NCM 105 NUTRITION AND DIET THERAPY By: Ray-Hannah G. Makakena, RND Instructor Nutrition and Dietetics Department First Semester, School Year 2020-2021
COURSE DESCRIPTION This course deals with the study of food in relation to health and illness. It covers nutrients and other substances and their action, interaction, and balance in relation to health and diseases and the process by which the human body ingests, digests, absorbs, transports, utilizes, and excrete food substances. It also focuses on the therapeutic and food service aspects of delivery of nutritional services in hospitals and other healthcare institutions. The learners are expected to develop the competencies in appropriate meal planning and education of a given client.
COURSE OUTLINE Protein: Classification Functions Food Sources Digestion, Absorption, and Utilization Individual Requirements and PDRI Effects of Excessive and Deficient Intakes
OBJECTIVES By the end of this class, the students will be able to: Describe the types and the classifications of proteins Identify functions of protein in the human body Name food sources of protein Explain the processes involved in the digestion, absorption, and utilization of protein in the body Estimate the individual requirements/PDRI of protein for each age group Predict the consequences of excessive and inadequate intakes of protein
THE MACRONUTRIENTS: PROTEIN By: Ray-Hannah G. Makakena , RND
Protein Originated from Greek word “ proteios ” meaning “to hold first place” or “is of prime importance. Amino acids- the building blocks of protein. Protein has 22 Amino acids.
Classifications 1. According to Essentiality Essential Semi-essential Non-essential 2.According to the Chemical Composition of Their Side Chains Basic Amino Acids Acidic Amino Acids Neutral Amino Acids Branched Chained Amino Acids 3.According to Hydrolytic Products and Sources 4.According to Structure and Spatial Arrangement of Amino Acids
ACCORDING TO ESSENTIALITY
Essential Amino Acids Is the one that cannot be synthesize by the body. They must be supplied ready-made or preformed in the diet. Essential Amino acids are: histidine, isoleucine, leucine, lysine, methionine, phenylalanine, threonine, trypthopan , valine
Semi-Essential Amino Acids Reduces the need for a particular Essential Amino Acids (EAA) or partially spares it. However, it cannot completely replace it. Semi-essential Amino Acids are: Arginine, Tyrosine, Cysteine, Glycine, Serine
Non-Essential Amino Acids Is not a dietary essential. It can be synthesized by the body as long as the materials for synthesis are adequate. Non-essential Amino Acids are: Glutamine, Glutamic Acid, Alanine, Aspartic Acid, Asparagine, Cystine , Proline, Citrulline , Homocysteine, Norleucine , Ornithine, Taurine, Hydroxyglycine , Hydroxyproline
ACCORDING TO THE CHEMICAL COMPOSITION OF THEIR SIDE CHAINS
1. Basic Amino Acids Those with additional amino acid group. Examples are lysine, arginine, histidine 2. Acidic Amino Acids Those that contain additional carboxyl group. Examples are: aspartic acid, glutamic acid
3. Neutral Amino Acids Those that contain additional acidic or basic group. Examples are: threonine, glycine, serine, alanine, tryptophan, phenylalanine, tyrosine 4. Branched-chain Amino Acids Are having aliphatic side-chains with a branch. Examples are: leucine, isoleucine, valine
ACCORDING TO HYDROLYTIC PRODUCTS AND SOURCES
Glucogenic – they follow CHO pathways in metabolism. Ketogenic- they are converted to ketone bodies like acetate
ACCORDING TO STRUCTURE AND SPATIAL ARRANGEMENT OF AMINO ACIDS
Fibrous Proteins Consists of long coiled/ folded chains of amino acids bound together in parallel line. Are insoluble in water and are able to provide support for cells and tissues. Examples: Keratin -chief protein of hair Collagen -connective tissue in tendons and bone matrices Fibrin -of a blood clot Myosin -of muscle Elastin -in blood vessel walls
Globular Proteins Coiled and tightly wounded and is relatively soluble in water. Examples: casein in milk, cheese, albumin in eggwhites
Classification of Protein and Sources 1. Simple Proteins -yield only amino acids on hydrolysis. Albumins Globulins Glutelins Prolamins Scleroproteins / Albuminolds
2. Conjugated Proteins -has “prosthetic” group. Nucleoproteins (protein combined with DNA found in chromosomes) Mucoproteins (with polysaccharides and occur in tissues and fluids) Lipoproteins (triglyceride and cholesterol needs to be transported with protein due to insoluble nature of these lipids) Chromoproteins (contains pigmented prosthetic group ex. Hemoglobin) Phosphoproteins Metalloproteins (contains metal) Flavoprotein (contain nucleic acid derivative of riboflavin)
3.Derived Protein -substances produced by partial hydrolysis A.Primary protein derivatives Proteins Metaproteins Coagulated proteins B.Secondary protein derivatives Proteoses Peptones Peptides
FUNCTIONS
General Functions Build and repair cells and tissues. Supply energy. Regulate body processes.
1.Body-building or Structural Role 20% of an adult body weight is protein. Protein is an integral part of cell nuclei and protoplasm. Solid mass of soft tissues like the vital organs, blood cells, and muscles are protein in nature.
All enzymes are protein and only some hormones are protein. All body fluids and secretions have protein, except bile. Antibodies contain protein.
2. Source of Energy One gram of protein supplies 4 calories. Adequate CHO and fat must be the primary sources of energy to save protein for its unique function of building and repairing tissues. Of the total caloric needs, 10-15% should be coming from protein.
3. Regulator of Body Processes Protein regulates osmotic pressure; hence helps maintain water balance and acid-base balance. If person has low plasma proteins, fluids accumulate between tissues resulting in edema. Protein transports substances (lipids, vitamins, minerals, and oxygen) around the body.
Digestion, Absorption, Utilization After protein is ingested, it passes through the gastrointestinal tract until the end-products (amino acids) are absorbed and circulated by the blood. The amino acids enters the metabolic pool and cells to perform various physiologic and structural roles.
General Principles of Protein Metabolism The amino acids are in a dynamic state. The All or None law applies in formation of cells and tissues. There is a limited number of amino acids that are labile ( easily altered). Synthesis of a particular protein is controlled by a genetic material (DNA and RNA). Protein metabolism is closely related with fat and CHO metabolism.
Protein Requirement and Allowance In the Philippines, 1.14 g/kg body weight for adults. In the USA, 0.9 g/kg is recommended. 10-15% of total caloric needs. Example: Total Caloric need= 1,890 Kcal 1,890 .15 (15%) = 283.5 kcal 283.5 kcal 4 kcal/gram (1 g of CHON=4 kcal) Protein Requirement=70.9/71 g/day
Effects of Excessive and Deficient Intakes
Effects of Deficient Intakes
Effects of Excessive Intakes The body is unable to store excess protein. Excess amino acids are converted to other usable molecules by the liver in the process of deamination. Deamination converts nitrogen from the amino acids into ammonia which is converted by the liver into urea in the urea cycle. Excretion of the urea is done by the kidneys.
SUMMARY Proteins are classified according to: Essentiality, the Chemical Composition of Their Side Chains, Hydrolytic Products and Sources, and Structure and Spatial Arrangement of Amino Acids. Deficiency will cause PEM. The functions are: build and repair cells and tissues , supply energy, and regulate body processes.
REFERENCES Basic Nutrition for Filipinos 6 th Edition by Adela Jamorabo -Ruiz and Virginia Serraon Claudio