14BBI33 - Enzymology
Course specification | ||||
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Course title | Enzymology | |||
Acronym | 14BBI33 | |||
Study programme | Biochemical Engineering and Biotechnology | |||
Module | ||||
Lecturer (for classes) | ||||
Lecturer/Associate (for practice) | ||||
Lecturer/Associate (for OTC) | ||||
ESPB | 5.0 | Status | ||
Condition | Облик условљености | |||
The goal | The aim of the course is to give a fundamental understanding of enzyme structure, function, basic principles of enzyme catalysis, mechanisms and kinetics of enzyme reactions focusing on mechanisms of inhibition, activation and regulation of enzyme activity. The aim of the course is also to enable students to master basic methods for the determination of enzyme activities and to provide knowledge about specific enzyme representatives relevant for industry. | |||
The outcome | After passing the course the student will gain basic knowledge about enzymes as biocatalysts as well as about basic principles of biocatalysis. Thus, the students become capable to work in the biotechnology sector taking account that the enzymatic catalysis is the basis of a number of biotechnological processes.In addition, they will learn basic techniques in the analysis of enzyme kinetics, mechanisms of enzyme inhibition and activation. After the course, the students will be able to describe the mechanisms and kinetics of enzyme actions, generate kinetic data, analyse kinetic data, and give appropriate interpretations. | |||
Contents | ||||
Contents of lectures | • Introduction to Enzymology (brief history of enzymology, Terms and definition in enzymology); • Nomenclature/Classification of enzymes; • Chemical nature of enzymes, structure and synthesis of enzymes; • Coenzymes and Cofactors; • Basic properties of enzymes: activity, specificity and stability (enzyme assay techniques, enzyme units, type of enzyme specificity, stability and denaturation of enzymes with practical work); • Catalytic principles and reaction mechanisms of enzymes (The theory of catalysis; selected examples of enzyme mechanisms: catalytic mechanism of enzymes without cofactors: serine proteases, lysozyme, ribonuclease A, mechanisms of metalloenzymes action: carboxypeptidase A, amylase); • Enzyme kinetics with calculations; • Enzyme inhibition and activation with calculations; • Regulation of enzyme activity: Allosteric regulation and cooperativity. Examples of allosteric enzymes and their modes of action; • Examples of specific enzymes relevant in industry and their properties. | |||
Contents of exercises | Practical covers calculation from enzyme kinetics. The content of Lab exercises covers basic determinations in enzyme kinetics, measurement and expression of enzyme activity (lipases, proteases), the investigation of the effect of temperature on activity of protease from Bacillus sp., determination of optimal pH for a selected enzyme (papain), determination of peroxidase activity in horseradish. | |||
Literature | ||||
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Number of hours per week during the semester/trimester/year | ||||
Lectures | Exercises | OTC | Study and Research | Other classes |
2 | 1 | 1 | ||
Methods of teaching | The course consists of a combined theoretical part (lectures and theoretical exercises) and practical laboratory work with traditional and new advanced methods of analyses used in work with enzymes.Lectures in the classroom (using computer and video beam, overhead projector and blackboard). Computational exercises from the practical part solved using licensed MS Office and enyzme kinetic software packages on PCs. | |||
Knowledge score (maximum points 100) | ||||
Pre obligations | Points | Final exam | Points | |
Activites during lectures | Test paper | 40 | ||
Practical lessons | 20 | Oral examination | ||
Projects | ||||
Colloquia | 40 | |||
Seminars |