1) The document discusses food proteins and enzymes, their importance in biological systems, and their various functions and sources.
2) Proteins are made up of amino acids and play many critical roles including as enzymes, hormones, antibodies, and structural components.
3) The document covers the classification of amino acids, sources of food proteins like meat and dairy, and the roles of enzymes in catalyzing biochemical reactions.
Proteins are complex polymers made up of amino acids linked by peptide bonds. They serve essential biological functions including catalyzing biochemical reactions as enzymes, transporting molecules, providing structure, and more. This document provides an introduction to food proteins and enzymes, discussing their importance, classification, sources, and functions. It defines proteins and enzymes, explains their roles in biological systems, and outlines the key amino acids that make up proteins.
Structure and classifications of proteinsHarshJaswal6
This document discusses the structure and classifications of proteins. It describes the primary, secondary, tertiary, and quaternary structures of proteins. The primary structure is the linear sequence of amino acids. Secondary structures include alpha-helices and beta-sheets formed by hydrogen bonding between amino acids. Tertiary structure refers to the 3D conformation of the entire polypeptide chain. Quaternary structure involves interactions between multiple polypeptide subunits. The document also classifies proteins based on their function, composition/solubility, and nutritional levels. Common protein structures and several color reaction tests for identifying proteins are outlined.
Biological and pharmaceutical importance of proteinsAsad Bilal
This document discusses the biological and pharmaceutical importance of proteins. It describes the various cellular functions of proteins such as their structural, enzymatic, hormonal, transport, and messenger roles. The structural importance of fibrous proteins like collagen is also covered. The document then discusses the use of proteins as pharmaceuticals and describes some applications including antibodies, vaccines, hormones and enzymes. It provides examples of iron and zinc chelate proteins and tumor markers.
Proteins are macromolecules composed of amino acids linked by peptide bonds. They perform many important functions in the body and are obtained from both animal and plant sources. The document discusses the structure of proteins including their composition of amino acids, classification based on shape and complexity, properties, and sources. It provides a detailed overview of the key aspects of protein structure and function.
Proteins , INTRODUCTION, GOOD PROTEINS, BAD PROTEINS, STRUCTURE OF PROTEINS, ...Tiffy John
Proteins , INTRODUCTION, GOOD PROTEINS, BAD PROTEINS, STRUCTURE OF PROTEINS, PRIMARY, SECONDARY, TERTIARY AND QUATERNARY STRUCTURE, FIBROUS AND GLOBULAR STRUCTURE, SOURCES, TYPES OF PROTEINS, FUNCTIONS,DEFICIENCIES
Proteins are composed of amino acids and are essential macronutrients that serve important structural and functional roles in the body. They are classified based on solubility and properties into simple, conjugated, and derived proteins and play roles like protection, movement, catalysis, signaling, structure, storage, and transport. The 20 standard amino acids that make up proteins are either essential or non-essential, with essential amino acids needing to be obtained through diet.
The document summarizes information about proteins including their structure, functions, daily requirements, and types. It discusses how proteins are composed of amino acids and form complex structures within cells. The main points are:
- Proteins are composed of chains of amino acids and perform critical functions within cells like building, catalyzing reactions, signaling, transporting materials, and providing defenses.
- Protein structure involves primary, secondary, tertiary, and sometimes quaternary levels that give proteins their shape and determine their specific roles.
- Essential proteins must be obtained through diet as the body cannot synthesize all amino acids. Complete proteins contain all essential amino acids while incomplete proteins require combination with other foods.
- Recomm
Proteins are complex biomolecules composed of amino acids. They have four levels of structure: primary, secondary, tertiary, and quaternary. The primary structure is the linear sequence of amino acids. Secondary structure involves folding into shapes like alpha helices and beta sheets. Tertiary structure is the overall 3D shape of a single protein chain. Quaternary structure refers to the shape of proteins with multiple chains. Proteins are classified based on shape (globular or fibrous) and function (enzymes, hormones, etc.). They have various properties including solubility, hydrolysis, and denaturation.
Proteins are complex polymers made up of amino acids linked by peptide bonds. They serve essential biological functions including catalyzing biochemical reactions as enzymes, transporting molecules, providing structure, and more. This document provides an introduction to food proteins and enzymes, discussing their importance, classification, sources, and functions. It defines proteins and enzymes, explains their roles in biological systems, and outlines the key amino acids that make up proteins.
Structure and classifications of proteinsHarshJaswal6
This document discusses the structure and classifications of proteins. It describes the primary, secondary, tertiary, and quaternary structures of proteins. The primary structure is the linear sequence of amino acids. Secondary structures include alpha-helices and beta-sheets formed by hydrogen bonding between amino acids. Tertiary structure refers to the 3D conformation of the entire polypeptide chain. Quaternary structure involves interactions between multiple polypeptide subunits. The document also classifies proteins based on their function, composition/solubility, and nutritional levels. Common protein structures and several color reaction tests for identifying proteins are outlined.
Biological and pharmaceutical importance of proteinsAsad Bilal
This document discusses the biological and pharmaceutical importance of proteins. It describes the various cellular functions of proteins such as their structural, enzymatic, hormonal, transport, and messenger roles. The structural importance of fibrous proteins like collagen is also covered. The document then discusses the use of proteins as pharmaceuticals and describes some applications including antibodies, vaccines, hormones and enzymes. It provides examples of iron and zinc chelate proteins and tumor markers.
Proteins are macromolecules composed of amino acids linked by peptide bonds. They perform many important functions in the body and are obtained from both animal and plant sources. The document discusses the structure of proteins including their composition of amino acids, classification based on shape and complexity, properties, and sources. It provides a detailed overview of the key aspects of protein structure and function.
Proteins , INTRODUCTION, GOOD PROTEINS, BAD PROTEINS, STRUCTURE OF PROTEINS, ...Tiffy John
Proteins , INTRODUCTION, GOOD PROTEINS, BAD PROTEINS, STRUCTURE OF PROTEINS, PRIMARY, SECONDARY, TERTIARY AND QUATERNARY STRUCTURE, FIBROUS AND GLOBULAR STRUCTURE, SOURCES, TYPES OF PROTEINS, FUNCTIONS,DEFICIENCIES
Proteins are composed of amino acids and are essential macronutrients that serve important structural and functional roles in the body. They are classified based on solubility and properties into simple, conjugated, and derived proteins and play roles like protection, movement, catalysis, signaling, structure, storage, and transport. The 20 standard amino acids that make up proteins are either essential or non-essential, with essential amino acids needing to be obtained through diet.
The document summarizes information about proteins including their structure, functions, daily requirements, and types. It discusses how proteins are composed of amino acids and form complex structures within cells. The main points are:
- Proteins are composed of chains of amino acids and perform critical functions within cells like building, catalyzing reactions, signaling, transporting materials, and providing defenses.
- Protein structure involves primary, secondary, tertiary, and sometimes quaternary levels that give proteins their shape and determine their specific roles.
- Essential proteins must be obtained through diet as the body cannot synthesize all amino acids. Complete proteins contain all essential amino acids while incomplete proteins require combination with other foods.
- Recomm
Proteins are complex biomolecules composed of amino acids. They have four levels of structure: primary, secondary, tertiary, and quaternary. The primary structure is the linear sequence of amino acids. Secondary structure involves folding into shapes like alpha helices and beta sheets. Tertiary structure is the overall 3D shape of a single protein chain. Quaternary structure refers to the shape of proteins with multiple chains. Proteins are classified based on shape (globular or fibrous) and function (enzymes, hormones, etc.). They have various properties including solubility, hydrolysis, and denaturation.
Proteins are essential macromolecules that make up 20% of the human body. They are composed of amino acids and perform many critical functions including structure, regulation, catalysis, movement and more. Protein synthesis occurs in ribosomes within cells. Proteins are not stored but are broken down if excess amino acids are consumed. They have primary, secondary, tertiary and quaternary levels of structure determined by amino acid sequence and interactions. There are 20 standard amino acids that are linked by peptide bonds to form proteins.
Post mortem changes in enzyme and proteinrani mamatha
Endogenous enzymes play an important role in postmortem changes in meat and fish that impact quality attributes. The three main types of muscle proteins - sarcoplasmic, myofibrillar, and stromal - undergo enzymatic changes mediated by proteases and lipases. The calpain system, including calpains, calpastatin and caspases, influences postmortem tenderization through proteolysis. Other enzymes like the proteasome also degrade muscle proteins. Lipolysis is mediated by lipases. These enzymatic changes impact texture, flavor, and other quality traits during maturation and processing of muscle foods.
Proteins are essential biomolecules that make up 15% of cells and perform many critical functions. They are composed of amino acid monomers linked into polymers that fold into complex three-dimensional shapes defined by non-covalent interactions between residues. Protein structure determines its diverse functions, which include serving as enzymes, hormones, antibodies, structural components, transporters, and more. Understanding protein structure is necessary to elucidate proteins' roles at the molecular level.
The document provides an overview of key concepts in pharmacology. It defines pharmacology and discusses the sources of drugs including plants, animals, microbes, marine life, minerals, and synthesis. It also covers pharmacokinetic concepts such as absorption, distribution, metabolism, and excretion. The types of drug actions are examined including therapeutic effects, side effects, adverse reactions, toxicity, and interactions. Classification of drugs and routes of administration are also summarized.
Proteins are composed of amino acids and are essential components of living cells. They serve many important functions in the body including building muscles, transporting nutrients, and regulating processes. There are different types of proteins classified by their structure and source. Amino acids are the building blocks of proteins and come from both animal and plant sources. Getting the proper amount and balance of proteins is important for health, but excess consumption has risks like obesity, heart disease, and kidney problems.
Proteins are organic compounds composed of amino acids linked by peptide bonds. They are classified based on their function in the body. The main classes of proteins include structural, catalytic, contractile, transport, protective, hormonal, immunological, genetic, and nutritive proteins. Structural proteins provide structure to cells and organs, catalytic proteins act as enzymes to speed up metabolic reactions, and transport proteins help move molecules within and between cells.
This document defines different types of proteins and describes their characteristics. It discusses simple proteins like albumin and globulin, conjugated proteins including nucleoproteins and phosphoproteins, and derived proteins such as proteoses and peptides. Simple proteins contain amino acids and differ in solubility, with albumin soluble in water and globulin insoluble. Conjugated proteins combine proteins with other molecules like nucleic acids or phosphate. Derived proteins are denatured or breakdown products of simple proteins.
The document discusses proteins and their structure. It defines proteins as polymers of amino acids, and describes the basic components of amino acids. There are 20 standard amino acids that make up proteins. Proteins are assembled through peptide bonds between amino acid residues. The protein structure is hierarchical, starting with the primary amino acid sequence, then forming secondary and tertiary structures through bonding interactions, and sometimes joining to form quaternary structures. Enzymes are important protein catalysts. Alzheimer's disease involves the abnormal accumulation of tau and amyloid proteins that form plaques and tangles in the brain, destroying neuronal structure and function over time.
Protein is a macronutrient that is essential to building muscle mass. It is commonly found in animal products, though is also present in other sources, such as nuts and legumes. There are three macronutrients: protein, fats and carbohydrates. Macronutrients provide calories, or energy.
Classification of Amino Acids, List of essential and non-essential amino acids, Essential Amino Acids, Chemistry of Amino Acids, 1) Zwitterions (physical properties), Detecting Amino acids, Introduction of Polypeptide, Polypeptide Chain.
This document discusses functional proteins, which are proteins that perform specific functions in the body beyond just structural roles. It provides examples of different types of functional proteins like enzymes, hormones, hemoglobin, and antibodies. It also discusses sources of proteins from foods like wheat, corn, fish, eggs, yogurt and classifies proteins as either complete or incomplete based on their amino acid content. Combining different plant and animal protein sources can create complete proteins that provide all essential amino acids.
Proteins are macromolecules composed of amino acid chains. They have four levels of structure - primary, secondary, tertiary, and quaternary. The primary structure is the amino acid sequence. Secondary structure involves local folding into structures like alpha helices and beta sheets. Tertiary structure describes the overall 3D shape formed by interactions between amino acid side chains. Quaternary structure refers to the shape of proteins made of multiple polypeptide subunits. Proteins serve many important functions and can be classified based on their structure, composition, or function.
The document discusses proteins, which are large organic compounds composed of amino acids linked by peptide bonds. Proteins are the most abundant and functionally diverse molecules in living systems, serving important structural and functional roles. They function as enzymes, hormones, regulators of fluid balance, transporters, and more. The document outlines various protein sources and discusses protein deficiency and its consequences. It also provides information on daily protein requirements based on body weight.
Proteins are complex organic molecules composed of amino acids linked by peptide bonds. They serve important structural and functional roles in the body. As the document outlines, proteins are classified based on their shape (globular or fibrous) or function, such as enzymes, hormones, structural proteins, transport proteins, and immune proteins. The four levels of protein structure - primary, secondary, tertiary, and quaternary - determine a protein's 3D structure. Proteins perform vital roles like muscle contraction, oxygen transport, preventing blood loss, and participating in metabolic reactions as enzymes. They are essential biomolecules that make up tissues and carry out important functions in the body.
Proteins are macromolecules made up of amino acids that are essential for human life. They are needed for growth, tissue repair, enzyme and hormone production. The building blocks of proteins are 22 amino acids, some of which must be obtained through diet. Common sources of protein include meat, eggs, dairy, grains, legumes and nuts. Protein requirements vary based on age, gender and activity level but adults generally need 0.8-1 grams of protein per kilogram of body weight daily. Proteins are classified based on structure, solubility and nutritional properties and perform many important functions in the human body.
This document discusses the properties and characteristics of amino acids. It covers their ionic properties, isoelectric points, optical activity, solubility, UV absorption, and various chemical reactions including esterification, acylation, alkylation, reactions with carbonyl compounds, and reactions involving functional groups like cysteine and methionine. It notes that amino acids are important in developing flavors and aromas in foods during high-temperature cooking methods like frying and baking.
The document discusses designing quality affordable housing in New Jersey. It focuses on creating housing that is connected, active, and sustainable. Connected housing incorporates common spaces like courtyards, balconies, and gardens to foster social interaction. Active design aims to encourage physical activity through outdoor recreation areas and community gardens. Sustainable housing incorporates green building practices and energy efficient design to help lower costs for residents.
This document provides information about purchasing a 3Com 3C16472-US product from Launch 3 Telecom. Launch 3 Telecom is an online retailer and telecom solutions provider that sells networking hardware and genuine 3Com replacement parts. The document describes payment and shipping options for purchasing the 3Com 3C16472-US and notes that Launch 3 Telecom also offers warranty support, repair services, and telecom installation services.
Proteins are essential macromolecules that make up 20% of the human body. They are composed of amino acids and perform many critical functions including structure, regulation, catalysis, movement and more. Protein synthesis occurs in ribosomes within cells. Proteins are not stored but are broken down if excess amino acids are consumed. They have primary, secondary, tertiary and quaternary levels of structure determined by amino acid sequence and interactions. There are 20 standard amino acids that are linked by peptide bonds to form proteins.
Post mortem changes in enzyme and proteinrani mamatha
Endogenous enzymes play an important role in postmortem changes in meat and fish that impact quality attributes. The three main types of muscle proteins - sarcoplasmic, myofibrillar, and stromal - undergo enzymatic changes mediated by proteases and lipases. The calpain system, including calpains, calpastatin and caspases, influences postmortem tenderization through proteolysis. Other enzymes like the proteasome also degrade muscle proteins. Lipolysis is mediated by lipases. These enzymatic changes impact texture, flavor, and other quality traits during maturation and processing of muscle foods.
Proteins are essential biomolecules that make up 15% of cells and perform many critical functions. They are composed of amino acid monomers linked into polymers that fold into complex three-dimensional shapes defined by non-covalent interactions between residues. Protein structure determines its diverse functions, which include serving as enzymes, hormones, antibodies, structural components, transporters, and more. Understanding protein structure is necessary to elucidate proteins' roles at the molecular level.
The document provides an overview of key concepts in pharmacology. It defines pharmacology and discusses the sources of drugs including plants, animals, microbes, marine life, minerals, and synthesis. It also covers pharmacokinetic concepts such as absorption, distribution, metabolism, and excretion. The types of drug actions are examined including therapeutic effects, side effects, adverse reactions, toxicity, and interactions. Classification of drugs and routes of administration are also summarized.
Proteins are composed of amino acids and are essential components of living cells. They serve many important functions in the body including building muscles, transporting nutrients, and regulating processes. There are different types of proteins classified by their structure and source. Amino acids are the building blocks of proteins and come from both animal and plant sources. Getting the proper amount and balance of proteins is important for health, but excess consumption has risks like obesity, heart disease, and kidney problems.
Proteins are organic compounds composed of amino acids linked by peptide bonds. They are classified based on their function in the body. The main classes of proteins include structural, catalytic, contractile, transport, protective, hormonal, immunological, genetic, and nutritive proteins. Structural proteins provide structure to cells and organs, catalytic proteins act as enzymes to speed up metabolic reactions, and transport proteins help move molecules within and between cells.
This document defines different types of proteins and describes their characteristics. It discusses simple proteins like albumin and globulin, conjugated proteins including nucleoproteins and phosphoproteins, and derived proteins such as proteoses and peptides. Simple proteins contain amino acids and differ in solubility, with albumin soluble in water and globulin insoluble. Conjugated proteins combine proteins with other molecules like nucleic acids or phosphate. Derived proteins are denatured or breakdown products of simple proteins.
The document discusses proteins and their structure. It defines proteins as polymers of amino acids, and describes the basic components of amino acids. There are 20 standard amino acids that make up proteins. Proteins are assembled through peptide bonds between amino acid residues. The protein structure is hierarchical, starting with the primary amino acid sequence, then forming secondary and tertiary structures through bonding interactions, and sometimes joining to form quaternary structures. Enzymes are important protein catalysts. Alzheimer's disease involves the abnormal accumulation of tau and amyloid proteins that form plaques and tangles in the brain, destroying neuronal structure and function over time.
Protein is a macronutrient that is essential to building muscle mass. It is commonly found in animal products, though is also present in other sources, such as nuts and legumes. There are three macronutrients: protein, fats and carbohydrates. Macronutrients provide calories, or energy.
Classification of Amino Acids, List of essential and non-essential amino acids, Essential Amino Acids, Chemistry of Amino Acids, 1) Zwitterions (physical properties), Detecting Amino acids, Introduction of Polypeptide, Polypeptide Chain.
This document discusses functional proteins, which are proteins that perform specific functions in the body beyond just structural roles. It provides examples of different types of functional proteins like enzymes, hormones, hemoglobin, and antibodies. It also discusses sources of proteins from foods like wheat, corn, fish, eggs, yogurt and classifies proteins as either complete or incomplete based on their amino acid content. Combining different plant and animal protein sources can create complete proteins that provide all essential amino acids.
Proteins are macromolecules composed of amino acid chains. They have four levels of structure - primary, secondary, tertiary, and quaternary. The primary structure is the amino acid sequence. Secondary structure involves local folding into structures like alpha helices and beta sheets. Tertiary structure describes the overall 3D shape formed by interactions between amino acid side chains. Quaternary structure refers to the shape of proteins made of multiple polypeptide subunits. Proteins serve many important functions and can be classified based on their structure, composition, or function.
The document discusses proteins, which are large organic compounds composed of amino acids linked by peptide bonds. Proteins are the most abundant and functionally diverse molecules in living systems, serving important structural and functional roles. They function as enzymes, hormones, regulators of fluid balance, transporters, and more. The document outlines various protein sources and discusses protein deficiency and its consequences. It also provides information on daily protein requirements based on body weight.
Proteins are complex organic molecules composed of amino acids linked by peptide bonds. They serve important structural and functional roles in the body. As the document outlines, proteins are classified based on their shape (globular or fibrous) or function, such as enzymes, hormones, structural proteins, transport proteins, and immune proteins. The four levels of protein structure - primary, secondary, tertiary, and quaternary - determine a protein's 3D structure. Proteins perform vital roles like muscle contraction, oxygen transport, preventing blood loss, and participating in metabolic reactions as enzymes. They are essential biomolecules that make up tissues and carry out important functions in the body.
Proteins are macromolecules made up of amino acids that are essential for human life. They are needed for growth, tissue repair, enzyme and hormone production. The building blocks of proteins are 22 amino acids, some of which must be obtained through diet. Common sources of protein include meat, eggs, dairy, grains, legumes and nuts. Protein requirements vary based on age, gender and activity level but adults generally need 0.8-1 grams of protein per kilogram of body weight daily. Proteins are classified based on structure, solubility and nutritional properties and perform many important functions in the human body.
This document discusses the properties and characteristics of amino acids. It covers their ionic properties, isoelectric points, optical activity, solubility, UV absorption, and various chemical reactions including esterification, acylation, alkylation, reactions with carbonyl compounds, and reactions involving functional groups like cysteine and methionine. It notes that amino acids are important in developing flavors and aromas in foods during high-temperature cooking methods like frying and baking.
The document discusses designing quality affordable housing in New Jersey. It focuses on creating housing that is connected, active, and sustainable. Connected housing incorporates common spaces like courtyards, balconies, and gardens to foster social interaction. Active design aims to encourage physical activity through outdoor recreation areas and community gardens. Sustainable housing incorporates green building practices and energy efficient design to help lower costs for residents.
This document provides information about purchasing a 3Com 3C16472-US product from Launch 3 Telecom. Launch 3 Telecom is an online retailer and telecom solutions provider that sells networking hardware and genuine 3Com replacement parts. The document describes payment and shipping options for purchasing the 3Com 3C16472-US and notes that Launch 3 Telecom also offers warranty support, repair services, and telecom installation services.
To add documents to your NHS network, go to the NHS networks website and log in. Select your network and click Add to choose a document from your computer to upload. Title and describe the document before saving it to the default or a custom folder. Documents can then be published by selecting viewing permissions at the section or page level from the toolbox.
El documento describe los tres tipos de pesca que se utilizan en los puertos de Málaga: la pesca de bajura cerca de la costa, la pesca de altura más lejos de la costa durante 1-2 semanas, y la pesca de gran altura a gran distancia durante meses. La producción pesquera anual en la provincia de Málaga es de unas 110 millones de euros y 6.000 toneladas. Los principales problemas medioambientales de la pesca son la contaminación por restos de jabón y los efectos del cambio climático.
To add pages to a network on the NHS UK website, log into your network account and click "Your networks". Select your network and then click "Add" and "Page" to create a new page. You can enter a title, summary, and body text for the page and add hyperlinks by highlighting text and inserting the URL link. Finally, use the "Viewing control" to publish or hide the new page.
This document provides an overview of Emmanuel Leroux as the Chief Application Engineer and discusses the application domains, markets, and technologies supported by PRESTO, a software tool for signal integrity analysis. PRESTO can efficiently simulate transmission lines on high-speed, complex systems. It supports PCB, MCM, and interconnect design/validation and can analyze EMC/EMI issues. PRESTO is used in industries like telecom, computer, automotive, aerospace, and consumer electronics. It supports technologies like PCBs, MCMs, and can simulate multiboard, backplane, and entire apparatus designs.
This document summarizes the services of a company that provides digital and data technology professionals to clients globally. The company has a market-leading network of highly skilled professionals that it has placed in over 590 organizations. It offers a suite of recruitment and staffing services, including permanent placement, contract recruitment, flexible workforces and skills benchmarking. The company prides itself on building long-term relationships and taking an immersive "off-grid" approach to understand niche markets and place over 1,000 professionals per year across 17 countries.
Tenerife es la isla más grande del archipiélago de las Islas Canarias, situadas frente a la costa noroeste de África. Tenerife tiene un clima suave sin temperaturas extremas y paisajes diversos que incluyen playas, bosques de pinos y el volcán Teide, la montaña más alta de España. Algunos lugares populares para visitar son Loro Parc, Siam Park, Costa Adeje y los carnavales de Santa Cruz de Tenerife, que son los segundos carnavales más importantes del mundo.
Los Mayas habitaron el sur de México y América Central desde hace aproximadamente 3,000 años. Desarrollaron una sociedad agrícola jerarquizada con gobernantes poderosos y clases sociales. Fueron expertos matemáticos, astrónomos y desarrollaron un avanzado sistema de escritura. Si bien sus ciudades entraron en declive hacia el 900 d.C., los Mayas continuaron viviendo en la región y su legado científico ha perdurado.
Software Engineering- Requirement Elicitation and SpecificationNishu Rastogi
The document discusses the process of requirements engineering for software development. It involves four main steps:
1) Feasibility study to determine if the project is possible.
2) Requirements gathering by communicating with clients and users to understand what the software should do.
3) Creating a software requirements specification (SRS) document that defines system functions and constraints.
4) Validating requirements to ensure they are clear, consistent, and can be implemented.
This document summarizes a presentation given by Michael Nir on delivering value through improving consumer experience. The presentation discusses how adopting agile, UX design thinking, and continuous feedback can help organizations better understand consumer needs and incorporate them into products. However, Nir notes that agile is often still development-centric and lacks sufficient feedback loops. The document then outlines Nir's recommendations for how large organizations can start applying these concepts through cross-functional teams, rapid feedback projects, and uncovering key assumptions about products through collaboration and experimentation.
How to Bust Clinical Trial Myths and Increase Participation - mdgroupmdgroup
In order for the public to benefit from ground-breaking medical research, well-attended clinical trials are vital. What holds potential participants back from participating in trials?
The document discusses various federal redevelopment programs that are at risk of being cut under the new presidential administration, including Community Development Block Grants, Low Income Housing Tax Credits, and HOME funds. It also provides details on how much funding different New Jersey cities and counties receive from federal homeless assistance and HUD programs. The document argues that cuts to these programs would significantly impact affordable housing development and homelessness assistance in New Jersey.
The document discusses how overthinking from a fear of failure can be overcome through prototyping. It provides examples of how prototyping has helped overcome fears in areas like gendered marketing, Christmas cards, and imposter syndrome. The presentation advocates for prototyping as it is accepting of failure and helps with collaboration. Examples are given of how famous products like Post-Its and Play-Doh came from failed prototypes. The document concludes that prototyping can counter overthinking and the fear of failure by allowing ideas to be made into a reality through action.
Este documento presenta información sobre técnicas de estudio efectivas. Incluye consejos sobre cómo crear un espacio de estudio ideal, planificar un horario de estudio diario, y métodos como la lectura activa, el subrayado, los esquemas y los resúmenes para comprender y retener la información de manera más efectiva.
This document provides instructions for building a basic Twitter bot using Python. It outlines setting up a Twitter developer account to get API keys, installing Python and relevant libraries like Tweepy, and writing a Python script to search for tweets containing a phrase and reply to each with a predefined message. The goal is to create a functional Twitter bot as an educational project without needing advanced Python knowledge. Various Python concepts used in the bot like dictionaries, functions, loops, and exception handling are also explained.
This document discusses proteins, including their structure, types, and functions. It notes that proteins are composed of amino acids, of which there are 20 common types. Proteins can have fibrous or globular structures depending on how the polypeptide chains are arranged. The structures of proteins include primary, secondary, tertiary, and sometimes quaternary structures. Examples of protein functions include digestion, transport, structure, signaling, defense, and storage. The document also discusses amino acid classification, protein denaturation, and the mechanism of enzyme catalysis.
This document discusses the classification and structure of proteins. It describes the four levels of protein structure: primary, secondary, tertiary, and quaternary. The primary structure is the linear sequence of amino acids. The secondary structure involves local folding patterns stabilized by hydrogen bonds. The tertiary structure is the overall three-dimensional shape of a protein determined by interactions between amino acid side chains. Quaternary structure refers to the arrangement of multiple protein subunits. The document also categorizes proteins based on their biological functions and physical properties.
Proteins are macromolecules made of amino acids linked by peptide bonds. They serve critical structural, functional, and regulatory roles in the body. Proteins have primary, secondary, tertiary and sometimes quarternary structures determined by their amino acid sequence. They perform diverse roles such as catalyzing biochemical reactions, transporting molecules, providing structure, and participating in immune defenses. Proteins are essential to the structure and function of all living organisms.
Proteins are organic macromolecules made of amino acids linked by peptide bonds. They range widely in size and function. The fundamental units are 20 different amino acids that make up the primary structure in different sequences. Secondary structures like alpha helices and beta sheets form due to hydrogen bonding of amino acid R groups. Tertiary and quaternary structures arise from further folding and interactions between polypeptide subunits. Proteins have important roles like enzymatic catalysis, transport, structure, regulation and defense. They are classified based on solubility and presence of non-protein groups.
This document provides information about protein, amino acids, and nucleic acids. It defines proteins as complex organic compounds that contain carbon, hydrogen, oxygen, and nitrogen. It notes that proteins are found in cells and are involved in many biological processes. It classifies proteins into simple, conjugated, and derived proteins and describes their structures. It also defines amino acids as components of proteins and lists their essential functions. It provides classifications of amino acids and describes their properties. Finally, it discusses nucleic acids and their roles in storing genetic information.
Proteins play many important biochemical roles in the body. They act as enzymes, hormones, antibodies, and structural components. Proteins can be classified based on their shape (fibrous or globular) or chemical composition (simple or conjugated). Simple proteins only contain amino acids, while conjugated proteins also contain non-amino acid groups like nucleic acids, lipids, carbohydrates, or metals. Proteins are further classified as complete or incomplete based on whether they contain all essential amino acids.
Proteins are multifunctional biomolecules that are involved in nearly all cellular processes. They have complex structures ranging from primary to quaternary that determine their diverse functions. Proteins can be classified based on their structure, biological function, shape/solubility, composition, and nutritional properties. They perform critical roles such as metabolism, support, transport, defense, regulation, and motion. Common properties include denaturation through heat, acids, bases, and other chemical and physical changes.
This document discusses proteins, including their structure, function, digestion, and importance. It notes that proteins are made up of amino acids and are essential for building muscle mass. During digestion, proteins are broken down into amino acids in the stomach and small intestine through chemical and mechanical processes aided by enzymes. The amino acids are then absorbed and transported to cells to build new proteins. Maintaining a variety of protein sources in the diet is important for health.
This document discusses the classification and properties of proteins. It describes four levels of protein structure: primary, secondary, tertiary, and quaternary. Proteins can also be classified by their biological function, which includes enzymes, transport proteins, storage proteins, contractile/motile proteins, structural proteins, defense proteins, regulatory proteins, and other functional proteins. Classification by shape and solubility includes fibrous, globular, and membrane proteins. Classification by composition distinguishes between simple and conjugated proteins. Nutritionally, proteins are either complete or incomplete. The document concludes by discussing properties like denaturation and its causes like heat, alcohol, acids, bases, and heavy metal salts.
The document discusses proteins and polypeptides. It defines proteins as polymers of amino acids that perform important structural and functional roles in the body. Proteins are classified based on shape, constitution and nature. Polypeptides are continuous chains of amino acids joined by peptide bonds. They are precursors to proteins and are synthesized through a process involving transcription and translation. Common methods for synthesizing polypeptides include Fischer's method which uses protecting groups to join amino acids, and modifications of this method.
This document discusses proteins, including their definition, composition, sources, storage, requirements, functions, structure, and classification. Some key points:
- Proteins are polypeptides composed of amino acids joined by peptide bonds. They are essential to life and perform many catalytic, structural, transport, and other functions.
- Sources of proteins include animal sources like meat and dairy as well as plant sources like legumes. Storage capacity in organisms is limited compared to carbohydrates and fats.
- Proteins are classified based on their nutritional value, function, structure, and physicochemical properties. Complete proteins contain all essential amino acids while incomplete proteins lack some.
- Structure depends on shape - globular
The document provides information about proteins including their introduction, chemical nature, physical properties, structure, classification, and functions. Some key points:
- Proteins are macromolecules composed of amino acid chains that serve important structural and functional roles in the body.
- They have complex hierarchical structures ranging from primary sequences to quaternary arrangements and take on globular or fibrous shapes.
- Proteins can be classified based on their shape, composition, solubility, and biological function. This includes categories like enzymes, structural proteins, and transport proteins.
- In addition to providing structure, proteins regulate body chemistry through roles as hormones, antibodies, and contractile proteins involved in muscle movement.
B.Sc. Biochem II Biomolecule I U 3.2 Classification of Protein & DenaturationRai University
This document discusses the classification and denaturation of proteins. It describes how proteins can be classified based on their structure, biological function, shape and solubility, composition, and nutritional basis. The main types of proteins classified by function include enzymes, transport proteins, storage proteins, contractile/motile proteins, structural proteins, and regulatory proteins. The document also discusses how proteins can be denatured, or lose their tertiary structure, through the application of heat, acids, bases, alcohols, heavy metal salts, and other stresses. Denaturation disrupts the bonding interactions that give proteins their shape.
Albumin is the major protein found in blood plasma and helps maintain osmotic pressure between blood vessels and tissues. It also serves as a carrier for many substances. Low albumin levels can be caused by conditions that damage the liver like cirrhosis, or by issues that cause excessive protein loss from the kidneys, intestines or burns. Albumin is essential for fluid balance and transport throughout the body.
PROTEINS & LEVELS OF STRUCTURAL CONFORMATION pptx.pptxVIVIEN63
This document discusses various aspects of protein structure and function. It begins by defining proteins and describing their essential roles in the body. It then covers the four levels of protein structural organization: primary, secondary, tertiary, and quaternary structure. Specific examples are provided to illustrate alpha helices, beta sheets, and triple helical structures. The document also discusses protein classification, functions, and conjugated proteins. Overall, it provides a comprehensive overview of the key concepts regarding protein structure and the important roles of proteins in biological systems.
This document discusses the structural hierarchy of proteins from primary to quaternary structure. It explains that proteins are made up of amino acids linked together in polypeptide chains. The primary structure is the sequence of amino acids in the chain. Secondary structures like alpha helices and beta sheets form due to hydrogen bonding. Tertiary structure is the 3D folding of secondary structures into the lowest energy state. Quaternary structure involves multiple polypeptide chains combining to form oligomeric proteins. The document also classifies proteins based on shape and constitution and discusses the functions of different types of proteins like enzymes, hormones, and structural proteins.
Proteins are made up of amino acids and play many critical roles in the body. They have a primary structure formed by a linear chain of amino acids and can fold into secondary and tertiary structures. Proteins are classified based on their composition, structure, and function. They serve as enzymes, structural components, nutrients, regulators, defense agents, transporters, and storage molecules essential for growth, repair, movement, signaling, immunity, and all biochemical reactions in the body.
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.
1. Many factors affect the rate of enzyme-catalyzed reactions including substrate concentration, inhibitors, pH, temperature, pressure, and water content.
2. Enzyme activity is highest at its optimal pH and temperature, and decreases significantly above and below these values. It is also affected by the concentrations of inhibitors and activators.
3. Environmental factors like temperature, pressure, and water content can irreversibly denature enzymes and decrease their activity. Careful control of these factors allows for inhibition of undesirable enzyme reactions in food processing and storage.
This document discusses protein reactions that occur during food processing. It covers both enzyme-catalyzed and chemical reactions that proteins undergo, including proteolytic enzymes like serine and cysteine endopeptidases. Specific modifications are described, such as the Maillard reaction and changes induced by heat, pH, oxidation. Controlling these reactions through processing conditions and enzymes is important for food properties and safety.
This document discusses the physico-chemical properties of proteins, including their physical and chemical properties. It describes proteins' ability to dissociate depending on pH, their optical activity, solubility which depends on factors like pH and salt concentration, and their ability to form foams and stabilize foams through adsorption at gas-liquid interfaces. It also discusses proteins' hydration, swelling power in water, and ability to form gels through polymeric networks or aggregate dispersions.
The document discusses the structure of proteins at different levels:
- Primary structure refers to the amino acid sequence in the polypeptide chain. Secondary structure involves hydrogen bonding that forms alpha helices or beta pleated sheets. Tertiary structure describes the overall 3D shape of the folded polypeptide chain. Quaternary structure involves the interactions between multiple polypeptide subunits. The document outlines the forces that stabilize protein structures such as disulfide bonds, hydrogen bonding, and hydrophobic interactions. Proteins are classified based on their composition, which can include modifications like glycoproteins, lipoproteins, or metal-binding groups.
This document provides an overview of peptides. It defines peptides as short chains of amino acids linked by peptide bonds. Peptides are distinguished from proteins based on their smaller size, typically containing fewer than 50 amino acid units. The document discusses peptide bond formation, characteristics of peptide bonds, classes of peptides, physical properties, examples of individual peptides, food-derived peptides with biological activity, and applications of peptides in molecular biology.
Mahua, Madhuca longifolia (Koenig) (Synonyms, Madhuca indica Gmelin; Family, Sapotaceae), is a large, shady, deciduous tree dotting much of the central Indian landscape, both wild and cultivated. The tree is valued for its flowers, fruits, seeds and timber. The buttercup fruit-seeds, generally ellipsoidally shaped (Figure 1). Madhuca longifolia fruit is valued for its seed which yield high quantity of fat (ca. 50%), commercially known as mahua butter or mowrah butter, and it has many edible and medicinal applications. The butter is of significant commercial importance in India and is used for both edible and cosmetic applications. Mowrah Butter is a yellowish-white butter with a mild odor. The butter is solid at room temperature, but melts readily on contact with the skin. Besides its edible and medicinal uses, Madhuca longifolia fats can also be utilized in the manufacture of laundry soaps and lubricants. Data about mowrah butter are very few and there are not reports in literature about detailed composition of mowrah fat. Recently, in our lab mowrah butter was subjected to detailed and comprehensive analyses to obtain informative profile about the chemical nature of mowrah butter (1). The antiradical action of mowrah butter with also compared extra virgin olive oil. The results will be important as an indication of the potentially nutraceutical and economical utility of mowrah butter as a new source of edible fats.
Oil Recovery from Enzymatically-treated Goldenberry (Physalis peruviana L...Mohamed Hassanien
Fruit processing industry produce a large amount of agro-waste products which are a rich source of dietary fibre, protein and oil. Goldenberry (Physalis peruviana L.) is one of the most promising fruits and many interesting functional products anticipated to be developed from it [1, 2]. The pomace (seeds and skins) represent a large portion of the waste generated during juice processing (ca. 27.4% of fruit weight). To date, there has been no report on the by-products of goldenberry as well as the aqueous extraction of these by-products. This work was done to study the effects of several processing factors on enzyme-aided aqueous extraction of oil from goldenberry pomace and to verify the applicability of this innovative technology to goldenberry by-products. The main variables affecting the hydrolytic process should be enzyme concentration, hydrolysis time, particle size and moisture. The effect of these variables on the oil extractability from goldenberry agro-waste after juice processing was studied. The results provide important information for the industrial application of goldenberry. As a first step toward developing goldenberry as a commercial crop, the data obtained will be useful as an indication of the potentially economical utility of goldenberry as a source of edible oil.
This document discusses various enzymatic analytical methods used for food analysis, including substrate determination, enzyme activity determination, enzyme immunoassay, and polymerase chain reaction. Specifically, it covers:
1) Substrate determination methods like end-point assays that use coupled enzyme reactions to measure food constituents.
2) Determining enzyme activity in food to evaluate quality and optimize processes by measuring reaction rates under controlled conditions.
3) Enzyme immunoassays like ELISA that use antibody-antigen reactions and enzyme-labeled antigens to detect food compounds.
4) Polymerase chain reaction (PCR) which amplifies DNA for sensitive species identification and detecting genetically modified foods. PCR allows analysis of heat-treated foods where proteins
The document discusses factors that affect enzyme-catalyzed reactions, including substrate concentration, inhibitors, pH, temperature, and pressure. It explains how the reaction rate depends on substrate and enzyme concentrations and can be influenced by activators and inhibitors. It also describes how each enzyme has an optimal pH range and temperature, and discusses how temperature affects reaction rates, microbial growth rates, and thermal inactivation of enzymes.
This document discusses reactions of proteins involved in food processing. It describes various enzyme-catalyzed reactions like those involving serine, cysteine, metallo and aspartic endopeptidases. It also discusses chemical and enzymatic modifications of proteins for food processing, including succinylation, reductive methylation, and disulfide bond reduction/reoxidation. The enzymatic plastein reaction is described which joins peptide fragments through peptide bonds. Overall, the document provides an overview of reactions and modifications that can change protein properties for uses in food processing.
This document discusses the physico-chemical properties of proteins under two main sections: physical properties and chemical reactions. The physical properties section describes 5 sub-properties: dissociation, optical activity, solubility/hydration/swelling, foam formation and stabilization, and emulsifying effect. The chemical reactions section lists 7 amino acid residues that proteins can undergo chemical modifications with: arginine, glutamic/aspartic acid, cystine, cysteine, methionine, histidine, and tyrosine. Protein properties and reactions are important for understanding protein structure, function, and applications in food processing.
The document discusses the structure of proteins at multiple levels, from primary to quaternary structure. It describes the primary structure as the amino acid sequence linked by peptide bonds. The secondary structure refers to local spatial arrangements, such as alpha helices and beta sheets, formed through hydrogen bonding between peptide bonds. Tertiary structure describes the overall 3D shape of the folded polypeptide chain. Quaternary structure applies to proteins made of multiple polypeptide subunits that assemble into an ordered structure. The document outlines various methods for determining protein structure, including amino acid sequencing and X-ray crystallography.
Peptides are short chains of amino acids linked by peptide bonds. They are distinguished from proteins by typically containing fewer than 50 amino acid units. Peptides are formed through condensation reactions between carboxyl and amino groups of separate amino acids, releasing a water molecule. Peptide bonds are rigid and planar, contributing to protein structure stability. Peptides serve many important biological functions and can be classified based on their production method, including through ribosomal translation, nonribosomal synthesis, and enzymatic digestion of proteins in foods. Bioactive peptides derived from food proteins can have beneficial effects like lowering blood pressure, cholesterol, and antimicrobial properties.
Implementation of International Educational ProgramMohamed Hassanien
This document discusses key elements for developing an international educational program, including a vision, mission, goals, values, student learning outcomes, and examples. It provides guidance on writing statements for each element and examples. The vision describes what the ideal future program would look like. The mission states the program's purpose and stakeholders. Goals are broad targets for the program. Values describe the program's principles. Student learning outcomes are specific statements of the knowledge and skills students will obtain.
Amino acids have several key properties:
1. They are amphoteric, taking on positive, negative, or neutral charges depending on pH. Their isoelectric point is when the net charge is neutral.
2. They have acidic and basic groups that allow them to undergo various chemical reactions like esterification, acylation, and reactions with carbonyl compounds.
3. When heated to high temperatures during cooking, amino acids can form mutagenic and potentially toxic compounds like acrylamide or heterocyclic amines. The Maillard reaction and Strecker degradation play important roles in these processes.
Fast Antiradical Test for Monitoring Deep Fried OilsMohamed Hassanien
This document presents research on developing a fast antiradical test for monitoring deep fried oils. Deep frying is commonly used worldwide but causes physical and chemical changes to oils through oxidation. The researchers aimed to compare physicochemical parameters and antiradical performance of oils during frying. Oils were analyzed after frying at different time points. Strong correlations were found between total polar compounds, absorptivity at 232nm/270nm, and antiradical scavenging activity against DPPH radicals. This suggests antiradical testing could rapidly monitor oil quality changes during frying. The method is accurate, inexpensive, and independent of oil type.
Lipid Classes, Sterols and Tocopherols of Black cumin (Nigella sativa L.), Co...Mohamed Hassanien
The document analyzes and compares the lipid classes, fatty acid profiles, and triacylglycerol compositions of black cumin, coriander, and niger seed oils. Specifically:
- The neutral lipid fraction constitutes over 90% of the total lipids in each seed oil. Black cumin has the highest ratio of saturated to polyunsaturated fatty acids in its neutral lipid fraction.
- Coriander seed oil has the highest levels of the monounsaturated fatty acid petroselinic acid and contains more triolein and tripetroselinin than the other seed oils.
- Niger seed oil stands out for its high content of saturated fatty acids like palmitic acid and trip
Investigation on Lipid Composition of Exotic OilseedsMohamed Hassanien
This document summarizes the results of a study investigating the lipid composition and bioactive compounds of black cumin, coriander, and niger seed oils. High levels of oils were recovered from the seeds, making them suitable for vegetable oil production. The seed oils contained high amounts of essential fatty acids and antioxidants like tocopherols. Black cumin and coriander seed oils in particular could be produced and marketed as crude oils. The polar lipid fractions of the seeds oils showed antioxidant effects and could potentially be used as natural additives, lecithins, or in cosmetics. Further research is needed to understand how the seed oil compositions relate to biological effects and how processing may impact their structures and antioxidative
Heritage Conservation.Strategies and Options for Preserving India HeritageJIT KUMAR GUPTA
Presentation looks at the role , relevance and importance of built and natural heritage, issues faced by heritage in the Indian context and options which can be leveraged to preserve and conserve the heritage.It also lists the challenges faced by the heritage due to rapid urbanisation, land speculation and commercialisation in the urban areas. In addition, ppt lays down the roadmap for the preservation, conservation and making value addition to the available heritage by making it integral part of the planning , designing and management of the human settlements.
2. -Introduction to Food Proteins and Enzymes
-Biological Importance of Protein
-Biological Functions of Protein
-Functions of Food Proteins
-Sources of Food Proteins
-Amino Acids (AA)
-Classification of Amino Acids
4. Introduction to Food Proteins and Enzymes
-Proteins play a central role in biological systems.
-Enzymes perform the biochemical processes that sustain the life
of a cell/organism.
-Proteins (such as collagen and keratin) also function as structural
components of cells and complex organisms.
-The functional diversity of proteins arises from their chemical
makeup. Proteins are highly complex polymers, made up of 20
different amino acids.
-The constituents are linked via substituted amide bonds. The
amide linkage in proteins is a partial double bond, which further
underscores the structural complexity of protein polymers.
-Complicated protein structure gives rise to a multitude of three-
dimensional structural forms with different biological functions.
5. Introduction to Food Proteins and Enzymes
-At the elemental level, proteins contain 50–55% carbon, 6–7%
hydrogen, 20–23% oxygen, 12–19% nitrogen, and 0.2–3.0% sulfur.
-Protein synthesis occurs in ribosomes. After the synthesis, some
amino acids are modified by cytoplasmic enzymes which changes
the composition of some proteins.
-Proteins that
are not enzymatically modified in cells are called homoproteins,
and those that are modified or complexed with nonprotein
components are called conjugated proteins or heteroproteins. The
nonprotein components are referred to as prosthetic groups.
-Examples of conjugated proteins include nucleoproteins
(ribosomes), glycoproteins (casein), phosphoproteins (kinases,
phosphorylases), lipoproteins (proteins of egg yolk, plasma
proteins), and metalloproteins (hemoglobin, and several enzymes).
6. Introduction to Food Proteins and Enzymes
-Proteins can be classified according to their structural organization.
-Globular proteins are exist in spherical shapes, resulting from
folding of the polypeptide chain(s) on itself.
-Fibrous proteins are exist in rod-shapes containing twisted linear
polypeptide chains (e.g., collagen, keratin, and elastin). Fibrous
proteins also can be formed as a result of linear aggregation of
small globular proteins, such as actin and fibrin.
-A majority of enzymes are globular proteins, and fibrous proteins
function as structural proteins.
7. Introduction to Food Proteins and Enzymes
-Biological functions of proteins can be classified as
-Enzyme catalysts,
-Structural proteins,
-Hormones (insulin and growth hormone),
-Transfer proteins (serum albumin and hemoglobin),
-Antibodies (immuno-globulins),
-Storage proteins (egg albumen and seed proteins), and
-Protective proteins (toxins and allergens).
-Storage proteins are found in eggs and seeds. These proteins act as
sources of nitrogen and amino acids for germinating seeds and
embryos.
-Protective proteins are a part of the defense mechanism for the
survival of certain microorganisms and animals.
8. Introduction to Food Proteins and Enzymes
-All biologically produced proteins can be used as food proteins.
However, for practical purposes, food proteins may be defined as
those that are easily digestible, nontoxic, nutritionally adequate,
functionally useable in food products, and available in abundance.
-Traditionally, milk, meats (including fish and poultry), eggs, cereals,
and oilseeds have been the major sources of food proteins.
However, because of the increase in world population,
nontraditional sources of proteins for human nutrition need to be
developed to meet the future demand.
-The suitability of such new protein sources for use in foods,
however, depends on their cost and their ability to fulfill the normal
role of protein ingredients in processed and home-cooked foods.
9. Introduction to Food Proteins and Enzymes
-The functional properties of proteins in foods are related
to their structural and physicochemical characteristics.
-A fundamental understanding of the physical, chemical,
nutritional, and functional properties of proteins and the
changes these properties undergo during processing is
essential if the performance of proteins in foods is to be
improved, and if new or less costly sources of proteins are
to compete with traditional food proteins.
10. Introduction to Food Proteins and Enzymes
-Enzymes are proteins with catalytic activity due to their power of
specific activation and conversion of substrates to products:
Substrate(s) Product(s)
-Some of enzymes are composed only of amino acids linked via
peptide bonds to give proteins that range in size from about 12,000
MW to 1,000,000 MW.
-Other enzymes contain additional components, such as
carbohydrate, phosphate, and cofactor groups. Enzymes have all
the chemical and physical characteristics of other proteins.
-Composition-wise, enzymes are not different from other proteins
found in nature and they comprise a small part of our daily protein
intake in our foods. However, unlike other groups of proteins, they
are highly specific catalysis for many chemical reactions required
by living organisms.
Enzyme
11. Introduction to Food Proteins and Enzymes
-Enzymes are synthesized in vivo by living organisms, based
on expression (translation) of specific genes.
-Enzymes are found in all living systems and make life
possible, whether the organisms are adapted to growing near
0°C, or at 37°C (humans), or near 100°C (microorganisms
found in hot springs).
-Enzymes accelerate reactions by factors of thousand times.
-Enzymes are highly selective for a limited number of
substrates, since the substrate(s) must bind correctly into the
active site before any catalysisoccurs.
-Enzymes control the direction of reactions, leading to specific
product(s) that can be very valuable by-products for foods,
nutrition, and health.
12. Proteins
•Proteins are complex organic nitrogenous
compounds of high molecular weight.
•Proteins are the most complex materials
produced in nature.
•They are consisting of α-amino acids
linked together by peptide linkages.
13. Proteins
•The name protein is derived from the Greek word
proteios “of prime importance or the first kind”
this is because proteins are the basis of the
cytoplasm of cells and are present in all living
organisms.
•Proteins are the most abundant macromolecules
in living cells and constitute 50% or more of their
dry weight.
14. Proteins
•Proteins are polymers of α-amino acids.
•Proteins are synthesized from only 20 amino
acids, known as the common amino acids.
•Amino acids are formed mainly of carbon,
hydrogen, oxygen and nitrogen.
•Nitrogen is a characteristic component of
proteins forming about 16% of their weight (i.e.
100 g of protein contains 16 g of nitrogen)
15. Biological Importance of Protein
1- Plasma membrane proteins (channel, carrier,
pump proteins) regulate the transfer of many
substances across the cell membrane
2- All receptors are protein in nature
3- All enzymes are proteins in nature
4-All antibodies (immuno-gobulins) are proteins
in nature
5- Some hormones are proteins in nature (e.g.
insulin and growth hormone).
16. Biological Importance of Protein (cont.)
6- Some proteins are protective
e.g. Keratins (skin, hair and nails) make the skin resistant
to chemicals
7-Some proteins are supportive
e.g. Collagen; the most abundant protein in animals.
8-Hemoglobin is a protein carries O2 in blood.
9-Actin and myosin are contractile proteins found in
muscle cells and responsible for muscular contraction.
10-Amino acids (AA) are converted to other nitrogenous
substances of great physiological importance (e.g.
creatine, histamine, heme, purines and pyrimidines).
17. 1. Catalytic function:
Nearly all chemical reactions in biological systems are
catalyzed by specific enzymes.
2. Transport and storage:
For example;
➢ Hemoglobin transports oxygen in blood.
➢ Myoglobin carries and stores oxygen in muscle.
➢ Albumin transports free fatty acids in blood.
➢ Transferrin transports iron in blood.
3. Coordinated motion:
Actin and myosin are contractile proteins in muscle.
Biological Functions of Protein
18. Biological Functions of Protein (cont.)
4. Structural and mechanical support:
- Collagen (a fibrous protein in skin and bone).
5. Defense function:
- Clotting factors (prevent loss of blood).
- Immuno-globulins (protect against infection).
6. Generation and transmission of nerve impulses:
Receptor proteins (neuro-transmitters, e.g. acetyl choline), are
responsible for transmitting nerve impulses.
7. Control of growth and differentiation:
The activities of different cells are coordinated by hormones.
Many hormones are polypeptides and proteins, such as insulin
and thyroid-stimulating hormone.
20. Functions of Food Proteins
-Amino acids, peptides and proteins are important constituents of
food.
-They supply the required building blocks for protein biosynthesis.
-They contribute to the flavor of food and are precursors for aroma
compounds.
-They contribute, with other food compounds such as
carbohydrates, to colors formed during thermal or enzymatic
reactions in production, processing and storage of food.
-Proteins contribute to food physical properties through their
ability to build or stabilize gels, foams, emulsions and fibrillar
structures.
-The nutritional energy value of proteins (17 kJ/g or 4 kcal/g) is as
high as that of carbohydrates.
21. -The most important sources of protein are grain, oilseeds and
legumes, followed by meat and milk.
-In addition to plants and animals, protein producers include algae
(Chlorella, Spirulina spp.), yeasts and bacteria (single-cell proteins
[SCP]).
-Bacteria of the species Pseudomonas in aqueous methanol
produce about 0.3 ton of protein per ton of alcohol.
-Some products rich in protein also result from other processes, e.
g., in oil and starch production.
-Protein concentrates and protein isolates serve to enhance the
nutritional value and to enhance of the physical properties of
foods. They are added to traditional foods, such as meat and cereal
products, but they are also used in the production of novel food
items such as meat and milk substitutes.
Sources of Food Proteins
22. Raw materials in which protein enrichment takes place include:
•Legumes such as soybeans,
•Wheat, which provide gluten as a by-product of starch production,
•Potatoes;after starch production, proteinisolatedby thermal coagulation,
•Eggs, which are processed into different products (e.g., whole egg, egg white
and egg yolk products),
•Milk,which supplies casein and whey protein,
•Fish, which supplies proteinconcentrates after fat extraction,
•Blood from slaughter animals, which is processed into blood meal, blood
plasma concentrate and globin isolate,
•Green plants grown for animal fodder, such as alfalfa, which are processed into
leaf proteinconcentrates through the thermal coagulationof proteins.
Sources of Food Proteins (cont.)
25. -There are about 200 amino acids found in nature.
-There are about 20 amino acids in a protein hydrolysate.
-With a few exceptions, their general in the simplest
case, R=H (aminoacetic acid or glycine).
-In other amino acids, R is an aliphatic, aromatic or
heterocyclic residue and may incorporate other
functional groups.
Amino Acids (AA)
26. -α-Amino acids are the building units of proteins.
-Each α-amino acid consists of
-an amino group (-NH2),
-a carboxylic acid group (-COOH),
- a hydrogen atom (-H) and
-a side chain group (-R),
all connected to a carbon atom called α- carbon atom.
The α-carbon is the first carbon next to the –COOH
group.
-The side chain group (R) is specific and unique for each
amino acid.
-The R may be a hydrogen, a straight or branched-chain
aliphatic group, an aromatic ring or a heterocyclic ring.
30. Basic amino acid structure
-α-Carbon is chiral (Asymmetric
carbon) in all amino acids
except for glycine.
-At pH 7 amino acids have both
+ve and -ve charges so called
dipolar ion or zwitterions.
-Amino acids have a tetrahedral
structure (3D shape).
32. -Natural amino acids are in
the L-configuration
-L and D forms are called
Optical isomers
(Stereoisomers = Enantiomers)
-Biological system in all
organisms synthesize and use
only L-amino-acids
33.
34. There are
20 amino acids
that make up
the proteins, each with
different side chain.
36. Classification of Amino Acids
• Side chain (R group) classification.
• Biological classification.
• Metabolic classification.
37. 1-Side Chain (R group) Classification
CHEMICAL CLASSIFICATION
-The amino acids are classified according to the
chemical structure of the side chain (R) into:
1. Aliphatic
2. Hydroxy
3. Sulfur containing
4. Aromatic
5. Acidic
6. Basic
7. Imino acids
39. Non Polar (hydrophobic) Amino Acids
• Side chains of non polar (hydrophobic) amino acids can not
participate in hydrogen or ionic bonds, but they form
hydrophobic interactions.
• In aqueous environment, non polar amino acids tend to be
present in the interior of proteins.
• Non polar (hydrophobic) amino acids include:
-Amino acids with aliphatic R group (glycine, alanine).
-Amino acids with aliphatic branched R group (valine, leucine
and isoleucine).
-Amino acids with aromatic R group (phenylalanine,
tryptophan).
-Amino acids with sulfur containing R group (methionine).
-Imino acid (proline).
40. Amino acids with non polar side chains
Glycine
(Gly - G)
Alanine
(Ala – A)
(Aliphatic)
41. Amino acids with non polar side chains
Isoleucine
(Ile – I)
Leucine
(Leu – L)
(branched chains, aliphatic)
Valine
(Val – V)
42. Amino acids with non polar side chains
Phenylalanine
(Phe – F)
Tryptophan
(Trp – W)
(Aromatic)
43. Amino acids with non polar side chains
Proline
(Pro – P)
(imino)
44. Amino acids with non polar side chains
Methionine
(Met – M)
(sulfur containing)
45. • Side chains of polar (hydrophilic) amino acids can participate in
hydrogenor ionic bonds.
• Therefore, in aqueous environment polar amino acids tend to be
presenton the surface of proteins.
• Polar (hydrophilic)amino acids are classifiedinto:
1. Polar chargedamino acids:
• Acidic amino acids (aspartic & glutamic acids) and
• Basic amino acids (arginine,lysine,histidine)
2. Polar unchargedamino acids:
• Amino acids with OH group(serine,threonine,tyrosine)
• Amino acids with SH group (cysteine)
• Amino acids with amide group (glutamine,asparagine)
Polar (hydrophilic) Amino Acids
46. Amino acids with polar charged side chains
Aspartic acid
(Asp – D)
Glutamic acid
(Glu – E)
(acidic group)
49. Amino acids with polar uncharged side chains
Cysteine
(Cys – C)
(with SH group)
50. Amino acids with polar uncharged side chains
Asparagine
(Asn – N)
Glutamine
(Gln – Q)
(with amide group)
51. 2-Biological (Nutritional) classification
On nutritional basis AA are classified into essential or non-
essential AA.
1- Non essential amino acids:
Amino acids that could be synthesized in the body, so they are
not needed in the diet. They are 10 AA.
2- Essential amino acids:
Amino acids that could not be synthesized in the body, so they
have to be taken in the diet, and their deficiency results in
diseases.
• The essential amino acids are not more important to our body
than the non-essential amino acids.
• Both (all 20 AA) are equally needed and equally essential for the
normal growth and good health.
53. 3-Metabolic classification
(According to their metabolic fate in the body )
Glucogenic amino acids:
Amino acids that can give glucose.
Ketogenicamino acids:
Amino acids that can give ketone bodies.
Glucogenic/Ketogenic(mixed) amino acids:
Amino acids that can give both ketone bodies
and glucose.