Survey
* Your assessment is very important for improving the workof artificial intelligence, which forms the content of this project
* Your assessment is very important for improving the workof artificial intelligence, which forms the content of this project
Proteins Chapter 4 The Nature of Proteins Basic Building Material All proteins are made up of amino acids. Amino acids are joined in unique, chain sequences to form specific proteins. Each amino acid is joined by a peptide bond. Amino acids are then reassembled in the body in a specific order to form a variety of proteins needed by the body. Because proteins are relatively large, complex molecules, they are often subject to mutations, or malformations in structure. Example: protein-folding mistakes are involved in Alzheimer’s disease. When protein is eaten, the protein in in foods is broken down into amino acids in the digestive process. Major Functions of Protein Dietary Importance The word amino refers to compounds containing nitrogen. Proteins have a basic structure of: carbon, hydrogen, oxygen and nitrogen. Protein is about 16% nitrogen. As such protein is the primary source of nitrogen in the diet. Chemical composition of protein: C – carbon H – hydrogen O – oxygen N - nitrogen Classes of Amino Acids There are 20 common amino acids, which are all vital to human life and health. These amino acids are classified as: indispensable, (9) dispensable, (5) or conditionally indispensable (6 ) in the diet according to whether the body can make them. Indispensible Amino Acids (amino acids necessary in the diet and cannot be left out) Nine (9) amino acids are classified as indispensable amino acids because the body cannot manufacture them in sufficient quantity, or at all. Refer to Box 4-1 page 48. Classes of Amino Acids – Cont’d Dispensable Amino Acids Refers to five (5) amino acids that the body can synthesize from other amino acids. These amino acids are needed by the body for healthy life, but are dispensable in the diet. The remaining six (6) amino acids are classified as conditionally indispensable. Like other amino acids they must be consumed in the diet. Balance Relative intake and output of substances in the body to maintain equilibrium necessary for health in various circumstances throughout life. Protein Balance: The body’s tissue proteins are constantly being broken down into amino acids, a process called catabolism, and they resynthesized into tissue proteins as needed, a process called anabolism. Protein Balance – Cont’d To maintain nitrogen balance, the part of the amino acid that contains nitrogen may be removed by deamination, then converted to ammonia (NH³) and excreted as urea in the urine. The remaining nonnitrogen residue can be used to make carbohydrate or fat or reattached to make another amino acid, if necessary. Tissue turnover is a continuous process of: reshaping, rebuilding, and adjusting as necessary to maintain overall protein balance within the body. The body also maintains a balance between: tissue proteins and plasma protein, which are then further balanced with dietary protein intake. Nitrogen Balance The body’s nitrogen balance indicates how well its tissues are being maintained. The intake and use of dietary protein is measured by the amount of nitrogen intake in food protein and the amount of nitrogen excreted in the urine. Positive Nitrogen Balance exists when the body takes in more nitrogen than it excretes, thus storing more nitrogen by building more tissue than it is losing. This situation occurs normally during periods of rapid growth. It can also occur with individuals who have been ill or malnourished and are being “built back up” with increased nourishment. Negative Nitrogen Balance When body takes in less nitrogen than it excretes. This means that the body has an inadequate protein intake and is losing nitrogen by breaking down more tissue than it is building up. This condition can be seen in situations of malnutrition and illness. Failure to maintain nitrogen balance may not become apparent for some time but eventually causes: loss of muscle tissue, impairment of body organs and functions, and increased susceptibility to infection. In children it causes growth retardation. Functions of Protein Primary Function: Tissue Building The primary functions of protein are: Protein is the fundamental structural material of every cell in the body. repair worn-out wasted, or The largest portion of the body is made up of protein. damaged tissue and Protein not only makes up the bulk of: the muscles, internal organs, brain, nerves, skin, hair, and nails, but is also a vital part of regulatory substances such as: enzymes, hormones, and blood plasma. build up new tissue Thus protein meets growth needs and maintains tissue health during adult years. Additional Body Functions Protein has other body functions relating to: energy, water balance, metabolism, and the body’s defense system Energy System: In times of need, protein may furnish additional body fuel to sustain body heat and energy, but this is a less efficient, backup source for use only when there is an insufficient supply of carbohydrate and fat. The available fuel factor of protein is 4 kcal/g. Water Balance Plasma protein, especially albumin helps control water balance throughout the body. Metabolism: Protein aids metabolic functions through enzymes, transport agents, and hormones. Controlling metabolic processes are the digestive and cell enzymes. Enzymes necessary for the digestion of carbohydrates, fats, and proteins. Proteins also act as the vehicle in which nutrients are carried throughout the body. Lipoproteins are necessary to transport fats in the water-soluble blood supply. (chylomicrons) Other proteins: hemoglobin (oxygen carrier), transferrin (iron transport), hormones: insulin and glucagon function in the metabolism of glucose Body Defense System Protein is used to build (lymphocytes) and antibodies as part of the body’s immune system to help defend against disease and infection. Food Sources Of Protein In a mixed diet, animal and plant foods provide a wide variety of many nutrients and proteins that supplement each other. The key to a balanced diet is variety. Food proteins are classified as complete or incomplete proteins, depending on their amino acid composition. Complete Proteins: Protein foods that contain all nine indispensable amino acids in sufficient quantity and ratio to meet the body’s needs are called complete proteins. These proteins are primarily of animal origin. Soybeans and soy products are exceptions. Soy products are the only plant sources of complete proteins. It Gelatin is not a complete protein. lacks three essential amino acids. The tasteless, odorless, brittle mixture of proteins, extracted by boiling pig skin and calf bones. Gelatin dissolves in hot water, forming a jellylike substance when cool and is used in preparation of various foods, medicine capsules, photographic film, etc. Incomplete Proteins Protein foods that are deficient in one or more of the nine indispensable amino acids are called incomplete proteins. These proteins are of plant origin (grains, legumes, nuts, seeds, vegetables, and fruits). Vegetarian Diets A mixture of plant proteins can provide adequate amount of amino acids when the basic use of various grains is expanded to include soy protein and other dried legume proteins such as beans and peas. This is the art of combining plant protein foods so that they “complement” one another and supply all nine indispensable amino acids. The underlying requirement for vegetarians, as for all people, is to eat a sufficient amount of varied foods to meet normal nutrient and energy needs. Review: Cultural Considerations Indispensable Amino Acids and Their Complementary Food Proteins Types of Vegetarian Diets 1. Lacto-ovo-vegetarians 2. Lacto-vegetarians 3. Ovo-vegetarians 4. Vegans Lacto-ovo-vegetarians: allows dairy products and eggs. Their mixed diet of plant and animal food sources, excluding only meat and fish, poses no nutritional problems. Types of Vegetarian Diets Lacto-vegetarians: accept Vegans: Follow a strict only dairy products from vegetarian diet and use no animal sources to animal foods. complement their basic The use of soybeans, soy milk, soybean curd diet of plant foods. (tofu) and processed Ovo-vegetarians: The only soy protein products enhances the nutritional animal foods included in value of the diet. this diet is eggs. Health Benefits and Risk The preventive mechanism at work in the vegetarian diet is the rich supply of: monounsaturated and polyunsaturated fatty acids, fiber, complex carbohydrates, antioxidants, and a restriction in saturated fat. Digestion of Protein: – The protein must be changed into amino acids by a process of mechanical and chemical digestion. – The mechanical breaking down of protein foods occurs by chewing in the mouth. Digestion of Proteins Stomach: A series of enzymes are necessary to break proteins into amino acids for absorption. All enzymes involved in protein digestion (proteases) are stored as inactive proenzymes called zymogens. Zymogens are then activated upon as needed. Chemical digestion of protein begins in the stomach. The stomach’s chief digestive function overall is the first stage in the enzymatic breakdown of protein. Digestion Of Protein – Cont’d Pepsin: It is the main gastric enzyme, specific to proteins. It is first produced as an inactive proenzyme, pepsinogen by the single layer of cells in the stomach wall. The hydrochloric acid within gastric juices then changes pepsinogen to the enzyme pepsin. The active pepsin begins splitting the links between the proteins’ amino acids, which changes the large amino acid chains that make up the protein into smaller short chains called peptides. Pepsin only completes the first stage of breakdown due to normal gastric emptying time. Digestion of Proteins Hydrochloric AcidProvides the acid medium necessary to convert pepsinogen to active pepsin. Begins the unfolding and denaturing of the complex protein chains. Rennin- (gastric enzyme) present only in infancy and childhood, especially important in the infant’s digestion of milk Small Intestine Protein digestion begins in the acidic medium of the stomach and is completed in the alkaline medium of the small intestine. Digestive enzymes from the pancreas and intestines take part. Small Intestine Pancreatic SecretionsThe following three enzymes from the pancreas continue to break down protein. 1. Trypsin : secreted as inactive trypsinogen is activated by the enzyme enterokinase. Enterokinase is secreted from the intestinal cells upon contact with food entering the duodenum, the first section of the small intestine. 2. Chymotrypsin: secreted first as the inactive chymotrypsinogen, is activated by trypsin already present 3. Carboxypeptidase: attacks the acid (carboxyl) end of the peptide chains, producing small peptides and some free amino acids Small Intestine Intestinal Secretions: To complete the breakdown and free the remaining amino acids the intestinal wall produces two more protein splitting enzymes: Aminopeptidase Dipeptidase Intestinal Secretions 1. Aminopeptidase attacks the nitrogencontaining (amino) end of the peptide chains and releases amino acids one at a time. Review Figure 45 Summary of Protein Digestion 2. Dipeptides completes the large task by breaking the remaining dipeptides into two free amino acids. The free amino acids are now ready to be absorbed directly into the portal blood circulation for use in building body tissues. Body Needs For Protein Protein requirementsThe following three factors influence our requirement for protein: – 1. tissue growth needs – 2. quality of the dietary protein – 3. additional needs owing to illness or disease Tissue Growth: During rapid growth periods, more protein is necessary to build new tissue and maintain present tissue. Human growth is most rapid during: fetal growth mother’s pregnancy, infant growth first years of life lactation needs of a breastfeeding mother, and adolescent growth and development into adulthood Illness or Disease An illness or disease especially with fever and increased tissue breakdown (catabolism) increases the body’s need for protein and kcalories for rebuilding tissue and to meet the demands of increased metabolic rate. After surgery, extra protein is needed for wound healing and restoring losses. Massive burns requires a large protein increase for the healing and grafting processes. Dietary Deficiency or Excess Protein-Energy Malnutrition- (PEM) The most severe cases are found in less industrialized countries where not only protein-rich foods are in short supply, but all foods are. Children are at the highest risk for developing PEM because of their elevated needs during rapid growth and development. Dietary Deficiency or Excess Persons with poor nutrient intake, such as the elderly or patients w/eating disorders, may suffer from PEM as well. Without the amino acids building blocks, the body cannot synthesize needed structural (muscle) or functional (enzymes, antibodies, hormones, etc.) proteins. Two severe forms of PEM are: Kwashiorkor Marasmus Protein-Energy Malnutrition Kwashiorkor: result from an acute deficiency of protein. It is common in children between 18 – 24 months who had been breastfeeding and then are rapidly weaned. They are switched from a nutritionally balanced breast milk to a diluted diet of mostly carbohydrates and little protein. They lack enough kcalories from protein sources. Characteristics include: edema in the feet and legs, a bloated abdomen, both from lack of protein in the blood to maintain fluid balance and transport fat away from the liver. Protein-Energy Malnutrition Marasmus: It is more likely to affect individuals of all ages, suffering from inadequate food sources. This is a chronic form of energy and protein deficiency which is basic starvation. Characteristics include: very emaciated appearance with little or no body fat stunted growth and development are even more severe with this form of PEM. Excess Dietary Intake The body has a finite need for protein. Once a person has met the dietary protein needs, additional protein is deaminated (the nitrogen is removed) and stored as fat or used as energy. Eating excess protein does not build muscle. The main problems with diets high in protein are: usually high in saturated fats- a risk for cardiovascular disease little room for fruits, vegetables, and other whole grains kidneys have to work overtime to rid the body of excess nitrogen Excess protein increases calcium losses in the bone when dietary calcium is inadequate Dietary Guides Children and adults should get 10% to 35% of their total caloric intake from protein. The RDA for both men and woman is set at 0.8 g of highquality protein per kg of desirable body weight per day. Example: The grams of protein required for an individual who weighs 150 lb ideal body weight would be? Answer: 54.4 g 150/2.2=68 kg 68 kg X 0.8 = 54.4 g The RDA is set to meet the nutritional requirements of most healthy people. Severe physical stress, such as illness, disease, and surgery can increase one’s needs for protein. Dietary Guidelines For Americans There are no known benefits in the consumption of a diet with a high animal protein content, which also carries added fat. The potential risks are related to: certain cancers, CAD, urinary calcium loss and kidney stones CRF The Dietary Guidelines for Americans recommend choosing foods from each of the five food groups based on the Food Guide Pyramid, consuming moderate amounts of foods from the meat and bean group. Moderate amounts equal two to three servings per day. QUESTIONS? Google and textbook images