FE 533

Enzym Characterization and Kinetics

  Instructor:      Prof. Dr. Ahmet Yemenicioðlu

                        Food Engineering Department

Phone: (232) 7506292

e-mail: ahmetyemenicioglu[at]iyte.edu.tr

    

Prerequisite(s): Non

 Objective of the course:

Objective of the course is to teach structures, reaction mechanisms and kinetics of enzymes.  The course provides detailed information about enzymes and prepares students to overcome major problems faced during enzyme studies with most appropriate and practical methods.   

 Reference Books:

Segel, I.H. (1976). Biochemical Calculations. New York, John Wiley and Sons.

 Course Outline

1.  Proteins

   1.1.Amino acids

   1.2. Charges of proteins

   1.3. Hydrophobicity of proteins and folding 

2. Structure of proteins

   2.1.Primary structure

   2.2. Secondary structures

   2.3. Tertiary structure

   2.4. Quaternary structure

   2.5. Loop regions and domain structures 

3. Molecular weights of proteins 

4. Enzymes

   4.1. General information about catalysts

   4.2. Active sites, coenzymes and mechanisms of enzymes

   4.3. Specificity of enzymes

   4.4. Classification of enzymes 

5. Enzyme assays

   5.1. Calculation and expression of enzyme activity

   5.2. Spectrophotometric assays

   5.3. Electrochemical assays

   5.4. Type of enzyme assays 

6. Enzyme kinetics

   6.1. Rapid equilibrium approach

   6.2. Steady-state approach

   6.3. Methods of plotting enzyme kinetics data

   6.4. Inhibition kinetics

      6.4.1.Competitive inhibiton

      6.4.2.Uncompetitive inhibition

      6.4.3.Noncompetitive inhibition

      6.4.4. Irreversible inhibition

      6.4.5. Mixed type inhibition

   6.5. Optimum temperature

   6.6. Optimum pH and pH stability

   6.7. Temperature stability

      6.7.1. Thermal inactivation curves

      6.7.2. Decimal reduction curves

      6.7.3. Temperature profiles  

Grading:

midterm examination: 30 %

homework assignments: 10 %

final examination: 60 %