Biocatalysis.pptx

Biocatalysis for M.Pharm 2nd semester

1. Presented by- Name- Jubair Sikdar Roll no-04 M. Pharm 2 nd semester Department of Pharmaceutical Chemistry NETES Institute of Pharmaceutical Sciences, Mirza BIOCATALYSIS

2. CONTENTS Introduction of Biocatalysis . Factors affecting the catalytic activity of enzymes Types of Biocatalyst Introducation of Enzyme Immobilization Application of Enzyme Immobilization

3. Introduction Biocatalysis refers to the use of living (biological) systems or their parts to speed up chemical reactions. In biocatalytic processes, natural catalysts, such as enzymes, perform chemical transformations on organic compounds. Utilizing natural or modified enzymes to perform organic synthesis is termed chemoenzymatic synthesis; the reactions performed by the enzyme are classified as chemoenzymatic reactions.

4. Factors affecting the catalytic activity of enzymes Enzyme Concentration : Product concentration increases with the increase of enzyme concentration. Substrate Concentration : The amount of enzyme is kept constant and the substrate concentration is then gradually increased, the reaction velocity will increase until reach maximum. Effect of inhibitors on Enzyme Activity : Enzyme inhibitors are substances which alter the catalytic action of the enzyme . Temperature : Enzyme catalysed reaction increases as the temperature is raised .

5. Effects of pH : The pH at which the enzyme is most active is known as optimal pH. Types of Biocatalyst Oxidoreductases: C atalyze oxidation/reduction reactions. For example, alcohol dehydrogenase converts primary alcohols to aldehydes .

6. Transferases: Transfer a functional group. alanine aminotransferase shuffles the alpha-amino group between alanine and aspartate . Hydrolases: C atalyze the hydrolysis of various bonds. For example, phosphatases break the oxygen-phosphorus bond of phosphate esters.

7. Lyases : Formation or removal of a double bond with group transfer . For example: Dehydratases remove water, as in fumarase (fumarate hydratase). Isomerases: C atalyze isomerization changes within a single molecule(Rearrangements ). For example, triose phosphate isomerase, carry out these rearrangements

8. Kinase : This enzyme in the body attaches a phosphate group to a high energy bond. It is a very important enzyme required for ATP production and activation of certain re-enzymes .

9. Enzyme Immobilization: Enzyme immobilization may be defined as a process of confining the enzyme molecules to a solid support over which a substrate is passed and converted to products . Immobilized Enzyme: An immobilized enzyme is one whose movement in space has been restricted either completely or to a small limited region . Why Immobilize Enzyme : Protection from degradation and deactivation. Re-use of enzymes for many reaction cycles, lowering the total production cost of enzyme mediated reactions. Ability to stop the reaction rapidly by removing the enzyme from the reaction solution . Enhanced stability .

10. Easy separation of the enzyme from the product . Product is not contaminated with the enzyme . Applications: Antibiotics Production: Immobilized enzymes are used to produce 6-aminopenicillin acid, penicillin, cephalosporin . Steroid Production: Synthesis of hydrocortisone and prednisolone. Amino Acid Production: Immobilized Amino acid acylase is used to resolute DL amino acid. the production of L-aspartic acid, L- tryptophan and L-alanine, L-DOPA (B- tyrosinase )

11. Acids Production : Acetic acid, Citric acid, L-Malic acid, 2-ketogluconicacid and 12-ketochenodeoxycholic acid .

12. REFERENCES Rajesh G. and Sujitha P: Pharmaceutical Biotechnology, Pee Vee Publication, Page:3-9 Geore M.W. and Chi- Hueng W. (1983), Enzyme as Catalysts in organic synthesis, Aldrichimiea Acta 16(2), 27-34. Biocatalysis for Organic Synthesis-https ://www.researchgate.net/publication/347973497

13. OPEN TO DISCUSSION

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