discusses research and development of chemistry and career prospects for chemistry graduates. Part of the course also provide students with the view of the foundation of chemistry through their applications to every day lives specifically in the topics of chemistry and the environment, green chemistry, food chemistry, chemistry of household products, cosmetics and personal care, medicines, drugs and crime.

This course introduces the classifications, synthesis and reactions of biomolecules such as carbohydrates, peptides, proteins and lipids. It will also emphasise on the three-dimensioal structures and fundamental concepts of stereochemistry. Infrared spectroscopy is included as a technique in characterizing the functional groups of compounds.

This course introduces students to the techniques and knowledge required in the synthesis or preparation of isomeric compounds, N-heterocyclic compounds, derivative of glucose, azo dyes and the isolation, purification and reaction of lipid.

Students will be exposed to the infrared spectroscopic technique as a tool to determine the functional groups of the synthetic and isolated compounds. The experiments selected for the course illustrate concepts explored in the Chemical Kinetics and Electrochemistry lecture, enable students to test the relation of theories with experiments, learn experimental methods used by physical chemist, develop laboratory skills and the ability to work independently, learn how to effectively present scientific results and appreciate the limitations inherent in both theoretical treatments and experimental measurements.

This course introduces the principles, instrumentation, and application of spectroscopic and chromatographic methods used in analytical chemistry. Emphasis is on ultraviolet-visible UV-Vis spectroscopy, fluorescence spectroscopy, mass spectrometry, atomic absorption spectroscopy and emission spectroscopy, liquid chromatography and gas chromatography.

The course introduces students to laboratory work related to instrumental methods of analysis. Experiments complement topics in Instrumental Analysis SSCC that include techniques in ultra violet-visible spectroscopy, atomic absorption spectroscopy, fluorescence spectroscopy, and flame emission photometry as well as liquid chromatography and gas chromatography.

This course is to introduce the students about polymers as materials with characteristic mechanical and physical properties, which are controlled by the structure and the methods of synthesis.

Topics covered in the course are polymer synthesis, the reaction of monomers to form polymers, copolymers or terpolymers either by chain-growth, step-growth polycondensation , ring-opening polymerisations. Polymerization mechanisms and polymerization kinetics related to degree of polymerization and molecular weight control and molecular distributions will be discussed in detail.

Physical aspect of polymer polymer structures, morphology, amorphous state and glass-transitions temperature Tg, crystalline state and melting temperature Tm will also be discussed. The inter-related molecular weights and molecular weight distributions on morphologies and their effects on the processing and final properties of polymers will be emphasized, as well as the structure-properties relation that influenced the overall properties of a polymer.

This course introduces basic computer data processing with no computer background required or assumed. The final year project gives the students the opportunity to demonstrate what they have learned throughout the course.

In the Undergraduate Project I, students are required to identify a project research and a supervisor in an agreeable field of chemistry. Apart from an initial briefing session on the Undergraduate Project I and laboratory safety requirement, there are no formal lectures to attend.

This course is designed to provide students with an understanding of the principles of analytical electrochemistry. Fundamental aspects of electrode reactions and structure of the interfacial region and application of electrode reactions to electrochemical characterization are included.

Major electroanalytical techniques will be discussed including potentiometry, amperometry, polarography, cyclic voltammetry, pulse and differential pulse voltammetry, square wave voltammetry, and stripping analysis.

Introduction to the principles of chemical and biochemical sensors will also be discussed. The course is intended to give an understanding of the basic principles of inorganic and organometallic polymers.

It will emphasise on the physical properties, chemical synthesis, the characterisation and practical applications of the polymers. All the major inorganic and organometallic polymers such as polyphosphazenes, polysilanes, polysiloxanes, polyferrocenes and other polymers will be dealt with. This course is designed to prepare students to formulate and solve material and energy balances on chemical process systems. It lays the foundation for courses in thermodynamics, unit operations, kinetics and process dynamics.

It introduces the engineering approach to solving process-related problems - breaking a process down into its components, establishing the relations between known and unknown process variables, assembling the information needed to solve for the unknowns using a combination of experimentation, empiricism and the application of natural laws to obtain the desired solution.

This course discusses the interconversion of various functional groups and the formation of C-C bonds; which represent two crucial areas in organic synthesis.

The retrosynthesis approach in organic synthesis will also be elaborated. Specific topic on carbonyl functionalities will be discussed which highlight the related condensation reactions. Further discussion on rearrangement, pericylic, asymmetric synthesis and metal-catalysed reactions will be emphasized.

Throughout the course, the usefulness of the synthetic methods will be related with their applications in various research and industry. Upon completion, the students should be able to plan synthetic strategy and pathway using both functional interconversion and C-C bond formation. The course teaches the chemistry of organometallic compounds. It includes the definition and classification of the compounds, electron rule and its limitations, types of bonding and methods of preparation followed by characterization of organometallic compounds.

The discussion continues with the type of reactions and application of organometallic compounds as catalysts and others; metal-carbonyl complexes: Organolanthanide and organoactinide chemistry.

The application of bioorganometallic compound: The course is focussed on the fundamentals of nuclear structure and physico-chemical properties in radioactivity. The mass-energy relationship presented in this course includes the binding energy of nuclear reactions - energetic of nuclear reactions, cross-section and types of reactions. Radioactivity phenomena as explained in rates of nuclear decay, determination of half lives and growth of radioactive products are covered.

Quantitative aspect of this course will be discussed under units of radioactivity, detection of radiation and instrumentation in radiochemistry. The study of the interaction of radiation with matter is included. Basic principles of nuclear reactors are also presented along with applications of radionuclides in chemistry and other related areas. Some aspects of nuclear energy generation, nuclear fuel reprocessing and nuclear waste disposal will also be discussed.

This course introduces the different types of ligands used in coordination chemistry and how their different modes of coordination lead to isomerism. The systematic way of naming metal complexes will be outlined. The different ideas on bonding in metal complexes will be discussed and this will help students to understand the advantages and limitations of each theory. The electronic spectra and colour properties of the metal complexes will be explained.

The substitution mechanistic pathways of metal complexes and its kinetics and how this mechanism is determined experimentally are illustrated. Spectroscopic characterization techniques of coordination compounds are also covered. The emphasis of this course is to provide the students with an appreciation for the synthesis and characterizations of coordination compounds.

It is also aimed to provide the students with a degree of competence in the laboratory skills required for accurate and precise chemical analysis. The experiments selected for this course include developing skills in the synthesis and isolation of coordination compounds or metal complexes with different kinds of ligands followed by characterization by conventional methods such as gravimetry, titrimetry and melting point, including characterization techniques used by coordination chemists such as UV-visible, NMR and FTIR spectroscopies.

The principles of the spectroscopic methods are described and discussed with respect to their respective spectral outputs and interpretation obtained from the as-synthesized coordination compounds. The emphasis of this course is to expose the students to the fundamental principles of molecular spectroscopy focusing on molecular energy levels and their interaction with electromagnetic radiation, spectral outputs and their interpretation in relation to molecular structure.

The branches of spectroscopy covered include rotational spectroscopy, vibrational spectroscopy IR and Raman , electronic spectroscopy absorption and emission and spin resonance spectroscopy NMR and ESR. The general spectrometer components and the requirements for high resolution spectrum of FTIR and FT NMR will be discussed to represent the practical aspects of this subject.

This course provides a basic introduction to quantitative chemical analysis, with emphasis on classical chemical methods. The course introduces general analytical techniques that include sampling, sample preparation, data analysis and method validation; and classical analytical methods that include gravimetric and volumetric techniques. The volumetric method will emphasize on acid-base, precipitation, complexation and redox titrations.

The course introduces students to Good Laboratory Practices in classical wet chemistry methods. Experiments are designed to complement the topics covered in Principles of Analytical Chemistry SSCC , which include gravimetric and volumetric techniques. The emphasis of this course is to expose the students to the fundamental principles and techniques of quantum chemistry in the description of atom and molecule in terms of electronic structure and properties.

This course is introduced by discussing wave particle behaviour of electron, Schrodingerwave equations and its applications to a particle in a box, harmonic oscillator, rigid rotor, hydrogen atom, and hydrogen like atoms. It continued further on the combination of atoms to form molecules; valencebond and molecular orbital theories; Huckel approximation; approximate techniques: This course teaches the students the principles of research methodology and information retrieval.

Topics include research philosophy and objectives, literature study and review, choosing and defining research problems and design, preparing and writing research proposals, technical report writing the elements of technical writing , types of technical report writing, dissertation writing, public speaking preparation and presentation and information retrieval search strategies. Presentation of assignment is also an important component in this course. This course introduces the basic principles, instrumentation and applications of separation methods commonly used in chemical analysis.

A general overview and classifications of common separation methods is first given followed by their basic principles of separation. Major separation methods and its applications discussed include extraction, chromatography and electrophoresis. This course introduces the application of computer methods in chemistry. Topics discussed include regression analysis, multivariate calibration, pattern recognition, experimental design and optimisation, handling of chemical structures, chemical databases, molecular modelling, and artificial intelligence.

Applications of these methods in data analysis, structural searching, prediction of properties and drug design are discussed. This course discusses the theory and application of infrared IR , nuclear magnetic resonance NMR , ultraviolet UV spectroscopies and mass spectrometry MS for structural determination of organic compounds.

In addition, elemental analysis for determination of molecular formula and index of hydrogen deficiency will be discussed. This course discusses the general principles of medicinal chemistry with emphasis on the molecular interaction of drugs with biological systems.

The functional groups commonly found in drugs are reviewed with respect to their nomenclature and chemical reactivity. The absorption and metabolism characteristics are then related to the physicochemical properties of these functional groups.

The theories and principles of drug-receptor interactions and drug design are presented, as well as the general principles of drug metabolism.

To illustrate current drug developments, this course will utilize examples from chemical biology, bioorganic chemistry and drug design. The research training enables the students to experience chemistry research in real world setting, whereby the equipment, instrumentation and work conducted are generally more advanced.

The students will be exposed to a different research environment and has the oppurtunity to interact with researchers in different fields. The students will be assessed based on the final report submitted to the faculty at the end of the training as well as the reports from both supervisors. This course is designed to provide students with an understanding of the principles and application of thermal analysis methods. Other thermal analysis methods discussed include microthermal analysis, thermomechanical analysis and dilatometry.

Discussions will also cover interpretation of thermograms and application of the thermal analysis methods. This course exposes students to solid state chemistry beginning with introduction to simple crystals structures, symmetry, lattices and units cells, crystalline solids, and lattice energy.

Following this, the main topic discussed include X-ray Diffraction and its use in solving single crystal structures; various preparative methods in solid states; bonding in solids states and electronic properties and electronic conductivity in simple metals, semiconductors and doped semiconductors; defects and non-stoichiometry; ionic conductivity in solids, solid electrolytes; non-stoichiometric compounds and electronic properties of non-stoichiometric oxides; application of physical techniques in characterization of inorganic solids; optical properties of solids; magnetic and dielectric properties of materials; phase diagram and its interpretation; relationship between structure, physicochemical and mechanical properties of materials including zeolites and related structures.

This course discusses the metabolism of biomolecules such as carbohydrates, lipids and proteins. Discussion includes catabolism and anabolism for each biomolecules.

Production of ATP from biomolecules based on Chemiosmotic theory will be discussed. Inborn errors of metabolism related to specific biomolecules will be highlighted. This is an introductory course on microscopic techniques that deals with the basic working principles and schematic diagram of construction of various microscopes, namely, light microscope, electron microscope, x-ray microscope, acoustic microscope, field ion microscope, and scanning probe microscope.

For each type of microscope, particular reference is given to the resolving power, sample preparation, and analysis of the micrograph. In general, this course will provide the students with necessary knowledge on the choice of microscope for study of materials. It comprises of chemical laboratory techniques such as glassware calibration, preparation and dilution of solutions, titration, separation, extraction, including data analysis and reporting.

Upon completion of the course, students should be able to apply appropriate general chemistry laboratory techniques, draw conclusions and present scientific data in a clear and logical manner. This course introduces the basic concepts of inorganic chemistry, focusing largely on structure, reactivity and periodicity of inorganic substances of the main group elements.

The course also teaches the systematic survey of the descriptive inorganic chemistry of the main group elements, including industrial applications and practical uses of important classes of inorganic compounds.

This course introduces the basic concepts and skills in inorganic chemistry practical. This course also exposes students to basic skill of handling chemicals and preparing solution. This course presents the fundamental concept and the application of chemical kinetics and electrochemistry. The chemical kinetics study includes rate and mechanism of reactions, orders of reactions, rate laws and the comparison of theories with experiments for simple gas reactions, reactions in solution, complex reactions, homogeneous catalysis, chain reactions and rapid reactions.

While electrochemistry includes the electrolyte conductivity, theory on conductivity, activity, transport numbers, electrochemical cells and electrode processes and kinetics. The emphasis of this subject is to expose the students to the fundamental concept and theory related to Laboratory Organization and Laboratory Design, Material and Chemical managements, Dangerous Instrumentations, Safety in Laboratory and Chemical Store, Safety Procedures and Documentations.

The subject will focus on the fundamental concepts of environmental studies and sustainability. Emphasis will be given on sustaining the ecosystem, biodiversity, natural resources and environmental quality. Awareness and practical application of green technology will also be discussed. This course introduces the fundamental concepts of natural products chemistry. The biosynthetic pathway of the secondary metabolites such as terpenes, flavonoids and alkaloids will be discussed.

Isolation, classification and structural identification of terpenes, flavonoids and alkaloids will be covered. Reaction and synthesis associated with these compounds will be further examined. This course provides an introduction to forensic science and the legal aspects. The roles of forensic scientist as crime scene investigator to laboratory analyst and finally as an expert witness in court are highlighted. Forensic analyses of paints, glass, hairs and fibres, fire debris, question document, drugs of abuse, blood, semen and saliva are covered in this course.

Upon completion, students should be able to develop and apply knowledge to describe the electrochemical corrosion processes and its prevention. Students should also be able to rationalize the importance of corrosion effect in industrial application and our lives. This course aims to give chemistry major students an understanding of the multidisciplinary nature of biotechnology. It includes understanding some of the basic principles of microbiology, biochemistry and engineering aspects of bioprocesses.

The course mainly focuses on industrial and environmental aspects of Biotechnology where chemist can play an important role.

Introduction to microbiology was first given to familiarize students with the terms commonly used in Biotechnology. Topics include classification of microorganisms; prokaryotic and eukaryotic cells; biomolecules, DNA as genetic material, bacterial growth and metabolism, microbial culture systems in bioreactors: Some insights into industrial biotechnology: While environmental biotechnology touches on bioremediation, sewage system and wastewater treatment processes and metal recovery.

Also a brief introduction on animal cloning and stem cells technology as a special interest topic. This course intended to give an overall introduction to the importance of materials and how chemistry controls its properties.

Types of materials include metals, semiconductors, superconductors, ceramics, glass, composites, polymers and nanomaterials. The different types of bonding exist in materials in terms of bonding such as ionic, covalent, metallic, van der Waals and H-bond are explained. The general properties of materials such as mechanical, electrical, optical and thermal will be discussed. The relationship between the structures of materials with respect to their physicochemical properties will be examined.

The synthesis, processing, fabrication and application of industrial materials are highlighted. Various characterization techniques of solid materials shall be discussed.

The course provides the concepts and principle of physical chemistry, starting with a brief discussion on gases, which include the properties and equation of state of ideal and real gas and continues with the principle of corresponding states.

The next topics emhasizes on Thermodynamics: Topics on the Chemical Equilibria will focus on chemical potentials and phase equilibria, which include phase rule and phase diagram of single component system. The final topic will cover Solutions: The experiments selected for the course illustrate concepts explored in the Chemical Thermodynamics lecture, enable students to test the relation of theories with experiments, learn experimental methods used by physical chemist, develop laboratory skills and the ability to work independently, learn how to effectively present scientific results and appreciate the limitations inherent in both theoretical treatments and experimental measurements.

This course discusses the fundamental concepts of functional groups in organic compounds. These include aliphatic and aromatic hydrocarbons, alcohols, phenols, organohalogen compounds, ethers, epoxides, aldehydes, ketones and carboxylic acids. In each topic, the students will be introduced to the structures of the functional groups and the nomenclatures common names and IUPAC names.

Physical properties, preparations, reactions and visual tests will also be discussed. Inter-conversion of the related functional groups and their reaction mechanisms are also included. This course is designed to discuss the basic principles involved in chemical industrial processes. It involves dimensional analysis, material and energy balances, basic unit operations, basic separation processes and process controll.

Dimension analysis stresses on the basic units, dimensions, conversions of units which is usually applied in scientific and engineering calculations. Material and energy balances discuss the fundamentals of material and energy balances calculations in non-reactive and reactive systems as well as recycle, by pass and purge on chemical process.

Basic unit operations and separation processes include type of reactors, heat exchanger, distillation, absorption and filtration processes. Process controll discuss the process flow, flow-diagram and automation on chemical industries. The industrial training gives the students the opportunity to acquire technical knowledge and practical skills not taught in classrooms. Through the industrial training, students will also have the opportunity to work with industrial workers and professionals, which will enable them to improve their communication skills and team working.

The students will be supervised by both faculty and industrystaff. Students are required to completetheexperimental work of the project identified during the Undergraduate Project I and document their findings. The students document the finding of their research in the form of project proceeding and final year project report.

The students will be assessed based on the report and proceeding submitted, projct presentation, attendance and laboratory work. The subject is designed to provide students with an understanding of the principles and procedures for the analysis of the chemical components of food. Introduction to food chemistry, food regulations, sample handling and preparation for data collection, reporting and analysis of data are included. Key analytical and separation techniques are discussed, including proximate analysis, classical techniques, and relevant modern instrumental techniques.

The course is intended to expose the students to organic chemicals in industries. The scope includes the organic chemicals used in foods, pharmaceuticals, cosmetics, agro-based industries, petroleum and polymers.

The synthesis and analysis of some selected chemicals will be discussed. The course will involve industrial chemicals such as flavours and fragrances; vitamins; antioxidants; dyes and colouring materials; common drugs including antibiotics, anti-inflammatory, anticancer, antihypertensive and antidepressant; soaps and detergents; insecticides, fungicides and pesticides.

Basic knowledge and uses of phytochemicals from herbs and spices will be introduced. In addition, general industrial chemicals for petroleum and polymers will be included. This course focuses on the principles of radioactivity and their applications in analytical chemistry including use of radiotracers in quantitative work. Error in techniques used will also be covered. Some of the analytical approaches discussed are isotope dilution analysis; radiometric titrations including selection of radiotracers.

Some techniques of using radiotracers such as liquid scintillation techniques, its principles and applications will be discussed. Other related techniques include radioimmunoassay, neutron activation analysis, radiocarbon dating and geological chronology, radiochromatography. Some industrial applications in industry will also be covered.. This course introduces students to the role of catalysts in chemical and biological processes. Kinetics and reaction mechanism of catalysed reactions and structural aspects of catalysts will be highlighted.

Emphasis is on the factors that influences catalysts reactivity in both homogeneous and heterogeneous catalysis. Different methods of preparation and characterization of catalytic material and the underlying principles with regard to industrial application of the catalyst will be discussed. Upon completion, students should be able to develop and apply knowledge in explaining the principles of catalysis in industrial processes, identify methods of preparing and characterizing catalysts such as supported metal catalysts, zeolites and metal oxides.

Mathematics is among the most fascinating of all intellectual disciplines, the purest of all art forms, and the most challenging of games.

It is a study of quantity, space, and change. Mathematicians seek out patterns, formulate new conjectures, and establish truth by rigorous deduction from appropriately chosen axioms, definitions and theorems. Mathematics is applied as an essential tool in many fields, including natural sciences, engineering, medicine, and the social sciences. Applied mathematics, the branch of mathematics concerned with application of mathematical knowledge to other fields, inspires and makes use of new mathematical discoveries and sometimes leads to the development of entirely new mathematical disciplines, such as statistics and operational research.

Industrial mathematics is one of the strands of applied mathematics aimed at industries. The study of mathematics is not only exciting, but important: This course aims at exposing students to this wonderful world of mathematics.

The course also enhances conceptual understanding in elementary mathematics such as indices, logarithm, radicals, trigonometry, vectors, complex numbers and mathematical induction. Upon completion, the students would have acquired some firm basic tools to pursue further mathematics.

This course strengthens principles of chemistry knowledge before proceeding to more specialized and higher levels chemistry subjects. The first part of this course exposes students to fundamentals of atoms and molecules and concepts which are known to be the main sources of chemical processes.

The second part of this course concentrates on stoichiometry and the relation between reacted species in reactions. The last part of this course strengthen student in term of fundamental knowledge of organic chemistry and introduces students the ideas of green chemistry concept. This course emphasis on working with data and the understanding of the different methods of designing and analyzing of the data.

Methods of designing experiments are intended for undergraduates with good algebra background and have been introduced to basic statistics. Students will also undergo training in using data analysis packages, including, but not limited to, the SPSS and Microsoft Excel.

This course introduces basic tools to derive and construct mathematical models using partial differential equations. Emphasis is given to the use of a conservation law. The methods of characteristics and separation of variables will be applied to solve the model equations. This course introduces the basic problems and techniques of decision making and comprises two major parts.

The first part covers basic principles and approaches in decision making. The second part explores the methods and applications of information that are used in making an optimal decision.

The course also covers differences between the classical frequencies approach and Bayesian approach in making decision, identify prior distributions and likelihood functions, and combine these two entities to obtain appropriate posterior distributions, which will then be combined with selected loss functions to obtain Bayesian estimators.

Concepts of conjugate distributions on prior and posterior distributions, important definitions in decision theory, proving admissibility and inadmissibility of a decision, process of making an optimal decision, utility and reward, and sensitivity analysis related to an optimal decision are also part of the course.

This course is an introduction to the theory and methods behind optimization under competing objectives involving single and also multiple decision makers. In this course, several approaches for finding the solution to the multi criteria decision problems will be explored, as well as the concepts of Pareto optimality and tradeoff curves to better understand the tradeoffs between objectives that occur in multi-objective decision making problems.

This course consists of two parts. The first part includes introduction to groups, types of groups, isomorphism between groups, composition of groups to form a direct product, and types of subgroups including normal subgroups and factor groups. The second part is a selected topic of Sylow Theorems and their applications.

The course is designed to provide students to learn time series modelling in theory and practice with emphasis on practical aspects of time series analysis. Methods are hierarchically introduced-starting with terminology and exploratory graphics, progressing to descriptive statistics, and ending with basic modelling procedures. The time series modelling will start with reviewing the fundamental concepts in regression, exponential smoothing and general class of Box Jenkins models.

This course discusses various scheduling classes namely single machine, parallel machine, flow shop, job shop and open shop. Approaches for modelling and solving scheduling problems of the mentioned scheduling classes will be discussed. Various performance measures will be considered in obtaining a good schedule. This course comprises of three parts. The first part is concerned with even, odd, periodic and orthogonal functions, its properties, Fourier series of periodic.

The second discuss about partial differential equations PDE. Linear and nonlinear first order equations. Classification of linear second order equations. The last part deals with complex variables. This part of the course introduces calculus of functions of a single complex variables. Topics covered include the algebra and geometry of complex numbers, complex differentiation and complex integration. This course discusses problem using numerical methods that involve systems of nonlinear equations and ordinary differential equations initial and boundary value problems.

This is an introduction to the theoretical and practical techniques in multivariate analysis. The theoretical links between multivariate techniques and corresponding univariate techniques, where appropriate is highlighted. Also, selected multivariate techniques are introduced. The course also covers relevant multivariate methods in R statistical programming software.

This course introduces the theory of inferential statistics. It is concerned with the frequentist approach to inference covering point and interval estimation of parameters and hypothesis testing. Properties of estimators such as unbiasedness and sufficiency are applied to estimators of parameters of various distributions.

Test of statistical hypotheses include certain best test, uniformly most powerful tests, likelihood ratio tests and chi-square tests. This course comprises of two parts; the first part covers topics on unconstrained optimisation such as one-dimensional and n-dimensional search methods, interpolation method and gradient methods.

The second part covers topics on constrained optimisation such as the Kuhn Tucker method, modified Hooke and Jeeves search method, complex method, penalty function methods, and the Sequential Unconstrained Minimization Technique SUMT. This course consists of two parts that is the theory of generalized linear model and the application of generalized linear model in regression model, one-factor analysis of variance and two-factor analysis of variance.

SPSS statistical package is used to apply generalized linear model to the above models. This course introduces sampling methods used in sample surveys. The students are given a comprehensive account of sampling theory for use in sample surveys and include illustrations of how the theory is applied in practice.

A prerequisite is familiarity with algebra, knowledge of probability for finite sample spaces and basic statistics. Topics include simple random sampling, sampling proportion and percentages, estimation of sample sizes, stratified random sampling, ratio estimators, systematic sampling, and cluster sampling. This course introduces the application and theoretical background of basic discrete-event simulation concepts and models. Topics included the basic queuing systems, random number generation, model development, model verification and validation and result analysis.

Students will be exposed to simulation model development using a simulation package. The course also helps the students to expand their critical thinking skills by experimenting with the simulated model for improvement. The course begins with an introduction to basic financial mathematics covering the computation of simple interest and discount rates, deriving the compound interest, and applications of different rates of interest in determining the present and future values of different types of annuities for different time periods.

The second part of the course concerns with classical quantitative finance i. An introduction to the subject of finance is presented. This consists of a collection of definitions and specifications concerning the financial markets in general. Then, the subject of derivatives and its concepts are introduced. Two main option pricings for pricing derivatives are examined: The Binomial option pricing and the Black-Scholes option pricing.

Physics is one of the most fundamental scientific disciplines with the main goal of understanding how the universe behaves. It covers a wide range of phenomena from the smallest sub-atomic particles to the largest galaxies, it is the scientific study of matter and energy and how they interact with each other.

Physicist is a scientist who studies or practices physics. Examples of careers in physics are scientists and researchers in various fields of scince and technology. The philosophy of physics is essentially a part of the philosophy of science. This course mainly discusses motion of a body or a system. Beginning with the basic and derived physical quantities and vector as mathematical tool, various types of motion such as linear, free-fall, projectile, circular, rotational and simple harmonic motions are described.

Other topics such as equilibrium, elasticity, gravitation and fluids mechanics illustrate the application of a body in motion under the influence of a force. The course examines the force of electromagnetism, which encompasses both electricity and magnetism.

It includes the exploration of some electromagnetic phenomena. It begins by examining the nature of electric charge and then a discussion of interaction of electric charges at rest. It then study about charges in motion particularly electric circuit. The principle of electromagnetic induction and how resistors, inductors and capacitors behave in ac circuits is discussed.

The understanding the electrical energy-conversion devices such as motors, generators and transformers are also discussed. Finally the study of the four fundamental equations that completely described both electricity and magnetism. The properties of the constituent amino acids, in the context of the cellular environment, largely determine spontaneous formation of the higher-level structure that is essential for protein function.

A protein may be made up of one polypeptide chain or many polypeptide chains subunits , the former is called monomer protein and the latter is referred to as polymer or oligomeric proteins. Myoglobin monomer and hemoglobin polymer of Hemoglobin protein ; ufq. Hemoglobin four subunits called globin subunits and in the centre it has a heme group ; www.

The dimer or polymer proteins may be made up of similar polypeptides or different polypeptides, so they are called homopolymers and heteropolymers. Such an association of more than one protein is referred to as quaternary structures. The binding forces responsible for such an association may be due to metal ions, hydrophobic interactions or ionic interactions.

Ribosome is made up of 70 or more proteins associated with rRNA in 3-D; www. Helix loop Helix, or beta-alpha beta, they are motifs. Several motifs join to generate a domain. Each of the domains has independent function s. Alpha helix, bundle of four helix, a globin fold; Parallel beta-sheets-alpha-beta barrel-Triose Phosphate Isomerase; Antiparallel sheets- immunoglobulins.

At gene level exons of a mRNA codes for a sequence of amino acids can generate either a motif or a domain depending upon the length of the exon sequence.

Many proteins do contain similar motifs and similar domains. Assume in a given genome there are twenty thousand protein coding genes. Each produces an mRNA consisting of 20 exons; now one can calculate the number of similar different domains by permutation- combinations. Motifs have structural and functional; a simple motif can be helix lop helix; two alpha helixes are joined by a simple loop ex. DNA binding motif and calcium binding motif. Three dominant helices form a parallel bundle against which the N-terminal helix packs at a right angle.

Two CH domains in tandem pack such that the C-terminal helix of the first domain connects the two domains to create a single compact fold. Zinc finger domain; www. Human Hair fiber; www. Histone octamers wrapped around by dsDNA; www. Globular proteins polypeptide chains which are folded into 3-D spherical structures are called globular proteins. Nearly and odd enzymatic proteins so far known are globular proteins.

Such proteins are soluble in water and some are buried in the lipid core of the membranes; which depends upon the kind of peripheral amino acid residues found on proteins, ex.

Hemoglobins, myoglobins, serum proteins are water soluble; Cytochrome oxidase, protein secretion proteins, etc. The globular proteins contain specific areas or sites at which they bind to specific substrates for enzymatic reactions. The intergrity of the 3-D shape is essential for their normal functions. Many globular proteins organize into fibrous proteins.

For example, a and B subunits of tubulins polymerize to form tubular microtubules. Similarly, the G action units polymerize into functional filament called F-actins. Such proteins are often called pseudo fibrous proteins. But polypeptide chains of a keratin and B collagen proteins are considered as true fibrous proteins. Human hairs are primarily made up of numerous a keratin helical polypeptides. Such helixes are intertwined with each other by disulphide bonds between helical chains.

All the chains in such structural fibers have NH2 or Carboxyl groups at the same ends. Basically, three such a keratin helical polypeptides are coiled to each other into a rope like structures called protofibrils.

Even such protofibrils associate to form a micro fibril. Many such micro fibrils join together into a macrofibril. A large number of such macrofibrils join together to form a super coiled structure called hair. Collagens are responsible for the strength of the ECM and form high tensile strength fibers and are prominent in tendons and ligaments.

Collagen fibers are bundles of collagen fibrils which are, in turn, bundles of collagen molecules which consist of three alpha chains of collagen polypeptides. Procollagen forms many types of tissue-specific collagens. Similarly, collagen is another super coiled muscle fibrous protein found in the tissues of higher vertebrates. The basic unit of collagen fibers is tropocollagen which is made up of three helical polypeptides twisted to each other.

Each tropocollagen is mm long and 1. Many such tropocollagen fibers are longitudinally arranged head to head to form long thick fibers. Many such fibers are longitudinally oriented to form muscle fibers called collagen fibers. Silk fibrions or fibrions secreted by silk moths, spiders and other insects are insoluble proteins but they are supple and flexible in nature.

Such fibers are different from a keratin fibers in their structure and flexibility. Keratins can be stretched to greater lengths, but silk fibrins cannot be stretched.

Bombax mori fibroin- Gly-ser-gly-ala-gly-Ala n; en. Water molecules are represented by blue dots. Silk fibroins are actually made up of polypeptide chains with beta confirmation, wherein the chain is extended into zig-zag rather than helical conformations.

Such zig zag fibers are oriented side by side parallel to each other and they are held to each other by interchain hydrogen bonds See Figure. That is the reason why silk fibers look like stretched pleated sheet structures.

The most significant feature of these proteins is the total absence of intra chain sulfhydril bonds and most of polypeptide chains are arranged parallel to each other.

Most of the cellular proteins fall into either into globular or fibrous types but some of the proteins found in both the animals and the plants rarely , contain another class of proteins which have both the features. Such proteins are called fibro globular proteins. Actin, Keratin and Microtubules ; www. Microtubules with motor proteins ; www. The best example to illustrate such structural combination is myosin.

It is made up of a head and a long tail. The tail consists of two long intertwined a helical polypeptides. On the contrary, the head consists of four polypeptide chains folded into globular structure; of which two are in continuity with tail fibers. The head proteins exhibit ATPase activity. The head and the tail protein of the myosin fibro globular proteins are interconnected by a region called hinge which exhibits random arrangement of the polypeptide chain. Largest Protein known today is: The chemical composition and the structure of proteins are so diverse, their functions also vary.

They are extra ordinary biomolecules endowed with a potentiality to provide structural stability to cell, determine the shape and perform myriads of functions. Though DNA act as the genetic material with all the information encoded within it, without functional protein, it is like a dummy tape without an instrument to play. No cellular component can be synthesized or processed without proteins. Their functions are pervasive; all biological activities are the functions of proteins.

However there are exceptions to this rule. There are many RNA molecules in their specific structural form can perform enzymatic reactions, where they can cleave a bond and make a bond.

Based on protein structure and functions a simple classification has been given below. The most specialized proteins are enzymes and they act as biological catalysts. So far or more enzymes have been identified from bacteria, fungi, animals and plants.

They are mainly responsible for biochemical activities of the cell. RuBisco protein complex-Octamer; www. Seed proteins like zein, gliedin etc are called storage proteins. They provide nutritional requirement of essential amino acids for animals. Such proteins are also stored in the white of eggs. Casein in milk and Ferritin in animal tissues.

Ferritin iron sequestering protein ; www. Proteins found in membranes, cytoskeletal fabric, capsids, collagen, elastin of muscles, mucoproteins of synovial fluids, keratin of hairs, nails, hoofs, borns, silk fibrions, spider webs, etc.

They provide mechanical support and strength to various structural components of the cellular tissues. Certain cellular components are transported from one region of the cell to the other or from one region of the body to the other. Specific proteins are responsible for the transportation of various cellular components.

Such proteins are called transport proteins. Microtubules and microtrabaculae transport sucrose in sieve tubes, microtubules and action filaments are involved in protoplasmic streaming. Hemoglobin, hemoeyanin and myoglobin transport oxygen in the blood of vertebrates and invertebrates. Serum albumin and B lipoproteins transport fatty acid components in the blood.

Iron binding proteins and ceruloplasmins transport iron and copper respectively. Elastin and fibrillins ; www. Flagillar proteins help in the movement of cells from one place to another.

Cytoskeletal fabric is responsible for the protoplasmic movement. Muscular proteins control mechanical movement of organs and the body. Most of the above said movements are due to the activity of contractile proteins like action and myosin. The DNA has encoded genetic information; to transfer the information proteins are required.

Helix lop Helix DNA binding protein ; www. Leucine zipper is a protein dimer formed between leucine residues in parallel oriented alpha helices, bound to DNA ; www. Antibodies are a class of serum proteins which act against the invasion of pathogenic bacteria, viruses or any other foreign substances.

They are highly specific to the antigens. Interferons induce antiviral proteins against the attack of certain viruses in mammalian dells. Thus, such proteins provide defensive mechanism against disease causing foreign agents. Fibrinogen and thrombin are another set of proteins, which prevent hemorrhage by blood clotting. Immunoglobulin proteins-general ; http: Certain pathogenic bacteria after infection release toxins which results in dehydration or food poisoning.

Snake venom is another class of proteins which can cause death in man. Ricin produced by castor seeds and gossip in from cotton can easily kills persons. Thus proteins not only act as saviors as in the case of antibodies, they can also act as killers. Animals produce certain proteins which control physiological activities, e.

They are synthesized and secreted by endocrinal glands. Insulin controls the blood sugar level; growth hormone controls the growth of the body. Thus many such hormones play important roles in the life cycle of animals. Further more some of the proteins control transcription and translation, thus they control gone expression and differentiation.

Even such proteins are called regulatory proteins. GAL-4 protein ; www. When proteins are heated or dissolved in certain solvents, their 3D structure, denatures and they become linear. This phenomenon is called denaturation; as a result, proteins lose their ability to perform their specific functions. On the other hand, the temperature of the said solution is brought back to the normal temperature, the sulfhydryl bonds are reformed and the 3-D shape is restored, so also its function.

Such a process is called renaturation. On the contrary, if the solution is heated to boiling temperature, proteins undergo irreversible destruction. When a solution containing proteins in their 3-D state are heated, to degree C, the sulfhydryl bonds break and polypeptides open out into straight helical structure; this is called denaturation.

And when the temperature brought to normal they fold back, it is called renaturation. The denaturation unfolding and renaturation refolding of a protein is depicted. The molecular weight of a protein depends upon the number and the kind of amino acid residues present in the chain. Added to this the number of sub-units present in a particular protein has to be taken into consideration for determining molecular weight of a protein complex.

The molecular weight of individual polypeptides or the total mol. Using these methods the mol. In olden days wine-making was an art. They used to prepare wine from different sources like fruits, barley and wheat by subjecting them to a process called fermentation. But they did not know what the actual mechanism of fermentation was. It was Louis Pasteur who demonstrated that fermentation requires living micro organisms like yeast cells. Buckner extracted a juice from yeasts, which was still capable of catalyzing the fermentation reactions.

Such catalytic components were earlier called, by Willy Kuhne as enzyme. Later, Sumner succeeded in isolating an enzyme called urease in pure crystalline form, since then a large number of enzymes have been isolated and identified.

Their chemical composition, structure, functions and kinetic mechanisms have been elucidated. In earlier days, nomenclature of enzymes was based on the substrate on which they acted ex. Sucrase on sucrose, lipase on lipids, protease on proteins, etc. As more and more number of enzymes was discovered in different labs all over the world, the trivial names gave rise to a lot of confusion.

In order to avoid confusion and ambiguity in giving names, an international society of enzymologists was established. Based on substrate and the kind of reaction they brought about, the enzymes were given names. In fact, naming and classification was done together. According to the international body of enzymologists, all enzymes are basically grouped into six classes of enzymes — such as oxido-reductases, transferases, hydrolases, isomerases, ligases and lyases; further sub groups have been identified.

Enzymes responsible for oxidation either by the addition of oxygen or removal of hydrogen or electrons are called oxidases. On the contrary, the enzymes which add hydrogen or electrons are termed as reductases.

Cytochrome oxidase, nitrate reductase, a -ketoglutamate dehydrogenase. Certain groups like amino groups, acyl groups, phosphates, etc can be transferred from one compound to another compound by specific transferase enzymes, ex. Aminotransferases, transcarboxylases, transhydrogenases, transacetylases etc. Catechol O-methyl transferase domain, http: The enzymes which by adding water molecules bring about breakdown of bonds are called hydrolases.

Majority of lysosomal enzymes are hydrolases of one or the other kind, e. Lipases, proteases, DNase, Ranse, Amylase, endonuclease etc. Pectin Lyase B; http: These enzymes add a group to compounds containing double bonds between carbon and carbon, carbon and nitrogen, carbon and oxygen, etc,.

Enzymes which are capable of transforming one isomer to another are called isomerases. They a re highly specific in their substrates and reactions, ex. Glucose 6-p isomerase converts glucose 6-p to fructose 6p. Phosphoglyceraldehyde can be converted to another isomer called dihydroxyacetone phosphate by gluoco-phospho glyceraldehyde isomerase. Triose phosphate Isomerase; http: Ligase enzymes bring about the bond formation between different molecules by removing a molecule of water.

In fact, their activities is in the opposite direction of hydrolyses. They bring about the synthesis of bigger compounds by the addition of simpler compounds. Such enzymes are also called synthetases, e. T7 DNA ligase; http: Almost all enzymes are made up of proteins as the major component.

In addition, some non-proteinaceous compounds like vitamins or inorganic ions are also bound to be the protein part of the enzyme. Such compounds are called co-enzymes.

They easily dissociate from the main enzyme. The apoenzyme and prosthetic groups can be separated by dialysis; where the prosthetic groups diffuse out of the membranous bag, but the bulky apoenzyme protein part is retained within the dyalytic membranes. The enzyme containing both apoenzyme and prosthetic group together is referred to as Holoenzyme. The main part of the enzyme is protein; it possesses a 3-D structural organization. The total surface area of the enzyme is very large, and it has specific sites at which the substrates bind to the enzyme.

The apoenzyme may be made up of a single protein or it may consist two or more monomers. Still their organization and association is very important for their specific function. However, some multiple enzyme systems, where two or more different enzymes are complexed together; and together they function. Such enzymes perform multi step reactions where intermediate products are retained on the enzymatic surface and only the final products are released from the surface of the multiple enzymes, ex.

Pyruvate dehydrogenase, ketogluterate dehydrogenase, Fatty acid synthetase, etc. The enzyme proteins are folded in such a way, they possess specific regions in the form of clefts or grooves of particular shape and dimensions. The surface area of such sites is always complementary to their substrates, so that the substrate and enzyme form a complex similar to that of lock and key association. Within such grooves or clefts, certain amino acids with specific R groups act as binding sites to which the substrates bind transitorily and exert forces to bring about reactions.

Hexokinase, the pacemaker of glycolysis; http: Some of the enzymes, besides possessing specific binding sites for substrates, contain other sites at which certain molecules bind and bring about conformational changes in the 3-D confirmation of the enzymatic protein.

Such bindings may activate an enzyme or inhabit the activity of the enzymes. Such enzymes are called allosteric enzymes. The components that bring about the activation or inactivation of allosteric enzymes are called allosteric affectors or effectors. The affecters block the activity and effectors activate the activity.

Multi-cellular organisms are made up of different organs containing specific tissues. Each of then perform a set of functions by producing specific enzymes. However, some of the enzymes synthesized within the cell are secreted to extra-cellular surfaces, such enzymes are called exoenzymes and those enzymes which are retained within the cell are called endoenzymes.

The enzymes present within a cell show a great range in their structures and functions. However, some of the enzymes are compartmentalized, so that each organ contains a group of enzymes which perform specific functions. For example, chloroplast contains enzymes responsible for photochemical and carbon pathways.

Nucleus possesses enzymes responsible for DNA replication, transcription, processing, etc. Likewise, cytosol contains enzymes for glycolysis, and many metabolic pathway enzymes and many others. Thus one can see intracellular compartmentalization of enzymes is for specific functions.

A large number of enzymes present in cells are continuously made irrespective of external or internal conditions. Such enzymes are called house keeping or constitutive enzymes. But under certain conditions, specific enzymes are synthesized de novo. Such enzymes are called induced enzymes. Enzymes are macromolecules and possess a large surface area with specific binding or acting sites. Enzymes act as biological catalysts.

This is determined by the turnover reactions. The total number of products produced by a given enzyme in a given time is called turnover number. Different enzymes exhibit different turnover rates.

Once the reaction is brought about, enzymes are ready for another sequence of reactions. If the concentration of substrates is more than the concentration of products, the enzyme favors forward reaction.

On the contrary, if the concentration of substrates is less than the concentration of products, the enzymes favor reverse reactions. However, not all enzymes are capable of bringing about reversible reactions and they exhibit unidirectional reactions. Trypsin and pepsin are proteolytic enzymes, but they cleave peptide bonds at specific amino acids, ex. Trypsin is specific to the carboxyl side of arginine or lysine. Pepsin is specific to amino acids of tyrosine or phenylalanine residue in the protein.

Such enzymes are called stereo specific enzymes, which are capable of transforming one isomer to another or vice versa. Enzymes being mainly made up of proteins, their 3-D organization depend upon S-S bonds.

Under normal temperatures such bonds are intact and perform normal functions but at very high temperatures, the S-S bonds break open and proteins get denatured and their function is impaired. Further more, the rate of reaction depends upon the temperature. As the rate of reaction depends upon the frequency of collision between the substrate and enzymes, the rate of movement of these reactants is controlled by the kinetic energy available in the system.

As enzymes are mainly made up of proteins, the electronic charge of the R-Groups found in amino acids depends upon the intracellular pH. Every enzyme has an optimal pH for its activity. Quite a number of enzymes are active at the range of pH 5. But certain enzymes like Trypsin and chymotrypsin are active at acidic pH On the contrary, Alkaline phosphotases are active at pH As pH of the cytoplasm determines the activity of functional groups found in enzymes, their activity is dependent on specific pH.

Normally substrates bind to enzymatic surface at specific sites, before catalytic action. But certain molecules other than substrates sometimes bind to active site or at some other site and bring about the inhibition of enzymatic activity. Such substances are called inhibitors, which may be competitive, non-competitive or un-competitive inhibitors.

Competitive inhibitors are those molecules, whose structural configuration is almost similar to that of actual substrates. As enzyme active sites recognize certain specific groups found in the substrate, any inhibitor molecule which possesses such groups identical to a substrate easily binds to active site. But the enzyme fails to bring about any catalytic reactions because of the internal structure of the inhibitors.

Thus competitive inhibitors, by binding to active sites prevent the binding of substrates to the enzymatic surface. Competitive inhibition could be reversed by the addition of excess amount of substrates.

For example, succinate, a substrate binds to its enzyme called succinate dehydrognase. If malonate, which has carboxyl groups similar to that succinate, is added, it easily recognizes the active sites in the enzyme and prevents the binding of real substrates.

Thus enzyme activity is inhibited. Certain organic or inorganic molecules inhibit enzymatic activity by distorting the 3-D surface of the protein or by blocking the active site non-competitively. The former kinds of inhibitors bind to a site of an enzyme other than active site and induce conformational change in the structure of proteins, thus making the enzyme inactive.

On the other hand, compounds like cyanide, rotenone, antimycin, etc bring to the active site of respiratory enzyme non-competitively and inhibit enzymatic activity. There are another class of compounds like Urea, Mercaptide compounds which break the S-S bonds and unfold the proteins and make it inactive. Lowers the Activation Energy: In living systems, molecules are under constant motion and exist at different energy states. Some may exist at higher energy state and some exist at may lower energy start.

Without the mediation of enzymes, substrates by themselves can react with each other by collision, provided the energy required is sufficiently high, at which point, molecules are in a transitory state.

The amount of energy required for a substrate to be at higher transitional state is referred to as activation energy. For example, sucrose breaks down spontaneously, if the activation energy available is of K.

But in the presence of enzyme invertase; it performs the same reaction with just K. Thus enzyme medicated catalysis requires less energy, because the binding of substrates to enzymes, which have a large surface, renders substrate molecules to be in a transitory state, because binding brings about stretching of the substrate bonds.

This greatly felicitates the reaction with minimum input of energy. Thus, enzymes economize the utilization of cellular energy and also make them efficient. Enzyme catalysis requires less energy, because the binding of substrates to enzymes, which have a large surface, renders substrate molecules to be in a transitory state, because binding brings about stretching of the substrate bonds.

Enzymes conserve energy during their course of reactions. An enzyme can exist in two or more different structural forms still perform the same functions.

Such enzymes are called isoenzymes. Such behavior is due to changes in the amino acid composition of enzymatic proteins, ex. Lactic dehydrogenase, it is a tetramer and it exists in five different forms; which are found in different organs. Such multiple forms of enzymes may be expressed at different stages of development. Electrophoretic methods have greatly helped in identifying such isoenzymes.

In recent years, studies on biosynthesis of macromolecules like polypeptides revealed that most of the proteins that are synthesized on mRNA template are larger than the functional proteins.

Such large inactive proteins are called precursor proteins or they may also exist as pre pro precursor proteins. Such proteins require enzymatic cleavage of certain part of the polypeptide chain for the activation of precursor proteins. Living organisms produce some inactive enzymes called zymogen granules, ex. Chymotrypsinogen, Trypsinogen, pepsinogen, etc. Chymotrypsinogen is activated into active Chymotrypsinogen by enzymatic cleavage of a peptide bond.

Similarly trypsinogens and pepsinogen are converted to active Trypsin and pepsins by enzymatic activation. Even insulin proteins are first synthesized as inactive precursor proteins, they are then made active by elimination of a particular segment of the protein chain.

Courtesy of Professor Stephan Strittmatter; http: Courtesy of Professor Joseph Wolenski. In recent years, various techniques like radioactive isotope labeling, spectrophotometric, immunoprecipitation techniques, etc.

Way back, Emil fisher proposed lock key model to explain the enzyme substrate reactions. However, this model has been slightly restructured to explain certain properties of enzymes. To going with the enzyme and substrate molecules collide with each other. If the collision brings their complementary surfaces together, the electronic forces operating upon the enzymes and substrate molecules, facilitate the binding of substrate to the active site located on the enzymatic surface.

The active site is always located in a cleft or a groove within the enzyme. Three kinds of reactions, intermolecular, intramolecular, and enzyme-catalysed , above diagram; http: The binding, is mostly due to non-covalent forces like hydrogen bonding and it is a transitory phenomenon.

The R groups in amino acid residues found in the active site exert many forces like Vander wall forces, hydrogen bonding, ionic interactions, or hydrophobic interactions.

This figure illustrates simple feedback inhibition. If the end product of the metabolic pathway E accumulates it inhibits the activity of the first enzyme in the pathway. Examples can be found in amino acid biosynthesis. The enzyme affected will be an allosteric enzyme. Control in a branched pathway.

In this case both end products are required to b bound to effect inhibition two different allosteric sites. Other strategies that are found: Feedback Inhibition ; http: Enzymes Advance Level; http: Such changes in enzyme topography by substrate were first proposed by Koshland Jr. The proper binding of the substrate to the enzyme renders the substrate to be in a transitional state.

The electronic forces operating in the region of active site bring about the reaction either in making of a bond or breaking off a bond or involving in the transfer of a group. The reorientation of bonds within a substrate molecule, brings about and change in the configuration, hence it becomes a product.

As products are in a stable form, they are repelled and released from the surface of the enzyme and make the enzyme free for another cycle of reactions. In the said mechanism, a single substrate binds to a single enzyme and the products produced may be one or two.

But there are many enzymatic reactions, where two substrates are involved to produce one or two products. In such cases the mechanism is slightly different.

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