Proteins

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Essential Amino Acids

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they must be obtained from foods. The body cannot make the carbon skeleton of the amino acid, cannot attach an amino group to the carbon skeleton, or cannot od the whole process fast enough to meet the body's needs.

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Nonessential amino acids

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11 of the amino acids are not necessary to receive from food as we can synthesize them.

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Conditional essential amino acids

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these are several nonessential amino acids that can be classified as this because during certain stages of life higher levels are required than normal.

Infancy, disease, or trauma.

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Transamination

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Nonessential amino acids can be synthesized through this process. Transamination involves the transfer of an amino group from 1 amino acid to a carbon skeleton to form a new amino acid.

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Deamination

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Losing an amino group from 1 amino acid without transferring it to another carbon skeleton.

Once an amino acid breaks down to its amino-free carbon skeleton it can be used for energy or synthesized into other compound (Glucose)

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Urea

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nitrogenous waste product of protein metabolism and the major source of nitrogen in the urine

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pool

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amount of nutrient found within the body that can be easily mobilized when needed

cells require a pool of essential amino acids for the synthesis of body proteins

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limiting amino acid

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the essential amino acid in smallest supply in a food or diet in relation to body needs

it limits the amount of protein the body can synthesize.

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complementary proteins

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when 2 or more plant proteins are combined to compensate for deficiencies in essential amino acid content in each protein. When complementary protein sources are combined the amino acids in one source can make up for the limiting amino acid in the other sources to yield a high-quality protein for the diet.

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Peptide Bonds

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bonds between the amino group and carboxyl group of amino acids

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Denaturation

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Alteration of a protein's 3-D structure

caused by exposure to acid or alkaline solution, enzymes, heat or agitation

this often destroys its normal biological function

can be beneficial as well as harmful

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Sources of Protein

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Proteins and amino acids are supplied by the diet as well as by the recycling and utilization of amino acids released during the breakdown of body proteins.

Dietary protein is also necessary for protein synthesis and repair. This includes meat, poultry, fish, milk, cheese, legumes, and nuts.

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Evalutation of Food protein quality

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these measures indicate a food protein's ability to support body growth and maintenance. Protein quality is determined primarily by the food's digestibility ( amount of amino acids absorbed) and the amino acid composition compared with a reference protein that provides the essential amino acid in amounts needed to support growth.

digestibility of animal proteins is relatively high compared to plant proteins

Only is accurate when protein intake is equal or less than the amount of protein needed to meet the requirement for essential amino acids. If its above then the remaining amino acids are degraded for use as energy

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Biological Value (BV)

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the measure of how efficiently the absorbed food protein is converted into body tissue protein. IF a food possesses adequate amounts of all 9 essential amino acids, it should allow a person to efficiently incorporate amino acids from food protein into body protein.

most animal proteins have high BV

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Protein efficiency ratio (PER)

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assess a food's protein quality. IT compares the amount of weight gain by a growing laborator animal consuming a standardized amount of protein being studied with the weight gain by an animal consuming a standardized amount of reference protein.

weight gain and growth measured in the PER are dependent on the incorporation of food protein into body tissue.

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Chemical Score

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a way to evaluate a foods protein quality

the amount of each essential amino acid in a gram of the food protein being tested is divided by the ideal amount for that amino acid in a gram of the reference protein

0-1 scale

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Protein Digestibility Corrected Amino Acid Score (PDCAAS)

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measures protein quality

multiply a foods chemical score by its digestibility.

0-1

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Recommended intakes of protein

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10 -35% of total calories from protein

nitrogen x 6.25 = protein

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Dietary Reference Intakes for Protein

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0.8 g/ kg body weight

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Protein Digestion and Absorption

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1. cooking

2. pepsin produced by stomach breaks down long polypeptide chains into shorter chains of amino acids through hydrolysis rxn. Controlled by hormone gastrin

3. Becomes chyme and moves into the duodenum tiggers CCK. Causes the pancreas to release protease, chymotrypsin, and carboxypeptidase into small intestine. Digest the polypeptides into short peptides and amino acids that are absorbed into the cells.

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Proteins functions

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1. provide structural support to body cells and tissues - collagen, actin, and myosin

2. maintain fluid balance- normal blood pressure in the arteries forces blood into capillary beds. proteins in capillary beds attracts the right amount of fluid back to the blood

3, Contributing to acid-base balance- protein pump chemical ions in and out of cells. they act as buffers.

4. Forming hormones, enzymes, and neurotransmitters

5. Contributing to immune functions- antibody proteins they bind to antigens (invader proteins) and prevent their attack on target cells

6. Transporting Nutrients - carry them from bloodstream to cells and across cell membranes to sites of action

7. Forming Glucose

8. Providing Energy - 4 kcal/g

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Capillary beds

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minute blood vessels, that create a junction between arterial and venous circulation. Gas and nutrient exchange occurs here between body cells and blood.

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Edema

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when protein consumption is inadequate the concentration of proteins in the blood eventually decreases. Excess fluid builds up in surrounding tissue. The tissues sweel causing edema

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Anergy

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Lack of an immune response to foreign compounds entering the body

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Protein- Energy Malnutrition

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condition resulting from insufficient amounts of energy and protein, which eventually result in body wasting and an increased susceptibility to infection and disease.

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Marasmus

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Develops slowly from a severe deficiency fo energy ( protein and micronutrients)

over time leads to extreme weight loss, muscle, and fat loss, and growth impairment.

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Kwashiorkor

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occurs more rapidly in response to a severe protein deficit, typically accompanied by underlying infection or disease.

Characterized by edema, moderate weight loss, growth impairment, and the development of a fatty liver

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High-Protein Diets

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protein intake not exceed 35% of energy intake anything exceeding does not benefit it may in fact cause more risks.

Kidneys are main concern as a high protein diet may overburden its capacity to excrete nitrogen waste.

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allergen

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components typically proteins that induce a hypersensitive response, with excess production of certain immune system antibodies. Subsequent exposure to the same protein leads to allergic symptoms.

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immunoglubulins

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proteins also called antibodies in the blood that are responsible for identifying and neutralizing antigens as well as pathogens that bind specifically to antigens.

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Anaphylaxix

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exposure to the allergenic food may cause a generalized life-threatening reaction involving all body systems.