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Presented by-
Name- Jubair Sikdar
Roll no-04
M. Pharm 2nd semester
Department of Pharmaceutical Chemistry
NETES Institute of Pharmaceutical Sciences, Mirza
BIOCATALYSIS
CONTENTS
Introduction of Biocatalysis.
Factors affecting the catalytic activity of enzymes
Types of Biocatalyst
Introducation of Enzyme Immobilization
Application of Enzyme Immobilization
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.
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.
• Effects of pH: The pH at which the enzyme is most active is known as
optimal pH.
Types of Biocatalyst
Oxidoreductases: Catalyze oxidation/reduction reactions.
For example, alcohol dehydrogenase converts primary alcohols to
aldehydes.
• Transferases: Transfer a functional group. alanine aminotransferase
shuffles the alpha-amino group between alanine and aspartate.
• Hydrolases: Catalyze the hydrolysis of various bonds. For example,
phosphatases break the oxygen-phosphorus bond of phosphate esters.
Lyases: Formation or removal of a double bond with group transfer. For
example: Dehydratases remove water, as in fumarase (fumarate
hydratase).
Isomerases: Catalyze isomerization changes within a single
molecule(Rearrangements). For example, triose phosphate isomerase, carry
out these rearrangements
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.
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.
• 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)
Acids Production :
Acetic acid, Citric acid, L-Malic acid, 2-ketogluconicacid and 12-
ketochenodeoxycholic acid.
REFERENCES
1. Rajesh G. and Sujitha P: Pharmaceutical Biotechnology, Pee Vee
Publication, Page:3-9
2. Geore M.W. and Chi-Hueng W. (1983), Enzyme as Catalysts in organic
synthesis, Aldrichimiea Acta 16(2), 27-34.
3. Biocatalysis for Organic Synthesis-
https://www.researchgate.net/publication/347973497
OPEN TO DISCUSSION
THANK YOU

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Biocatalysis.pptx

  • 1. Presented by- Name- Jubair Sikdar Roll no-04 M. Pharm 2nd 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: Catalyze 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: Catalyze 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: Catalyze 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 1. Rajesh G. and Sujitha P: Pharmaceutical Biotechnology, Pee Vee Publication, Page:3-9 2. Geore M.W. and Chi-Hueng W. (1983), Enzyme as Catalysts in organic synthesis, Aldrichimiea Acta 16(2), 27-34. 3. Biocatalysis for Organic Synthesis- https://www.researchgate.net/publication/347973497