Biological Catalyst.pptx

BIOLOGICAL CATALYSIS

1. Biological Catalyst Dr.Gurumeet C Wadhawa ,Assistant Professor, Department of Chemistry. Rayat Shikshan sansthas Veer Wajekar ASC College,Phunde,Uran

2. Introduction ▪ A catalyst is a substance which alters to promote the reaction, and a substance especially an enzyme, that initiates or modifies the rate of a chemical reaction in a living body is termed as biocatalyst. ▪ They are enzymes or microbes that initiate or accelerate chemical reactions

3. ENZYMES: • Enzymes are chemical substances which are mostly proteins . • Enzymes catalyze nearly all the biochemical reactions in the living cells. • They have unique three dimensional shapes that fits the shape of reactants • Enzymes are typically derived from plants, micro-organisms (yeast , bacteria or fungi) or animal tissue (e.g. protease from pancreas).

4. Production Of Enzyme • Commercial sources of enzymes are obtained from three primary sources, i.e. animal tissue , plants and microbes. • These naturally occurring enzymes are quite often not readily available in sufficient quantities for food applications or industrial use. • However, by isolating microbial strains that produce the desired enzyme and optimizing the conditions for growth, commercial quantities can be obtained.

5. Production Of Enzyme(Cont.) • This artificial method of producing enzyme was earlier known as Fermentation. • Today, this fermentation process is carried out in a contained vessel. Once fermentation is completed, the microorganisms are destroyed; the enzymes are isolated, and further processed for commercial use. • Enzyme manufacturers produce enzymes in accordance with all applicable governmental regulations, including the appropriate federal agencies such as FDA(Food & Drug Administration, Chemical industries, research laboratories)

6. Types of Biocatalyst • Oxidoreductases : catalyze oxidation/reduction reactions. For example, alcohol dehydrogenase converts primary alcohols to aldehydes. In this reaction, ethanol is converted to acetaldehyde, and the cofactor, NAD, is converted to NADH. In other words, ethanol is oxidized, and NAD is reduced. • Transferases : transfer a functional group. alanine aminotransferase shuffles the alpha - amino group between alanine and aspartate.

7. Types of Biocatalyst(Cont.) • 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).

8. Types of Biocatalyst(Cont.) • Isomerases: catalyze isomerization changes within a single molecule(Rearrangements) . For example, triose phosphate isomerase, carry out these rearrangements. • Ligases: removing the elements of water from two functional groups to form a single bond.

9. Types of Biocatalyst(Cont.) • 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 enzymes.

10. Some Important Enzymes of Human Body Digestive Enzymes Digestive enzymes are secreted by the body that helps in digestion of food. The names of enzymes that help in digestion are: Amylase: This enzyme helps in breaking down carbohydrates. It is found in saliva, pancreas and intestinal juices. Proteases: It helps in digestion of proteins. It is present in the stomach, pancreatic and intestinal juices. Lipases: Lipases assist in digestion of fats. It is seen in the stomach, pancreatic juice and food fats.

11. Reaction for breakdown of Carbohydrates , Protein and Fat

12. Factor affecting catalytic activity of enzyme 1.Enzyme Concentration: Product Concentration increases with the increase of enzyme concentration.

13. Factor affecting catalytic activity of enzyme 2.Substrate Concentration: It has been shown experimentally that if the amount of the enzyme is kept constant and the substrate concentration is then gradually increased, the reaction velocity will increase until it reaches a maximum. After this point, increases in substrate concentration will not increase the velocity (delta A/delta T). This is represented graphically in Figure .

14. Factor affecting catalytic activity of enzyme 3.Effects of Inhibitors on Enzyme Activity: Enzyme inhibitors are substances which alter the catalytic action of the enzyme and consequently slow down, or in some cases, stop catalysis. There are three common types of enzyme inhibition - competitive, non-competitive and substrate inhibition.

15. Factor affecting catalytic activity of enzyme 4. Temperature Effects: Like most chemical reactions, the rate of an enzyme-catalyzed reaction increases as the temperature is raised. A ten degree Centigrade rise in temperature will increase the activity of most enzymes by 50 to 100%. Variations in reaction temperature as small as 1 or 2 degrees may introduce changes of 10 to 20% in the results.

16. Factor affecting catalytic activity of enzyme 5.Effects of pH: Enzymes are affected by changes in pH. The most favorable pH value - the point where the enzyme is most active - is known as the optimum pH. This is graphically illustrated in Figure.

17. DNA replication • DNA replication is a biological process that occurs in all living organisms . • Biocatalysts are the most important aspect in molecular biology(DNA replication, cloning) e.g. Polymerases (to polymerize), Restrictases(to cut the DNA strands) ,DNA ligases( to bind the DNA strands).

18. Application in Medical Field. 1.Diagnostic Purpose 2.Therapeutic purpose

19. Industrial Application of Enzyme Biocatalysis: • Enzymes are the most proficient catalysts, offering much more competitive processes compared to chemical catalysts. • The number of industrial applications for enzymes has exploded in recent years, mainly owing to advances in protein engineering technology and environmental and economic necessities.

20. Biocatalysts in industrial biotechnology • Fine and bulk chemical industries: Enzymes provide a more powerful way of producing enantiomerical pure compounds mainly through high chemoselectivity , regioselectivity , and streoselectivity . Some examples showing the contribution of biocatalysis to fine and bulk chemical fields are described here.

21. Examples:

22. Pharmaceutical industry • The pharmaceutical substances have become increasingly complex, and public and environmental quests for green technologies have increased. Therefore, the industry is seeking low-cost, safer, and greener biocatalytic processes as alternatives to traditional chemical catalysis • Specific reactions that can be replaced with biocalaysis have been identified in the synthesis of pharmaceuticals, including chiral amine synthesis, stereo and regio-specific hydroxylation of complex molecules, and other redox reactions.

23. Examples:

24. Food industry • most uses of biocatalysis have focused on hydrolytic reactions for debranching, improving the solubility, and clarification. • A recent trend in the food industry is to develop functional foods such as prebiotics, low-calorie sweeteners, and rare sugars.

25. EXAMPLES

26. Cosmetic industry • Recently,the cosmetic industry has faced a challenge because of increasing consumer demands for natural and eco-friendly cosmetics. • Arbutin is the most common skin-lightener, and is known to inhibit melanogenesis without causing melano-cytotoxicity • As an enzymatic approach to producing arbutin, various enzymes have been used, including α -amylase, α -glucosidase, transglucosidase, sucrose phosphorylase, and dextransucrase

27. Textile industry • For the development of cleaner processes, the use of enzymes is rapidly growing. Typical examples include the staining of jeans using cellulase from Trichoderma viride , and a bio-carbonization process in the case of wool . • Cellulase and protease are used in the polishing step for clear dyeing, the improvement of color and surface vividness, and resistance to wrinkles.

28. Demerits of Biocatalysts: • Enzymes require narrow operation parameters. • Enzymes display their highest catalytic activity in water. • Enzymes may cause allergies. • Often low specific activity. • Instability at extreme temperatures and pH values. • Availability for selected reactions only - long development time for new enzymes.

29. Possibilities • Over the past decades, enzyme-based processes have continuously substituted traditional chemical processes in many areas, especially fine chemical and pharmaceutical industries. Owing to the development of new technologies in enzyme engineering as well as economic pressure and public concern about environmental pollution, such replacement will be more accelerated. • Therefore, it would be a great chance for researchers to explore new applications and technologies in enzyme engineering. • Current trend in enzyme engineering based on the focused-directed evolution in conjunction with computational methods will continue and even accelerate.

30. References: •BIBLIOGRAPHY: Outlines of Biochemistry- Eric Conn, Paul Stumf WEBLIOGRAPHY: •http://www.lsbu.ac.uk •http://www.worldofteaching.com •http://www.enzymes.me.uk •http://www.enzymetechnicalassoc.org •http://www.media.wiley.com •http://www.sc.ehu.es •https://bodytomy.com/enzymes-in-body •https://www.cliffsnotes.com/study-guides/biology/biochemistry-i/enzymes/six-types-of-enzyme-catalysts •Tanja Gulder, Baran Group Meeting 07/11/2009: http://www.scripps.edu/baran/images/grpmtgpdf/Gulder_Jul_09.pdf •Choi J-M, et al, Industrial applications of enzyme biocatalysis: Current status and future aspects, Biotechnol Adv (2015), http://dx.doi.org/10.1016/j.biotechadv.2015.02.014 •Bennett, T. P., and Frieden, E.: Modern Topics in Biochemistry, pg. 43-45, Macmillan, London (1969). •Holum, J.: Elements of General and Biological Chemistry , 2nd ed., 377, Wiley, NY (1968). •Martinek, R.: Practical Clinical Enzymology: J. Am. Med. Tech., 31, 162 (1969). •Harrow, B., and Mazur, A.: Textbook of Biochemistry, 109, Saunders, Philadelphia (1958). •Pfeiffer, J.: Enzymes, the Physics and Chemistry of Life , pg 171-173, Simon and Schuster, NY (1954)

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