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PDCAAS
Protein digestibility-corrected amino acid score (PDCAAS) is a method of evaluating the protein quality, quality of a protein based on both the amino acid requirements of humans and their ability to digest it. The PDCAAS rating was adopted by the US FDA and the Food and Agriculture Organization, Food and Agriculture Organization of the United Nations/World Health Organization (FAO/WHO) in 1993 as "the preferred 'best'" method to determine protein (nutrient), protein quality. In 2013, FAO proposed changing to Digestible Indispensable Amino Acid Score. Methodology Using the PDCAAS method, the protein quality rankings are determined by comparing the amino acid profile of the specific food protein against a standard amino acid profile with the highest possible score being a 1.0. This score means, after digestion of the protein, it provides per unit of protein 100% or more of the Essential amino acid, indispensable amino acids required. The formula for calculating the PDCAAS percentage ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Protein Quality
Protein quality is the digestibility and quantity of essential amino acids for providing the proteins in correct ratios for human consumption. There are various methods that rank the quality of different types of protein, some of which are outdated and no longer in use, or not considered as useful as they once were thought to be. The Protein Digestibility Corrected Amino Acid Score (PDCAAS), which was recommended by the Food and Agriculture Organization of the United Nations (FAO), became the industry standard in 1993. FAO has recently recommended the newer Digestible Indispensable Amino Acid Score (DIAAS) to supersede PDCAAS. The dairy industry is in favor of this, because while PDCAAS truncates all protein types that exceed the essential amino acid (EAA) requirements to 1.0, DIAAS allows a higher than 1.0 ranking: while for example both soy protein isolate and whey isolate are ranked 1.0 according to PDCAAS, in the DIAAS system, whey has a higher score than soy. PDCAAS versus DIAA ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Digestible Indispensable Amino Acid Score
Digestible Indispensable Amino Acid Score (DIAAS) is a protein quality method proposed in March 2013 by the Food and Agriculture Organization to replace the current protein ranking standard, the Protein Digestibility Corrected Amino Acid Score (PDCAAS). The DIAAS accounts for amino acid digestibility at the end of the small intestine, providing a more accurate measure of the amounts of amino acids absorbed by the body and the protein’s contribution to human amino acid and nitrogen requirements. This is in contrast to the PDCAAS, which is based on an estimate of digestibility over the total digestive tract. Values stated using this method generally overestimate the amount of amino acids absorbed. Reference pattern Amino acid requirements were determined in two parts. The amino acid distribution of breast milk was used for the 0 to 6 month age range, and existing amino acid data was used for older ages after adjustment for digestibility. The reference amino acid requirements are pr ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Protein Efficiency Ratio
Protein efficiency ratio (PER) is based on the weight gain of a test subject divided by its intake of a particular food protein during the test period. From 1919 until very recently, the PER had been a widely used method for evaluating the quality of protein in food. The food industry in Canada currently uses the PER as the standard for evaluating the protein quality of foods. The official method for determining the protein efficiency ratio is from Health Canada's Health Protection Branch Method FO-1, October 15, 1981. The U.S. Food and Drug Administration now uses the Protein Digestibility Corrected Amino Acid Score (PDCAAS) as the basis for the percent of the U.S. recommended daily allowance (USRDA) for protein shown on food labels. However, the PER is still used in certain FDA regulations. The US FDA official methods to calculate the PER are as stated in the Official Methods of Analysis of AOAC International, 16th ed. (1995) Section 45.3.05, AOAC Official Method 982.30 Protein E ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Protein (nutrient)
Proteins are essential nutrients for the human body. They are one of the building blocks of body tissue and can also serve as a fuel source. As a fuel, proteins provide as much energy density as carbohydrates: 4 kcal (17 kJ) per gram; in contrast, lipids provide 9 kcal (37 kJ) per gram. The most important aspect and defining characteristic of protein from a nutritional standpoint is its amino acid composition. Proteins are polymer chains made of amino acids linked together by peptide bonds. During human digestion, proteins are broken down in the stomach to smaller polypeptide chains via hydrochloric acid and protease actions. This is crucial for the absorption of the essential amino acids that cannot be biosynthesized by the body. There are nine essential amino acids which humans must obtain from their diet in order to prevent protein–energy malnutrition and resulting death. They are phenylalanine, valine, threonine, tryptophan, methionine, leucine, isoleucine, lysine, an ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Protein Combining
Protein combining or protein complementing is a dietary theory for protein nutrition that purports to optimize the biological value of protein intake. According to the theory, vegetarian and vegan diets may provide an insufficient amount of some essential amino acids, making protein combining with multiple foods necessary to obtain a complete protein food. The terms ''complete'' and ''incomplete'' are outdated in relation to plant protein. The position of the Academy of Nutrition and Dietetics is that protein from a variety of plant foods eaten during the course of a day supplies enough of all essential amino acids when caloric requirements are met. Though it is undisputed that diverse foods can be combined to make up for their respective limiting amino acids, a general consensus has emerged among nutrition scientists and writers contrary to the original vegetarian nutrition dogmas of the 1970s. Though historically, protein combining was promoted as a method of compensating for s ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Essential Amino Acid
An essential amino acid, or indispensable amino acid, is an amino acid that cannot be synthesized from scratch by the organism fast enough to supply its demand, and must therefore come from the diet. Of the 21 amino acids common to all life forms, the nine amino acids humans cannot synthesize are phenylalanine, valine, threonine, tryptophan, methionine, leucine, isoleucine, lysine, and histidine. Six other amino acids are considered conditionally essential in the human diet, meaning their synthesis can be limited under special pathophysiological conditions, such as prematurity in the infant or individuals in severe catabolic distress. These six are arginine, cysteine, glycine, glutamine, proline, and tyrosine. Six amino acids are non-essential (dispensable) in humans, meaning they can be synthesized in sufficient quantities in the body. These six are alanine, aspartic acid, asparagine, glutamic acid, serine, and selenocysteine (considered the 21st amino acid). Pyrrolysine (consi ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Limiting Amino Acid
An essential amino acid, or indispensable amino acid, is an amino acid that cannot be synthesized from scratch by the organism fast enough to supply its demand, and must therefore come from the diet. Of the 21 amino acids common to all life forms, the nine amino acids humans cannot synthesize are phenylalanine, valine, threonine, tryptophan, methionine, leucine, isoleucine, lysine, and histidine. Six other amino acids are considered conditionally essential in the human diet, meaning their synthesis can be limited under special pathophysiological conditions, such as prematurity in the infant or individuals in severe catabolic distress. These six are arginine, cysteine, glycine, glutamine, proline, and tyrosine. Six amino acids are non-essential (dispensable) in humans, meaning they can be synthesized in sufficient quantities in the body. These six are alanine, aspartic acid, asparagine, glutamic acid, serine, and selenocysteine (considered the 21st amino acid). Pyrrolysine (consid ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Leucine
Leucine (symbol Leu or L) is an essential amino acid that is used in the biosynthesis of proteins. Leucine is an α-amino acid, meaning it contains an α-amino group (which is in the protonated −NH3+ form under biological conditions), an α- carboxylic acid group (which is in the deprotonated −COO− form under biological conditions), and a side chain isobutyl group, making it a non-polar aliphatic amino acid. It is essential in humans, meaning the body cannot synthesize it: it must be obtained from the diet. Human dietary sources are foods that contain protein, such as meats, dairy products, soy products, and beans and other legumes. It is encoded by the codons UUA, UUG, CUU, CUC, CUA, and CUG. Like valine and isoleucine, leucine is a branched-chain amino acid. The primary metabolic end products of leucine metabolism are acetyl-CoA and acetoacetate; consequently, it is one of the two exclusively ketogenic amino acids, with lysine being the other. It is the most import ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Lysine
Lysine (symbol Lys or K) is an α-amino acid that is a precursor to many proteins. It contains an α-amino group (which is in the protonated form under biological conditions), an α-carboxylic acid group (which is in the deprotonated −COO− form under biological conditions), and a side chain lysyl ((CH2)4NH2), classifying it as a basic, charged (at physiological pH), aliphatic amino acid. It is encoded by the codons AAA and AAG. Like almost all other amino acids, the α-carbon is chiral and lysine may refer to either enantiomer or a racemic mixture of both. For the purpose of this article, lysine will refer to the biologically active enantiomer L-lysine, where the α-carbon is in the ''S'' configuration. The human body cannot synthesize lysine. It is essential in humans and must therefore be obtained from the diet. In organisms that synthesise lysine, two main biosynthetic pathways exist, the diaminopimelate and α-aminoadipate pathways, which employ distinct e ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Bean
A bean is the seed of several plants in the family Fabaceae, which are used as vegetables for human or animal food. They can be cooked in many different ways, including boiling, frying, and baking, and are used in many traditional dishes throughout the world. Terminology The word "bean" and its Germanic cognates (e.g. German '' Bohne'') have existed in common use in West Germanic languages since before the 12th century, referring to broad beans, chickpeas, and other pod-borne seeds. This was long before the New World genus '' Phaseolus'' was known in Europe. After Columbian-era contact between Europe and the Americas, use of the word was extended to pod-borne seeds of ''Phaseolus'', such as the common bean and the runner bean, and the related genus ''Vigna''. The term has long been applied generally to many other seeds of similar form, such as Old World soybeans, peas, other vetches, and lupins, and even to those with slighter resemblances, such as coffee beans, vanilla ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Methionine
Methionine (symbol Met or M) () is an essential amino acid in humans. As the precursor of other amino acids such as cysteine and taurine, versatile compounds such as SAM-e, and the important antioxidant glutathione, methionine plays a critical role in the metabolism and health of many species, including humans. It is encoded by the codon AUG. Methionine is also an important part of angiogenesis, the growth of new blood vessels. Supplementation may benefit those suffering from copper poisoning. Overconsumption of methionine, the methyl group donor in DNA methylation, is related to cancer growth in a number of studies. Methionine was first isolated in 1921 by John Howard Mueller. Biochemical details Methionine (abbreviated as Met or M; encoded by the codon AUG) is an α-amino acid that is used in the biosynthesis of proteins. It contains a carboxyl group (which is in the deprotonated −COO− form under biological pH conditions), an amino group (which is in the protonated fo ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Isoleucine
Isoleucine (symbol Ile or I) is an α-amino acid that is used in the biosynthesis of proteins. It contains an α-amino group (which is in the protonated −NH form under biological conditions), an α-carboxylic acid group (which is in the deprotonated −COO form under biological conditions), and a hydrocarbon side chain with a branch (a central carbon atom bound to three other carbon atoms). It is classified as a non-polar, uncharged (at physiological pH), branched-chain, aliphatic amino acid. It is essential in humans, meaning the body cannot synthesize it, and must be ingested in our diet. Isoleucine is synthesized from pyruvate employing leucine biosynthesis enzymes in other organisms such as bacteria. It is encoded by the codons AUU, AUC, and AUA. Metabolism Biosynthesis As an essential nutrient, it is not synthesized in the body, hence it must be ingested, usually as a component of proteins. In plants and microorganisms, it is synthesized via several steps, startin ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
