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Protein milkshakes, made from protein powder (center) and milk (left), are a common bodybuilding supplement.

Proteins are broken down in the stomach during digestion by enzymes known as proteases into smaller polypeptides to provide amino acids for the organism, including the essential amino acids that the organism cannot biosynthesize itself. Aside from their role in protein synthesis, amino acids are also important nutritional sources of nitrogen.

Proteins, like carbohydrates, contain 16.8 kilojoules (4 kilocalories) per gram as opposed to lipids which contain 37.8 kilojoules (9 kilocalories) and alcohols which contain 29.4 kilojoules (7 kilocalories). The liver, and to a much lesser extent the kidneys, can convert amino acids used by cells in protein biosynthesis into glucose by a process known as gluconeogenesis. The amino acids leucine and lysine are exceptions.

Sources

Dietary sources of protein include meats, eggs, nuts, grains, legumes, and dairy products such as milk and cheese.[1] Of the 20 amino acids used by humans in protein synthesis, 11 "nonessential" amino acids can be synthesized in sufficient quantities by the adult body, and are not required in the diet (though there are exceptions for some in special cases). The nine essential amino acids[2], plus arginine for the young[3], cannot be created by the body and must come from dietary sources.

Most animal sources and certain vegetable sources have the complete complement of all the essential amino acids in adequate proportions. However, it is not necessary to consume a single food source that contains all the essential amino acids, as long as all the essential amino acids are eventually present in the diet: see complete protein and protein combining.

Quality

Different proteins have different levels of biological availability (BA) to the human body. Many methods have been introduced to measure protein utilization and retention rates in humans. They include biological value, net protein utilization, and PDCAAS (Protein Digestibility Corrected Amino Acids Score) which was developed by the FDA as an improvement over the Protein Efficiency Ratio (PER) method. These methods examine which proteins are most efficiently used by the body. In general they conclude that animal complete proteins that contain all the essential amino acids such as milk, eggs, and meat are of most value to the body.[4]

Egg whites have been determined to have the standard biological value of 100 (though some sources may have biological values higher), which means that most of the absorbed nitrogen from egg white protein can be retained and used by the body. The biological value of plant protein sources is usually considerably lower than animal sources.[4] For example, corn has a BA of 70 while peanuts have a relatively low BA of 40.[5]

Digestion

Digestion typically begins in the stomach when pepsinogen is converted to pepsin by the action of hydrochloric acid, and continued by trypsin and chymotrypsin in the intestine. The amino acids and their derivatives into which dietary protein is degraded are then absorbed by the gastrointestinal tract. The absorption rates of individual amino acids are highly dependent on the protein source; for example, the digestibilities of many amino acids in humans differ between soy and milk proteins[6] and between individual milk proteins, beta-lactoglobulin and casein.[7] For milk proteins, about 50% of the ingested protein is absorbed between the stomach and the jejunum and 90% is absorbed by the time the digested food reaches the ileum.[8] Biological value (BV) is a measure of the proportion of absorbed protein from a food which becomes incorporated into the proteins of the organism's body.

Dietary requirements

According to the recently updated US/Canadian Dietary Reference Intake guidelines, women aged 19–70 need to consume 46 grams of protein per day, while men aged 19–70 need to consume 56 grams of protein per day to avoid a deficiency.[9] The difference is because men's bodies generally have more muscle mass than those of women, or this may be attributed to weight difference by taking 0.8 g(of protein)/kg of healthy body weight.

Because the body is continually breaking down protein from tissues, even adults who do not fall into the above categories need to include adequate protein in their diet every day. If enough energy is not taken in through diet, as in the process of starvation, the body will use protein from the muscle mass to meet its energy needs, leading to muscle wasting over time. If the individual does not consume adequate protein in nutrition, then muscle will also waste as more vital cellular processes (e.g. respiration enzymes, blood cells) recycle muscle protein for their own requirements.

Other recommendations suggest 0.8 gram of protein per kilogram of healthy bodyweight per day while other sources suggest that higher intakes of 1-1.4 grams of protein per kilogram of bodyweight for enhanced athletes or those with a large muscle mass.[10]

How much protein needed in a person's daily diet is determined in large part by overall energy intake, as well as by the body's need for nitrogen and essential amino acids. Physical activity and exertion as well as enhanced muscular mass increase the need for protein. Requirements are also greater during childhood for growth and development, during pregnancy or when breast-feeding in order to nourish a baby, or when the body needs to recover from malnutrition or trauma or after an operation.[11]

Deficiency

In developing countries

Protein deficiency is a serious cause of ill health and death in developing countries. Protein deficiency plays a part in the disease kwashiorkor. War, famine, overpopulation and other factors can increase rates of malnutrition and protein deficiency. Protein deficiency can lead to reduced intelligence or mental retardation, see deficiency in proteins, fats, carbohydrates.

In countries that suffer from widespread protein deficiency, food is generally full of plant fibers, which makes adequate energy and protein consumption very difficult. Protein deficiency is generally caused by lack of total joules, making it an issue of not getting food in total. Symptoms of kwashiorkor include apathy, diarrhea, inactivity, failure to grow, flaky skin, fatty liver, and edema of the belly and legs. This edema is explained by the normal functioning of proteins in fluid balance and lipoprotein transport. [12]

Dr. Latham, director of the Program in International Nutrition at Cornell University claims that malnutrition is a frequent cause of death and disease in third world countries. Protein-energy malnutrition (PEM) affects 500 million people and kills 10 million annually. In severe cases white blood cell numbers decline and the ability of leukocytes to fight infection decreases.[citation needed]

In developed countries

Protein deficiency is relatively rare in developed countries but some people have difficulty getting sufficient protein due to poverty. Protein deficiency can also occur in developed countries in people who are dieting or crash dieting to lose weight, or in older adults, who may have a poor diet. Convalescent people recovering from surgery, trauma, or illness may become protein deficient if they do not increase their intake to support their increased needs. Bob Lanier, a biology professor at Jesuit College Preparatory School of Dallas claims in his Discourse on Minorities in Developed Countries that protein deficiency is more common today than statistics might reveal. Lanier provides a variety of data and connects widespread protein deficiency among low income minority families to explain poor academic performance.

Excess consumption

The body is unable to store excess protein. Protein is digested into amino acids which enter the bloodstream. Excess amino acids are converted to other usable molecules by the liver in a process called deamination. Deamination converts nitrogen from the amino acid into ammonia which is converted by the liver into urea in the urea cycle. Excretion of urea is performed by the kidneys. These organs can normally cope with any extra workload but if kidney disease occurs, a decrease in protein will often be prescribed.[13][citation needed]

Many researchers think excessive intake of protein forces increased calcium excretion. If there is to be excessive intake of protein, it is thought that a regular intake of calcium would be able to stabilize, or even increase the uptake of calcium by the small intestine, which would be more beneficial in older women.[14]

Specific proteins are often the cause of allergies and allergic reactions to certain foods. This is because the structure of each form of protein is slightly different; some may trigger a response from the immune system while others remain perfectly safe. Many people are allergic to casein, the protein in milk; gluten, the protein in wheat and other grains; the particular proteins found in peanuts; or those in shellfish or other seafoods. [citation needed]

Testing in foods

The classic assay for protein concentration in food is the Kjeldahl method. This test determines the total nitrogen in a sample. The only major component of most food which contains nitrogen is protein (fat, carbohydrate and dietary fibre do not contain nitrogen). If the amount of nitrogen is multiplied by a factor depending on the kinds of protein expected in the food the total protein can be determined. On food labels the protein is given by the nitrogen multiplied by 6.25, because the average nitrogen content of proteins is about 16%. The Kjeldahl test is used because it is the method the AOAC International has adopted and is therefore used by many food standards agencies around the world.

The limitations of the Kjeldahl method were at the heart of the Chinese protein export contamination in 2007 and the 2008 Chinese Milk Scandal in which the industrial chemical melamine was added to the milk or glutens to increase the measured "protein".[15]

See also

References

  1. ^ USDA National Nutrient Database for Standard Reference, Release 20, United States Department of Agriculture. Last modified on September 26, 2007.
  2. ^ World Health Organization, Food and Agriculture Organization of the United Nations , United Nations University (2007). "Protein and amino acid requirements in human nutrition" (PDF). WHO Press. Retrieved 2008-07-08. The indispensable amino acids are leucine, isoleucine, valine, lysine, threonine, tryptophan, methionine, phenylalanine and histidine. Histidine is considered to be an indispensable amino acid because of the detrimental effects on haemoglobin concentrations that have been observed when individuals are fed histidine-free diets.{{cite web}}: CS1 maint: multiple names: authors list (link)
  3. ^ "Amino acids". Department of Biochemistry and Molecular Biophysics, University of Arizona. Retrieved 2008-07-08.
  4. ^ a b Protein Quality Comparison Chart. Retrieved from the Whey Protein Institute on 2008-05-24. [dubious ]
  5. ^ Wardlaw GM (2006). Perspectives in nutrition. Boston: McGraw-Hill Higher Education. pp. 259, 260. ISBN 0-07-282750-5.
  6. ^ Gaudichon C, Bos C, Morens C, Petzke KJ, Mariotti F, Everwand J, Benamouzig R, Dare S, Tome D, Metges CC (2002). "Ileal losses of nitrogen and amino acids in humans and their importance to the assessment of amino acid requirements". Gastroenterology. 123 (1): 50–9. doi:10.1053/gast.2002.34233.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  7. ^ Mahe S, Roos N, Benamouzig R, Davin L, Luengo C, Gagnon L, Gausserges N, Rautureau J, Tome D (1996). "Gastrojejunal kinetics and the digestion of [15N]beta-lactoglobulin and casein in humans: the influence of the nature and quantity of the protein". Am J Clin Nutr. 63 (4): 546–52.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  8. ^ Mahe S, Marteau P, Huneau JF, Thuillier F, Tome D (1994). "Intestinal nitrogen and electrolyte movements following fermented milk ingestion in man". Br J Nutr. 71 (2): 169–80. doi:10.1079/BJN19940124.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  9. ^ "Dietary reference intakes: macronutrients" (PDF). Institute of Medicine. Retrieved 2008-05-18.
  10. ^ Tarnopolsky MA, Atkinson SA, MacDougall JD, Chesley A, Phillips S, Schwarcz HP (1992). "Evaluation of protein requirements for trained strength athletes". Journal of Applied Physiology. 73 (5): 1986–95. PMID 1474076. {{cite journal}}: Unknown parameter |month= ignored (help)CS1 maint: multiple names: authors list (link)
  11. ^ World Health Organization, Food and Agriculture Organization of the United Nations , United Nations University (2007). "Protein and amino acid requirements in human nutrition" (PDF). WHO Press. Retrieved 2008-07-08.{{cite web}}: CS1 maint: multiple names: authors list (link)
  12. ^ Jeffery Schwartz; Bryant, Carol A.; DeWalt, Kathleen Musante; Anita Courtney (2003). The cultural feast: an introduction to food and society. Belmont, California: Thomson/Wadsworth. pp. 282, 283. ISBN 0-534-52582-2.{{cite book}}: CS1 maint: multiple names: authors list (link)
  13. ^ Born Steve. "Fueling for endurance: ten mistakes endurance athletes make and how you can avoid them". UltraCycling Magazine.
  14. ^ Kerstetter JE, O'Brien KO, Caseria DM, Wall DE, Insogna KL (2005). "The impact of dietary protein on calcium absorption and kinetic measures of bone turnover in women". J Clin Endocrinol Metab. 90: 26–31. doi:10.1210/jc.2004-0179. PMID 15546911.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  15. ^ Stephen Chen (18 September 2008). "Melamine - an industry staple". South China Morning Post. pp. Page A2.

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