This document discusses immobilized multi-enzyme systems and their applications. It begins by defining immobilized enzymes as enzymes that are physically confined to retain catalytic activity and can be reused continuously. The main advantages of immobilized enzymes are increased stability and ease of reuse. Various methods for immobilizing enzymes are discussed, including covalent binding, cross-linking, adsorption, ionic bonding, entrapment, and encapsulation. Specific industrial enzymes like lipases, proteases, amylases, and cellulases are highlighted along with their uses and benefits of immobilization.
1. Corn is genetically modified to be resistant to the herbicide glyphosate. Tobacco is genetically modified to reduce nicotine levels.
2. Government agencies regulate GM foods to ensure they are safe. In the US, GM foods are required to be labeled if the nutritional value is changed or a new allergen is introduced.
3. 'Super weeds' refer to weeds that have become resistant to herbicides as a result of cross-pollination with herbicide-tolerant genetically modified crops. This can occur if the herbicide-tolerant gene transfers to weeds, making them resistant and harder to control.
This document discusses the applications of enzymes in industry. It begins by introducing enzymes and their functions in nature. It then discusses several types of enzymes and their functions, such as cellulase breaking down cellulose. It provides examples of how enzymes are used in industries like detergents, starch conversion, fuel alcohol production, and food. Enzymes allow detergents to clean effectively at lower temperatures. They are also used to convert starch to sugars in industries like high fructose corn syrup production. The document concludes that using enzymes provides savings in resources like energy and water.
Microbial enzymes are widely used in food processing due to their ability to catalyze specific reactions. About 80% of total enzyme production by dollar value is used by the food industry. Enzymes offer advantages over whole microorganisms by catalyzing single step conversions of specific substrates to products. The main classes of enzymes used in food processing are hydrolases, isomerases, and oxidoreductases. Recombinant DNA technology allows for improved production of enzymes in bacteria and yeast. Immobilizing enzymes allows for their reuse, reducing costs. Thermostable enzymes are advantageous as they maintain activity at higher temperatures, increasing reaction rates. Enzymes are also used to treat food waste by converting components into value-added
This document provides information about enzyme immobilization. It discusses how immobilizing enzymes attaches them to an insoluble support, which allows them to be reused over multiple catalytic cycles while being easily separated from reaction products. The advantages of immobilization include improved enzyme stability under various conditions and the ability for repetitive use. Common immobilization techniques include adsorption, ionic binding, covalent binding, cross-linking, and entrapment. The choice of support material and technique can impact enzyme activity and stability. Characterization of immobilized enzymes includes measuring activity, bound protein, and specific activity of the bound protein.
Role of immobilized Enzymes in Food industryJasmineJuliet
Immobilization techniques, Immobilization techniques in food industry, Immobilized Enzymes, Need for immobilization, Role of immobilized Enzymes in Food Industry, Methods of immobilization, Production of lactose free milk, Production of High Fructose corn syrups, Production of Juice in industry level by Immobilized enzymes of Pectinase, Meat tenderization by immobilized Enzymes, Immobilized Amino acylase, immobilized glucose isomerase, immobilized pectinase, Immobilized alkaline phosphatase.
Immobilization involves attaching enzymes or cells to insoluble carriers to make them stable and reusable. The main immobilization techniques are adsorption, covalent binding, ionic interactions, cross-linking, and entrapment. Immobilization provides advantages like enabling enzyme use in non-aqueous solvents and extreme pH/temperatures while maintaining activity. It also allows for reuse of enzymes and reduces product inhibition. The document discusses various industrial applications of immobilized enzymes and cells in areas like biomedical treatment, food production, biofuel synthesis, waste treatment, and more.
1. Corn is genetically modified to be resistant to the herbicide glyphosate. Tobacco is genetically modified to reduce nicotine levels.
2. Government agencies regulate GM foods to ensure they are safe. In the US, GM foods are required to be labeled if the nutritional value is changed or a new allergen is introduced.
3. 'Super weeds' refer to weeds that have become resistant to herbicides as a result of cross-pollination with herbicide-tolerant genetically modified crops. This can occur if the herbicide-tolerant gene transfers to weeds, making them resistant and harder to control.
This document discusses the applications of enzymes in industry. It begins by introducing enzymes and their functions in nature. It then discusses several types of enzymes and their functions, such as cellulase breaking down cellulose. It provides examples of how enzymes are used in industries like detergents, starch conversion, fuel alcohol production, and food. Enzymes allow detergents to clean effectively at lower temperatures. They are also used to convert starch to sugars in industries like high fructose corn syrup production. The document concludes that using enzymes provides savings in resources like energy and water.
Microbial enzymes are widely used in food processing due to their ability to catalyze specific reactions. About 80% of total enzyme production by dollar value is used by the food industry. Enzymes offer advantages over whole microorganisms by catalyzing single step conversions of specific substrates to products. The main classes of enzymes used in food processing are hydrolases, isomerases, and oxidoreductases. Recombinant DNA technology allows for improved production of enzymes in bacteria and yeast. Immobilizing enzymes allows for their reuse, reducing costs. Thermostable enzymes are advantageous as they maintain activity at higher temperatures, increasing reaction rates. Enzymes are also used to treat food waste by converting components into value-added
This document provides information about enzyme immobilization. It discusses how immobilizing enzymes attaches them to an insoluble support, which allows them to be reused over multiple catalytic cycles while being easily separated from reaction products. The advantages of immobilization include improved enzyme stability under various conditions and the ability for repetitive use. Common immobilization techniques include adsorption, ionic binding, covalent binding, cross-linking, and entrapment. The choice of support material and technique can impact enzyme activity and stability. Characterization of immobilized enzymes includes measuring activity, bound protein, and specific activity of the bound protein.
Role of immobilized Enzymes in Food industryJasmineJuliet
Immobilization techniques, Immobilization techniques in food industry, Immobilized Enzymes, Need for immobilization, Role of immobilized Enzymes in Food Industry, Methods of immobilization, Production of lactose free milk, Production of High Fructose corn syrups, Production of Juice in industry level by Immobilized enzymes of Pectinase, Meat tenderization by immobilized Enzymes, Immobilized Amino acylase, immobilized glucose isomerase, immobilized pectinase, Immobilized alkaline phosphatase.
Immobilization involves attaching enzymes or cells to insoluble carriers to make them stable and reusable. The main immobilization techniques are adsorption, covalent binding, ionic interactions, cross-linking, and entrapment. Immobilization provides advantages like enabling enzyme use in non-aqueous solvents and extreme pH/temperatures while maintaining activity. It also allows for reuse of enzymes and reduces product inhibition. The document discusses various industrial applications of immobilized enzymes and cells in areas like biomedical treatment, food production, biofuel synthesis, waste treatment, and more.
Enzymes are biological catalysts that speed up biochemical reactions. They are used in many industrial applications such as food processing, detergents, and biofuel production. Enzymes have several advantages over inorganic catalysts such as high specificity and ability to function under mild conditions. In food processing, enzymes are used in dairy, meat, baking, and brewing. Common enzymes include amylases, proteases, lipases, and pectinases. The paper, biofuel, and brewing industries also utilize enzymes like cellulases, xylanases, and amylases. Overall, enzymes are valuable biocatalysts with many applications in biotechnology due to their specificity and efficiency.
This document discusses various methods of enzyme immobilization including adsorption, covalent binding, entrapment, and membrane confinement. It then outlines several applications of immobilized enzymes in biomedical fields, food industry, wastewater treatment, biodiesel production, textile industry, detergent industry, and pharmaceutical industry. Specifically, it notes that immobilized enzymes are used in medicine to treat diseases, in food to increase enzyme stability, in biodiesel production to improve catalyst recovery, and in industries like textiles and detergents to allow enzymes to withstand harsh conditions.
This document discusses glucose isomerase (GI), an enzyme that converts glucose to fructose and is important industrially. GI is found in bacteria, fungi, and plants. It is commonly used to produce high fructose corn syrup and convert xylose to ethanol. Methods to immobilize GI include adsorbing it to carriers like DEAE-cellulose or entrapping whole cells that produce GI in polymers. Immobilizing GI makes it reusable and more stable for industrial applications like high fructose corn syrup production.
The document discusses various topics from Unit 4 of the Biology for Engineers course:
1. Probiotics and enzymes were discussed, including the beneficial bacteria used in food production and industrial applications of enzymes.
2. Biofertilizers were introduced, which are microorganisms that enrich soil nutrients through nitrogen fixation, phosphorus solubilization, and stimulating plant growth. Common types of biofertilizers include Rhizobium, Azospirillum, and mycorrhizae.
3. The production of the Rhizobium biofertilizer was briefly outlined, noting its role in nitrogen fixation through root nodules in leguminous plants.
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.
The document discusses bio-catalysis and the use of enzymes in organic synthesis. It notes that bio-catalysts are derived from renewable resources, are biodegradable, and allow reactions to proceed under mild conditions. Examples are given of green bio-catalytic processes developed by Pfizer and Codexis for manufacturing pharmaceuticals. The types of bio-catalyst enzymes are described along with their advantages over traditional chemical catalysts. Methods of immobilizing enzymes on supports are summarized, including entrapment, cross-linking, and attachment to porous or nano-structured materials.
In this context, there is a need to use “biodetergent or biocleaners”, which offer a better option to the synthetic detergents with respect to their biodegradability, low toxicity, non-corrosiveness environmental-friendliness, enhanced cleaning properties and their increased efficiency and stability in different formulations.
To counter these limitations, enzyme-based detergents are fast emerging as an alternative to synthetic detergents owing to their
biodegradability,
low toxicity,
non- corrosiveness,
environmental friendliness,
enhanced cleaning properties,
increased efficiency and stability in different formulations.
They are therefore also being referred to as “green chemicals”
Presently, proteases, amylases, lipases and cellulases make up the major portion of the market for industrial enzymes in cleaning applications.
Protease enzymes were first hydrolases introduced into detergent formulations specifically for the degradation of protein-based stains. Proteases have been classified according to the nucleophile or reactive component found at their catalytic sites
Enzymes are biological catalysts that speed up biochemical reactions. They are used in many industrial processes like food production, cleaning products, and medical applications. Enzymes function with high selectivity and specificity. Enzyme technology utilizes enzymes from sources like plants, animals, and microbes. Key industries that use enzymes include food production, animal feed, detergents, dairy, and biofuels. Enzymes offer advantages over inorganic catalysts like operating at mild conditions and generating pure products.
Enzyme definition, Enzyme immobilization introduction , Enzyme immobilization definition, Explanation about support/ matrix, Examples about immobilized enzymes and their product, Advantages of immobilization, Applications of immobilization, Methods of immobilization in different categories like Adsorption method, Covalent bonding method, Entrapment method, Co polymerization /Cross linking method, Encapsulation method, Applications of immobilized enzymes, Diagrammatic explanation about methods of immobilization.
Immobilization various techniques and it's therapeutic applicationsananyaroy878073
This document summarizes various techniques for immobilizing enzymes and their therapeutic applications. It defines enzyme immobilization as restricting an enzyme's movement by trapping it within an inert support material. The main techniques discussed are adsorption, entrapment, encapsulation, covalent bonding, and cross-linking. Adsorption physically binds enzymes to carrier surfaces, while entrapment traps them within porous matrices. Encapsulation encloses enzymes within semi-permeable membranes. Covalent bonding and cross-linking form strong chemical bonds between enzymes and supports. Therapeutic uses of immobilized enzymes include producing antibiotics, diagnosing and treating diseases, and applications in food processing, research, biodiesel production, and waste treatment.
Enzymes are protein catalysts that speed up biochemical reactions without being consumed. They are produced by living organisms and work by lowering the activation energy of reactions. Enzymes are used as biocatalysts in industries like food processing and are essential for human digestion and DNA replication. Environmental factors like temperature and pH can impact enzyme activity, as can cofactors and inhibitors. Biocatalysts offer advantages over chemical catalysts like milder reaction conditions and higher product quality. They have many applications including food processing, diagnostics, and molecular biology.
This document discusses the various applications of microbial enzymes in the food industry. It outlines several key enzymes produced by microorganisms that are used in food processing, including α-amylases, glucoamylases, proteases, lactase, lipases, phospholipases, and cellulases. These enzymes are widely used in industries like baking, brewing, dairy, and more to improve qualities like flavor, texture, and shelf life of foods. Microbial enzymes are preferable to plant and animal enzymes for industrial use due to properties like stability, consistency, and low cost of production.
This document discusses enzymes, their sources and applications. It notes that enzymes are key to biological activities and catalyze chemical reactions in living cells. Over 4000 enzymes are known with 200 used commercially. The top three enzyme producers are Novozymes, DuPont and Roche. Enzymes have various applications including in technical areas like pulp/paper and textiles, food processing like dairy and baking, and household care. Microbial enzymes from bacteria, fungi and yeast are now commonly used due to stability and variety. The document provides details on leading enzyme companies and specific enzyme applications in industries like textiles, detergents, dairy and food processing.
Cellulases are enzymes that break down cellulose by hydrolyzing the beta-1,4-glycosidic bonds between glucose molecules in cellulose. There are three main types of cellulases - endocellulases, exocellulases, and beta-glucosidases. Fungi are a major producer of cellulases and species like Aspergillus, Trichoderma, and Penicillium are used industrially to produce cellulase enzymes. Cellulases have many applications including use in food processing, textiles, pulp and paper, biofuels, agriculture, and more.
Development of Metoprolol Tartrate Sustained Release Formulations by using Mo...BRNSSPublicationHubI
This document discusses the development of metoprolol tartrate sustained release formulations using modified starches. It begins by introducing metoprolol tartrate as a drug candidate for sustained release formulations and modified starches as potential release retardants. It then provides background on the basic structure and sources of starch, as well as various applications of native and modified starches in pharmacy, including as tablet disintegrants, controlled release polymers, plasma volume expanders, in bone tissue engineering, artificial red blood cells, nanotechnology, and microparticles. The goal of the study is to design sustained release metoprolol tartrate formulations using different modified starches prepared from various natural starches to evaluate their effect on drug release characteristics.
AMYLASES AND PROTEASES ARE THE ENZYMES USED A LOT IN FOOD INDUSTRIES FOR THE PRODUCTION OF FOODS. THESE ARE SUPPOSED TO PRODUCE AT A LARGER QUANTITIES IN ORDER TO FULFILL THE DEMANDS FROM THESE INDUSTRIES, THE LARGE SCALE PRODUCTION OF THESE ENZYMES MUST BE CARRIED OUT. THIS METHOD OF LARGER PRODUCTION OF THESE ENZYMES ARE EXPLAINED IN THIS PRESENTATION.
This document discusses enzyme immobilization. It begins by defining enzymes and their function, then describes why immobilization is useful. Enzymes are immobilized to make them reusable, more stable, and easier to separate from reaction products. The document outlines several immobilization methods including adsorption, covalent binding, cross-linking and entrapment. It notes the advantages and disadvantages of each method. Finally, applications of immobilized enzymes in industries like food, biomedical, and research are presented.
Enzymes are biological catalysts that are proteins and greatly increase the rate of biochemical reactions. They contain an active site that converts substrates to products. Enzymes accelerate reactions by lowering the activation energy required for substrates to reach the transition state. This is achieved through the enzyme-substrate complex. Immobilizing enzymes makes them reusable and more stable while reducing costs. Common immobilization methods include entrapment in a polymer matrix, microencapsulation, adsorption, covalent binding, and cross-linking to a support. Enzyme applications include medical, analytical, manipulative, and industrial uses.
This presentation was provided by Steph Pollock of The American Psychological Association’s Journals Program, and Damita Snow, of The American Society of Civil Engineers (ASCE), for the initial session of NISO's 2024 Training Series "DEIA in the Scholarly Landscape." Session One: 'Setting Expectations: a DEIA Primer,' was held June 6, 2024.
Enzymes are biological catalysts that speed up biochemical reactions. They are used in many industrial applications such as food processing, detergents, and biofuel production. Enzymes have several advantages over inorganic catalysts such as high specificity and ability to function under mild conditions. In food processing, enzymes are used in dairy, meat, baking, and brewing. Common enzymes include amylases, proteases, lipases, and pectinases. The paper, biofuel, and brewing industries also utilize enzymes like cellulases, xylanases, and amylases. Overall, enzymes are valuable biocatalysts with many applications in biotechnology due to their specificity and efficiency.
This document discusses various methods of enzyme immobilization including adsorption, covalent binding, entrapment, and membrane confinement. It then outlines several applications of immobilized enzymes in biomedical fields, food industry, wastewater treatment, biodiesel production, textile industry, detergent industry, and pharmaceutical industry. Specifically, it notes that immobilized enzymes are used in medicine to treat diseases, in food to increase enzyme stability, in biodiesel production to improve catalyst recovery, and in industries like textiles and detergents to allow enzymes to withstand harsh conditions.
This document discusses glucose isomerase (GI), an enzyme that converts glucose to fructose and is important industrially. GI is found in bacteria, fungi, and plants. It is commonly used to produce high fructose corn syrup and convert xylose to ethanol. Methods to immobilize GI include adsorbing it to carriers like DEAE-cellulose or entrapping whole cells that produce GI in polymers. Immobilizing GI makes it reusable and more stable for industrial applications like high fructose corn syrup production.
The document discusses various topics from Unit 4 of the Biology for Engineers course:
1. Probiotics and enzymes were discussed, including the beneficial bacteria used in food production and industrial applications of enzymes.
2. Biofertilizers were introduced, which are microorganisms that enrich soil nutrients through nitrogen fixation, phosphorus solubilization, and stimulating plant growth. Common types of biofertilizers include Rhizobium, Azospirillum, and mycorrhizae.
3. The production of the Rhizobium biofertilizer was briefly outlined, noting its role in nitrogen fixation through root nodules in leguminous plants.
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.
The document discusses bio-catalysis and the use of enzymes in organic synthesis. It notes that bio-catalysts are derived from renewable resources, are biodegradable, and allow reactions to proceed under mild conditions. Examples are given of green bio-catalytic processes developed by Pfizer and Codexis for manufacturing pharmaceuticals. The types of bio-catalyst enzymes are described along with their advantages over traditional chemical catalysts. Methods of immobilizing enzymes on supports are summarized, including entrapment, cross-linking, and attachment to porous or nano-structured materials.
In this context, there is a need to use “biodetergent or biocleaners”, which offer a better option to the synthetic detergents with respect to their biodegradability, low toxicity, non-corrosiveness environmental-friendliness, enhanced cleaning properties and their increased efficiency and stability in different formulations.
To counter these limitations, enzyme-based detergents are fast emerging as an alternative to synthetic detergents owing to their
biodegradability,
low toxicity,
non- corrosiveness,
environmental friendliness,
enhanced cleaning properties,
increased efficiency and stability in different formulations.
They are therefore also being referred to as “green chemicals”
Presently, proteases, amylases, lipases and cellulases make up the major portion of the market for industrial enzymes in cleaning applications.
Protease enzymes were first hydrolases introduced into detergent formulations specifically for the degradation of protein-based stains. Proteases have been classified according to the nucleophile or reactive component found at their catalytic sites
Enzymes are biological catalysts that speed up biochemical reactions. They are used in many industrial processes like food production, cleaning products, and medical applications. Enzymes function with high selectivity and specificity. Enzyme technology utilizes enzymes from sources like plants, animals, and microbes. Key industries that use enzymes include food production, animal feed, detergents, dairy, and biofuels. Enzymes offer advantages over inorganic catalysts like operating at mild conditions and generating pure products.
Enzyme definition, Enzyme immobilization introduction , Enzyme immobilization definition, Explanation about support/ matrix, Examples about immobilized enzymes and their product, Advantages of immobilization, Applications of immobilization, Methods of immobilization in different categories like Adsorption method, Covalent bonding method, Entrapment method, Co polymerization /Cross linking method, Encapsulation method, Applications of immobilized enzymes, Diagrammatic explanation about methods of immobilization.
Immobilization various techniques and it's therapeutic applicationsananyaroy878073
This document summarizes various techniques for immobilizing enzymes and their therapeutic applications. It defines enzyme immobilization as restricting an enzyme's movement by trapping it within an inert support material. The main techniques discussed are adsorption, entrapment, encapsulation, covalent bonding, and cross-linking. Adsorption physically binds enzymes to carrier surfaces, while entrapment traps them within porous matrices. Encapsulation encloses enzymes within semi-permeable membranes. Covalent bonding and cross-linking form strong chemical bonds between enzymes and supports. Therapeutic uses of immobilized enzymes include producing antibiotics, diagnosing and treating diseases, and applications in food processing, research, biodiesel production, and waste treatment.
Enzymes are protein catalysts that speed up biochemical reactions without being consumed. They are produced by living organisms and work by lowering the activation energy of reactions. Enzymes are used as biocatalysts in industries like food processing and are essential for human digestion and DNA replication. Environmental factors like temperature and pH can impact enzyme activity, as can cofactors and inhibitors. Biocatalysts offer advantages over chemical catalysts like milder reaction conditions and higher product quality. They have many applications including food processing, diagnostics, and molecular biology.
This document discusses the various applications of microbial enzymes in the food industry. It outlines several key enzymes produced by microorganisms that are used in food processing, including α-amylases, glucoamylases, proteases, lactase, lipases, phospholipases, and cellulases. These enzymes are widely used in industries like baking, brewing, dairy, and more to improve qualities like flavor, texture, and shelf life of foods. Microbial enzymes are preferable to plant and animal enzymes for industrial use due to properties like stability, consistency, and low cost of production.
This document discusses enzymes, their sources and applications. It notes that enzymes are key to biological activities and catalyze chemical reactions in living cells. Over 4000 enzymes are known with 200 used commercially. The top three enzyme producers are Novozymes, DuPont and Roche. Enzymes have various applications including in technical areas like pulp/paper and textiles, food processing like dairy and baking, and household care. Microbial enzymes from bacteria, fungi and yeast are now commonly used due to stability and variety. The document provides details on leading enzyme companies and specific enzyme applications in industries like textiles, detergents, dairy and food processing.
Cellulases are enzymes that break down cellulose by hydrolyzing the beta-1,4-glycosidic bonds between glucose molecules in cellulose. There are three main types of cellulases - endocellulases, exocellulases, and beta-glucosidases. Fungi are a major producer of cellulases and species like Aspergillus, Trichoderma, and Penicillium are used industrially to produce cellulase enzymes. Cellulases have many applications including use in food processing, textiles, pulp and paper, biofuels, agriculture, and more.
Development of Metoprolol Tartrate Sustained Release Formulations by using Mo...BRNSSPublicationHubI
This document discusses the development of metoprolol tartrate sustained release formulations using modified starches. It begins by introducing metoprolol tartrate as a drug candidate for sustained release formulations and modified starches as potential release retardants. It then provides background on the basic structure and sources of starch, as well as various applications of native and modified starches in pharmacy, including as tablet disintegrants, controlled release polymers, plasma volume expanders, in bone tissue engineering, artificial red blood cells, nanotechnology, and microparticles. The goal of the study is to design sustained release metoprolol tartrate formulations using different modified starches prepared from various natural starches to evaluate their effect on drug release characteristics.
AMYLASES AND PROTEASES ARE THE ENZYMES USED A LOT IN FOOD INDUSTRIES FOR THE PRODUCTION OF FOODS. THESE ARE SUPPOSED TO PRODUCE AT A LARGER QUANTITIES IN ORDER TO FULFILL THE DEMANDS FROM THESE INDUSTRIES, THE LARGE SCALE PRODUCTION OF THESE ENZYMES MUST BE CARRIED OUT. THIS METHOD OF LARGER PRODUCTION OF THESE ENZYMES ARE EXPLAINED IN THIS PRESENTATION.
This document discusses enzyme immobilization. It begins by defining enzymes and their function, then describes why immobilization is useful. Enzymes are immobilized to make them reusable, more stable, and easier to separate from reaction products. The document outlines several immobilization methods including adsorption, covalent binding, cross-linking and entrapment. It notes the advantages and disadvantages of each method. Finally, applications of immobilized enzymes in industries like food, biomedical, and research are presented.
Enzymes are biological catalysts that are proteins and greatly increase the rate of biochemical reactions. They contain an active site that converts substrates to products. Enzymes accelerate reactions by lowering the activation energy required for substrates to reach the transition state. This is achieved through the enzyme-substrate complex. Immobilizing enzymes makes them reusable and more stable while reducing costs. Common immobilization methods include entrapment in a polymer matrix, microencapsulation, adsorption, covalent binding, and cross-linking to a support. Enzyme applications include medical, analytical, manipulative, and industrial uses.
This presentation was provided by Steph Pollock of The American Psychological Association’s Journals Program, and Damita Snow, of The American Society of Civil Engineers (ASCE), for the initial session of NISO's 2024 Training Series "DEIA in the Scholarly Landscape." Session One: 'Setting Expectations: a DEIA Primer,' was held June 6, 2024.
A review of the growth of the Israel Genealogy Research Association Database Collection for the last 12 months. Our collection is now passed the 3 million mark and still growing. See which archives have contributed the most. See the different types of records we have, and which years have had records added. You can also see what we have for the future.
How to Add Chatter in the odoo 17 ERP ModuleCeline George
In Odoo, the chatter is like a chat tool that helps you work together on records. You can leave notes and track things, making it easier to talk with your team and partners. Inside chatter, all communication history, activity, and changes will be displayed.
How to Fix the Import Error in the Odoo 17Celine George
An import error occurs when a program fails to import a module or library, disrupting its execution. In languages like Python, this issue arises when the specified module cannot be found or accessed, hindering the program's functionality. Resolving import errors is crucial for maintaining smooth software operation and uninterrupted development processes.
Leveraging Generative AI to Drive Nonprofit InnovationTechSoup
In this webinar, participants learned how to utilize Generative AI to streamline operations and elevate member engagement. Amazon Web Service experts provided a customer specific use cases and dived into low/no-code tools that are quick and easy to deploy through Amazon Web Service (AWS.)
Chapter wise All Notes of First year Basic Civil Engineering.pptxDenish Jangid
Chapter wise All Notes of First year Basic Civil Engineering
Syllabus
Chapter-1
Introduction to objective, scope and outcome the subject
Chapter 2
Introduction: Scope and Specialization of Civil Engineering, Role of civil Engineer in Society, Impact of infrastructural development on economy of country.
Chapter 3
Surveying: Object Principles & Types of Surveying; Site Plans, Plans & Maps; Scales & Unit of different Measurements.
Linear Measurements: Instruments used. Linear Measurement by Tape, Ranging out Survey Lines and overcoming Obstructions; Measurements on sloping ground; Tape corrections, conventional symbols. Angular Measurements: Instruments used; Introduction to Compass Surveying, Bearings and Longitude & Latitude of a Line, Introduction to total station.
Levelling: Instrument used Object of levelling, Methods of levelling in brief, and Contour maps.
Chapter 4
Buildings: Selection of site for Buildings, Layout of Building Plan, Types of buildings, Plinth area, carpet area, floor space index, Introduction to building byelaws, concept of sun light & ventilation. Components of Buildings & their functions, Basic concept of R.C.C., Introduction to types of foundation
Chapter 5
Transportation: Introduction to Transportation Engineering; Traffic and Road Safety: Types and Characteristics of Various Modes of Transportation; Various Road Traffic Signs, Causes of Accidents and Road Safety Measures.
Chapter 6
Environmental Engineering: Environmental Pollution, Environmental Acts and Regulations, Functional Concepts of Ecology, Basics of Species, Biodiversity, Ecosystem, Hydrological Cycle; Chemical Cycles: Carbon, Nitrogen & Phosphorus; Energy Flow in Ecosystems.
Water Pollution: Water Quality standards, Introduction to Treatment & Disposal of Waste Water. Reuse and Saving of Water, Rain Water Harvesting. Solid Waste Management: Classification of Solid Waste, Collection, Transportation and Disposal of Solid. Recycling of Solid Waste: Energy Recovery, Sanitary Landfill, On-Site Sanitation. Air & Noise Pollution: Primary and Secondary air pollutants, Harmful effects of Air Pollution, Control of Air Pollution. . Noise Pollution Harmful Effects of noise pollution, control of noise pollution, Global warming & Climate Change, Ozone depletion, Greenhouse effect
Text Books:
1. Palancharmy, Basic Civil Engineering, McGraw Hill publishers.
2. Satheesh Gopi, Basic Civil Engineering, Pearson Publishers.
3. Ketki Rangwala Dalal, Essentials of Civil Engineering, Charotar Publishing House.
4. BCP, Surveying volume 1
This document provides an overview of wound healing, its functions, stages, mechanisms, factors affecting it, and complications.
A wound is a break in the integrity of the skin or tissues, which may be associated with disruption of the structure and function.
Healing is the body’s response to injury in an attempt to restore normal structure and functions.
Healing can occur in two ways: Regeneration and Repair
There are 4 phases of wound healing: hemostasis, inflammation, proliferation, and remodeling. This document also describes the mechanism of wound healing. Factors that affect healing include infection, uncontrolled diabetes, poor nutrition, age, anemia, the presence of foreign bodies, etc.
Complications of wound healing like infection, hyperpigmentation of scar, contractures, and keloid formation.
This presentation includes basic of PCOS their pathology and treatment and also Ayurveda correlation of PCOS and Ayurvedic line of treatment mentioned in classics.
How to Setup Warehouse & Location in Odoo 17 InventoryCeline George
In this slide, we'll explore how to set up warehouses and locations in Odoo 17 Inventory. This will help us manage our stock effectively, track inventory levels, and streamline warehouse operations.
This slide is special for master students (MIBS & MIFB) in UUM. Also useful for readers who are interested in the topic of contemporary Islamic banking.
2. introduction
✓ Enzymes physically confined or localized in a certain defined region of space with
retention of their catalytic activities, and which can be used repeatedly and
continuously.
✓ Immobilized enzymes are currently the subject of considerable interest because of
their advantages over soluble enzymes.
✓ In addition to their use in industrial processes, the immobilization techniques are the
basis for making a number of biotechnology products with application in diagnostics,
bioaffinity chromatography, and biosensors.
✓ At the beginning, only immobilized single enzymes were used, after 1970s more
complex systems including two-enzyme reactions with cofactor regeneration and
living cells were developed.
✓ The enzymes can be attached to the support by interactions ranging from reversible
physical adsorption and ionic linkages to stable covalent bonds.
✓ The primary benefit of immobilization is protecting the enzymes from the harsh
environmental conditions (e.g., elevated temperatures, extreme pH values, etc.).
3. The use of immobilized enzymes in industry is becoming a routine process for the
manufacture of many key compounds in the pharmaceutical, chemical, and food
industry.
Some enzymes like lipases are naturally robust and efficient, can be used for the
production of many different molecules, and have found broad industrial
applications.
Some more specific enzymes, like transaminases, have required protein engineering
to become suitable for applications in industrial manufacture.
For all enzymes, the possibility to be immobilized and used in a heterogeneous form
brings important industrial and environmental advantages such as simplified
downstream processing or continuous process operations.
A series of large-scale applications of immobilized enzymes with benefits for the
food, chemical, pharmaceutical, cosmetics, and medical device industries.
Several hundred enzymes have been immobilized in different forms and more than a
dozen immobilized enzymes; for example, penicillin G acylase, invertase, lipases,
proteases, etc. have been used as catalysts in various large-scale processes.
4.
5. Fig. Problems associated with enzyme usage (left), and the advantages of
immobilization processes (right).
6. Useful Enzymes for Industrial Applications
Lipase – Lipases are hydrolases that catalyze the conversion of
triacylglycerols to fatty acids and glycerol. Lipase enzymes catalyze
transesterification, interesterification, and esterification reactions. Lipase
substrates are varied, including lipids, phospholipids, ether lipids,
lysophospholipids, etc. This class of enzymes can undergo vital functions in
transportation, digestion, and processing of dietary lipids. They are used in
the production of emulsifiers, flavors, fragrances, cosmetics, thermoplastics,
agrochemicals, and many other commonly used products. Lipases are also
applied in the fabrication of several biodiesels by triglyceride
transesterification, in addition to the manufacturing of concentrated fatty
acids by means of fat hydrolysis.
Unfortunately, not all classes of lipases are able to operate at elevated
temperature (i.e., 100 °C); besides that, the half-lives of the enzymes are
conveyed to be very concise. Consequently, the production of extra stable
lipase forms that can endure the high production temperatures and have a
longer shelf-life is desirable. Immobilization is one of the approaches that is
adequate for attaining stable lipase enzymes.
7. Proteases - Proteases catalyze proteolysis, breaking down proteins into
amino acids and/or small polypeptides. These classes of enzymes perform that
mainly by means of cleavage of the peptide bonds in the proteins through
hydrolysis reactions. Proteases are involved in diverse fundamental biological
functions, such as protein catabolism, digestion of ingested proteins, and cell
signaling.
Proteases are crucial to several industries that require the enzyme-
aided/digestion of proteins from different sources, e.g., pharmaceutical, dairy,
leather, food, baking, textile, and brewing industries.
Furthermore, proteases are used in various forms of medical therapies and are
considered an important biocatalyst that is used in laboratories, medical care
institutions, and hospitals. There is also significant attention on the
examination of protease classes that are capable of catalyzing reactions in
cold water, which will ease their application for detergent use in tap water, i.e.,
room temperature. Proteases have very short half-lives, and thus
immobilization is needed for attaining a stable form of the enzyme to widen
and ease their worldwide application.
8. Amylase - Amylases comprise ∼30% of the consumption of enzymes globally.
Amylases are applied in starch manufacturing for the hydrolysis of starch to
transform starch to a syrup of glucose, fructose, etc.
Amylases obtained from microorganisms possess an extensive spectrum of
functions due to having more stability than those obtained from plant and animal
sources. Additionally, amylases from microorganisms’ origins have a big
production capacity and produce enzymes of certain required properties.
These are significantly applied in the food processing sector, e.g., for preparing
digestive aids and starch syrups. In the paper industry, amylases are used for
the amendment of the starch in coated papers through the manufacturing of
high molecular weight and low-viscosity starch. Last but not least, amylases
could be potentially useful for the manufacturing of fine chemicals.
Nevertheless, the applications of lipases are often obstructed by their low
stability, short shelf-storage life, and extreme sensitivity to process conditions.
These drawbacks can be greatly lessened by means of immobilization
approaches.
9. Cellulase – Cellulases are produced mainly from bacteria and fungi, and
these catalyze most cellulolysis reactions. Cellulase enzymes break down
cellulose molecules to oligosaccharides and beta-glucose.
Cellulase enzymes are crucial in several industrial sectors. They are used in
undesirable color extractions from fruit juices and pulps. Cellulases are also
used in the detergent industry as color brighteners and softeners, as well as in
the biostoning of jeans products. Additionally, these enzymes are used in
pretreating biomass for improving the nutritious value of food, as well as in
treating industrial waste. They also possess a broad-scale application in
pharmaceutical, animal feed, textile, and paper processing industries, which
makes them ranked as one of the most significant worldwide enzymes.
Nonetheless, using cellulase in all of these industries is restricted because of
their reduced stability, concise shelf-storage life, extreme sensitivity to many
of the processes’ conditions, etc. These drawbacks can be greatly reduced by
means of immobilization approaches of cellulases.
10. The recent expansion of biotechnological/nanotechnology advances has revitalized
interest in the immobilization strategies of enzymes to a great extent.
Immobilization strategies entail fixing or entrapping enzymes within solid support
materials. Researchers have suggested several support materials, besides many
beneficial approaches for the immobilization of enzymes.
The main function of the support is to stabilize the structures of enzymes and accordingly
preserve their efficacy to a great extent by rendering them more resistant to the
surrounding environments.
Enzyme immobilization permits an easy recovery of both the used enzymes and their
support materials, and this is particularly beneficial in the food, medical, and
pharmaceutical applications.
Enzymes in their immobilized forms possess much higher stability and are also easier to
handle when compared to their free forms.
Additionally, the enzymatic reaction can occur in a nonaqueous medium where the solid
supports preserve the enzyme’s constituents and make them stronger, which enhances
their catalytic activity and renders them reusable for several times.
Immobilization of Enzymes
11. Another benefit of the immobilization process is that the catalysts can alter from
homogeneous to heterogeneous forms after the enzymatic binding, which assists in
separating the enzymes, producing products with high purity.
Various immobilization methods have been applied so far including encapsulation,
cross-linking, covalent binding, adsorption, and entrapment
12. Modes of immobilization
Covalent Binding
✓ Covalent binding is a well-established technique of enzyme immobilization
that is accomplished by connecting the enzymes with support materials (e.g.,
porous silica, polyacrylamide, agarose, porous glass, etc.) via highly stable,
strong linkages.
✓ Covalent binding possesses many advantages, such as producing durable
enzymes and obtaining a sufficient recovery of the enzymes as to be reused.
Covalent binding increases the stereospecificity of the enzymes, elevating
their stability.
✓ For instance, covalently bonded lipases with glyoxyl agarose showed a 3-fold
enhancement in their enantioselectivity (asymmetric synthesis).
✓ By applying this method, there is a low probability of enzyme leakage even
with the presence of high concentrations of substrates or along with strong
buffer solutions, which usually facilitates many kinds of denaturation
reactions.
13. Cross-linking
✓ Cross-linking immobilization is a strategy where enzymes are interconnected
through covalent bonding without carriers.
✓ The intermolecular cross-linking is accomplished through the presence of linker
agents, which are used as bridges between two adjacent enzyme molecules.
✓ Cross-linking immobilization delivers a robust connection between the enzymes,
leading to superior stabilities. Several types of cross-linking strategy were reported,
e.g., cross-linked spray-dried enzymes, cross-linked aggregates, cross-linked
dissolved enzymes, etc.
✓ Cross-linked dissolved enzymes refer to intermolecular cross-linkages of enzymes
in their crystal forms using glutaraldehyde.
✓ It is a distinguished active immobilized enzyme technique that produces
controllable particle sizes (1–100 μm).
✓ It possesses significant resistance to organic solvents and elevated temperatures.
Its high stability, recycling with optimum catalytic activity, and volumetric efficiency
make it highly desirable for industrial biotransformations.
14. Adsorption
✓ Immobilization by adsorption is a simple carrier bound technique where reversible
immobilization is attained. This technique mainly depends on physical adsorption.
Materials applied for the adsorption to occur include ion-exchange resins, alumina,
activated carbon, and many more.
✓ This method is relatively cheap and easily implemented, yet it possesses a weak binding
force (i.e., hydrogen bonds, salt linkage, ionic bonds, hydrophobic bonds, etc.) among the
carrier and the enzyme.
✓ Depending on the arrangements of proteins and the charges of matrices, a strongly
adsorbed/undistorted enzyme can be produced. In this strategy, any kind of carrier
materials could be used, yet not all types of enzymes could be immobilized on any carrier
material because, for an appropriate adsorption to take place, some conditions must be
met, i.e., the affinity of the enzyme–carrier is of vital importance.
✓ A successful adsorption is guaranteed with the presence of specific active groups that are
present on the carrier material. These help in the development of interactions among the
enzymes and carriers. Yet, if not present, these interactions could be modified via adding
carrier modifiers that enable the connections between the enzymes and carriers.
✓ The advantages of enzyme immobilization by adsorption are that minimal activation steps
are required, few reagents are needed, and it is a cheap method and easily implemented.
15. Figure. Effect of the surface modifier in adsorption immobilization. The
surface modifier strengthens the binding of an enzyme to its carrier.
16. Ionic Bonding
✓ Ionic bonding is a straightforward, inexpensive, and reversible immobilization
technique that entails ionic interaction among the enzymes and the support
materials.
✓ The nature of this noncovalent immobilization is that the procedure is simply
reversed by altering the temperature as well as the ionic strength. (32) The
support materials used in this immobilization technique are generally charged,
as the proteins should have opposite charges in order for them to bind
together.
✓ The ionic bonding is simply reversed by changing the pH or through salting out
of the enzymes. To sustain an optimum pH throughout the reaction, easy
control of the acidity/alkalinity in the mixture is undertaken, as the matrix that
immobilizes the enzyme is steadily charged.
✓ The occurrence of a charged support produces some complications, such as
distortion of the enzyme structure, changes in the enzyme kinetics, etc.
✓ Besides that, excessive charges can deteriorate the enzyme catalysis, which
may thus hinder obtaining a high product yield
17. Entrapment
✓ Entrapment is an irreversible immobilization process. It is simply described as
caging of enzymes in a network of fibers, through covalent or noncovalent bonds.
✓ It is also described as the entrapment of enzymes inside a support material or
fiber, either having a lattice structure or in the membranes of polymers.
✓ In using this method, the enzyme leakage can be easily avoided through
controlling the pore size of the polymeric network that permits the free diffusion
of the reaction contents, either substrates or products.
✓ In this strategy, enzymes do not react with polymers; consequently, denaturation
is generally prevented. The entrapment technique has diverse advantages
including high loading capacity of the enzymes, low fabrication costs, enhanced
mechanical stability of the entrapped enzymes, and lower mass transfer.
✓ It also allows the modification of the encapsulation material to get an optimum
microenvironment by attaining an optimal pH, suitable polarity, or amphilicity.
18. Encapsulation
✓ The encapsulation immobilization technique involves entrapping several
biomolecules into different polymeric matrices.
✓ Encapsulation is analogous to entrapment in the way that both the enzymes
and the cells are free in solutions yet in a controlled space.
✓ Encapsulation is aimed at immobilizing sensitive enzymes and cells’ solutions
bounded in tiny vesicles having porous membranes.
✓ Sizable enzymes cannot move out or into the capsules, yet tiny
substrates/products could move freely across a semipermeable membrane.
✓ Encapsulation maintains biological systems in a fine film so as to avert the
biocatalysts from contact with the environment, which might damage their
efficiency. Therefore, encapsulation allows the activity of biocatalysts to last
for long periods.