Enzymes use of exogeneous enzymes
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This document discusses enzymes as biocatalysts and the use of exogenous enzymes in food processing. It defines enzymes as proteins that act as catalysts to speed up biochemical reactions. The document outlines the mechanisms of enzymatic catalysis and factors that affect enzyme activity, such as temperature, pH, and substrate concentration. It describes the use of carbohydrate-transforming enzymes like amylases and lipases in food applications including starch hydrolysis, bakery, brewing, and flavour generation. The document also discusses the Michaelis-Menten equation and models of enzyme-substrate interaction.
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Enzyme structure, classification _ and _mechanism of action _ _
Enzymes are proteins that catalyze chemical reactions without being consumed in the process. They speed up reactions by lowering the activation energy needed. Enzymes contain an active site that substrates fit into. The enzyme-substrate complex undergoes changes that reduce activation energy. Environmental factors like temperature and pH can impact enzyme activity. Cofactors like vitamins are sometimes required for activity. Inhibitors can bind enzymes and block their activity. Enzymes are classified based on the type of reaction they catalyze.
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Enzymes are biological catalysts that speed up biochemical reactions without being consumed. They achieve this by lowering the activation energy of reactions. Hydrolases are a class of enzymes that catalyze hydrolytic reactions by adding water across bonds to break them down. One important hydrolase is human factor Xa, which promotes blood coagulation as part of the prothrombinase complex. Factor Xa can be inhibited by drugs like rivaroxaban, which selectively and directly inhibits both free and protein-bound factor Xa to interrupt the coagulation cascade and inhibit thrombin formation.
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Enzymes are biological catalysts that speed up reactions by lowering their activation energy. They have an active site that binds to specific substrate molecules. The rate of enzymatic reactions is affected by temperature, pH, and substrate concentration. Temperature and pH can cause enzymes to denature and lose their structure and function. Immobilized enzymes are used widely in industry, such as lactase to produce lactose-free milk for those who are lactose intolerant. Students should design experiments to test how temperature, pH, and substrate concentration impact enzyme activity rates.
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Enzymes are biological catalysts that speed up chemical reactions without being changed themselves. They are globular proteins that contain an active site where substrates bind and reactions occur. Enzymes lower the activation energy of reactions, allowing reactions to proceed more quickly. The lock-and-key and induced fit hypotheses describe how enzymes and substrates interact. An enzyme's activity can be affected by factors like temperature, pH, substrate and enzyme concentration. Enzymes can be immobilized to increase stability and allow continuous reaction processes. Common immobilization methods include cross-linking and adsorption.
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The document discusses various topics related to enzymes, including:
1. The classification system for enzymes known as EC numbers which divides enzymes into six main groups based on reaction type.
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- Enzymes work by lowering the activation energy of reactions, allowing products to form faster and reactions to reach equilibrium more quickly.
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Enzymes are biological catalysts that speed up chemical reactions in cells. They are proteins with an active site that binds to a specific substrate molecule. The enzyme-substrate complex undergoes a reaction, producing products. Each enzyme only works on one substrate. Reaction rates are affected by temperature and pH, with an optimum level. Above or below this, the enzyme denatures and loses function. Enzymes help drive many reactions in living things and industrial processes like breaking down stains or lactose.
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Enzymes are protein catalysts found in cells and tissues. They are responsible for chemical reactions in the body and can be detected in serum to diagnose diseases. Increased enzyme levels in serum may indicate tissue damage or certain disease states. Common enzymes measured include alkaline phosphatase, acid phosphatase, amylase, lipase, SGPT and SGOT which can help diagnose diseases of the bones, prostate, pancreas and liver. Enzymes function as biological catalysts by lowering the activation energy of reactions and increasing their rates without being consumed in the process. They are highly specific and their activity can be affected by factors like pH, temperature, substrate and inhibitor concentrations.
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تطبيقات الانزيمات فى التصنيع الغذائى
Enzymes have many applications in food processing. Examples include:
1. Glucose oxidase and catalase are used to remove oxygen and glucose from foods to prevent browning and extend shelf life.
2. Amylases are used in brewing and baking to break down starches.
3. Proteinases or peptidases are used in cheese production, meat tenderizing, and improving dough properties.
4. Immobilized enzymes can be reused, making them more economical for continuous processes.
IMMOBILIZATION OF ENZYMES
ENZYMES are large biological molecules (catalysts) that speed up rate of chemical reaction without being used up in the reaction. (responsible for the thousands of chemical interconversions that sustain life).
IMMOBILIZATION means that the biocatalysts are limited in moving due to chemically or physically treatment.
Immobilised enzymes
Industrial enzymes are often immobilized to improve their stability and allow for continuous reuse. There are two main types of reactor systems used - stirred tank reactors and continuous flow reactors. Stirred tank reactors involve stirring the immobilized enzyme with substrate in a batch process. Continuous flow reactors pass substrate through a column of immobilized enzyme in a continuous process. Immobilization can shift pH and temperature optima and improve stability. Important industrial applications of immobilized enzymes include high fructose corn syrup production using glucose isomerase and hydrolysis of lactose using beta-galactosidase.
Immobilization of enzymes
Enzyme immobilization is defined as confining the enzyme molecules to a distinct phase from the one in which the substrates and the products are present.
It is achieved by fixing the enzyme molecules to or within some suitable material.
Enzyme Function and Properties.pptx
An enzyme is a protein catalyst that makes chemical changes in biological systems. Various categories are used in baked goods, beverages, dairy, beer, glucose syrups, starch and other food products.1
In bakery systems, enzymes act as:
Dough conditioners
Fermentation enhancers
Anti-staling agents
This enables bakers to remove undesirable additives and make clean label baked goods.
Origin
Enzymes are naturally present in many living organisms such as animals, plants, bacteria and fungi. There, they participate in metabolic processes. Also, they can be found in food materials such as cereal flours, fruits and vegetables
Enzyme immobilization
Enzyme immobilization involves restricting the movement of enzymes by confining them to a solid support. This allows for repeated use of enzymes, enhanced stability, and easy separation of products. Common immobilization methods include physical adsorption, covalent bonding, cross-linking, and entrapment. Immobilized enzymes have various applications, such as isomerization of glucose to fructose using immobilized glucose isomerase, and use of immobilized urease in compact artificial kidneys. Immobilization provides benefits like recyclability and cost-efficiency compared to free enzymes.
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dtubbenhauer@gmail.com
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Enzymes use of exogeneous enzymes
- 1. ENZYMES AS BIOCATALYSTS & USE OF EXOGENEOUS ENZYMES( CARBOHYDRATE AND LIPID-TRANSFOMING ENZYMES) AVNEET KAUR 317006 FSQM
- 2. ENZYMES Proteins functioning as catalysts that speed up reactions by lowering the activation energy. Has important traits: are proteins are catalysts exhibit selectivity towards substrates. Enzymes are specific. Enzymes provide a specific environment within which a given reaction is energetically more favorable.
- 3. MECHANISMS OF ENZYMATIC CATALYSIS Substrate is changed into product via high energy transition state. E + S ES ES E + P
- 4. Active sites: clefts or grooves, composed of amino acids from different parts of the polypeptide . Co-factor: non protein molecule which carries out chemical reactions that can not be performed by standard 20 amino acids. Substrate: reactant in biochemical reaction. Inhibitors: decrease the rate of enzyme-catalyzed reactions. Can be competitive(Structurally similar inhibitor and substrate bind to the same site) or non- competitive(bind non-covalently and reversibly at the sites other than the active site).
- 6. MODELS OF ENZYME –SUBSTRATE INTERACTION
- 7. FACTORS AFFECTING ACTIVITY Temperature Enzyme concentration Surface area Pressure Substrate concentration pH
- 8. EXOGENEOUS ENZYMES Enzymes which are present in raw, uncooked food are called food enzymes to indicate where they come from: the food itself. Uses: • glucose, HFCS production of food commodities • beer stabilization, meat tenderization modification of components • cheese ripening, juice extraction, faster dough mixing process improvement
- 9. CARBOHYDRATE-TRANSFORMING ENZYMES Most enzymes are hydrolytic and are collectively referred to as glycosyl hydrolases or glycosidases. accounts for about half of enzyme use as processing aids in the food industry. functions by either general acid–base catalysis and/or nucleophilic catalysis. Types (based on the fate of the anomeric configuration (α or β) of the hydrolyzed glycosidic bond) “retaining” or “inverting”,
- 11. STARCH-TRANSFORMING ENZYMES α-Amylase • Hydrolyze starch into smaller dextrins • Make “thin” starch suspensions • Has three separate domains (catalysis, granular starch binding site, and for calcium binding) β-Amylase • exoenzyme that releases successive maltose units from the nonreducing end of a polysaccharide chain by hydrolysis of α- 1,4-glucan linkages. Glucoamylase • produce glucose from starch • Uses : in alcohol production, baking, dental hygiene, fruit juicing • Hydrolyzes 1,4- α-D-glucose residues
- 12. Applications of these include starch hydrolyses, bakery industry and brewery and fermentation.
- 13. SUGAR TRANSFORMATION AND APPLICATIONS • Xylose (glucose) isomerase – used in sweetener production Glucose Isomerization • Glucose oxidase obtained from Aspergillus niger. • Removes oxygen in liquids or within packages, or generating gluconic acid. Glucose Oxidation • production of soft-centered confections and to produce artificial honey from sucrose. Sucrose Hydrolysis (Inversion)
- 14. LIPID-TRANSFORMING ENZYMES Lipase: Act only at the oil–water interface. liberates flavoring (short-chain) fatty acids from lipids and rearranges fatty acyl groups along the glycerol backbone. Used in flavour generation, for example in enzyme modified cheeses. Helps in preparation of structured lipids. Added as dough improvers, which manifests as increased bread volume, more uniform crumb and air cell size.
- 15. Lipoxygenases: Generally considered to have detrimental effects. One beneficial use of is to provide oxidizing power during dough conditioning. oxidizes unsaturated fatty acids generating oxidizing conditions that help strengthen the gluten network by affecting disulfide cross-links within the gluten. Secondary oxidation reactions -destroy endogenous carotenoids.
- 16. Phospholipases: types: A1, A2, C, and D. PhospholipaseA2 has potential use as an agent to create superior lysophospholipid emulsifiers from phospholipid- rich sources, such as egg yolk. Added to crude oil during degumming stage to hydrolyze phospholipids at the sn-2. Important for the removal of otherwise nonhydratable phospholipids.
- 17. THANK YOU!