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Amino Acid

Amino acids are organic compound, the building blocks of proteins.

  • All Essential Amino Acids

    An essential amino acid, or indispensable amino acid, is an amino acid that cannot be synthesized by the organism, and must be supplied in diet. 

    The 9 amino acids humans cannot synthesize (F V T W M L I K H):

    • phenylalanine
    • valine
    • threonine
    • tryptophan
    • methionine
    • leucine
    • isoleucine
    • lysine
    • histidine

    Animal and plant proteins are made up of about 20 common amino acids.

    Synthesis of 6 other amino acids - conditionally essential - can be limited under special conditions (R C G Q P Y)arginine, cysteine, glycine, glutamine, proline, and tyrosine.

    Dispensable amino acids can be synthesized in the human body, 5 (A D N E S): alanine, aspartic acid, asparagine, glutamic acid and serine .

  • Amino Acid Requirements for Adults

    Estimates of Amino Acid Requirements for adultsmg / kg per day

    • Phenylalanine + tyrosine: 14
    • Leucine: 14
    • Methionine + cystine13
    • Histidine: 8–12
    • Lysine: 12
    • Isoleucine: 10
    • Valine: 10
    • Threonine: 7
    • Tryptophan: 3.5

  • Amino Acids

    Protein plays a crucial role in almost all biological processes and amino acids are the building blocks of it.

    A large proportion of our cells, muscles and tissue is made up of amino acids - 20% Of the human body is made up of protein. 

    ~500 Amino acids are known, 20 appear in the genetic code, 9 are essential for humans because they cannot be created from other compounds by the human body, and must be taken from food.

    Amino acids carry out many important bodily functions: 

    • give cells their structure;
    • play a key role in the transport and the storage of nutrients;
    • have an influence on the function of organs, glands, tendons and arteries;
    • essential for healing wounds and repairing tissue; 
    • important removal of waste deposits.

  • Lysine Enhances Gluten

    Lysine was shown to enhance the nutritive value of gluten for humans. 

    The mean nitrogen balance index for gluten was 0.62. For gluten plus lysine, it was significantly higher, 0.76, approaching the value for casein.

  • Nitrogen Balance

    Nitrogen balance is a measure of nitrogen input minus nitrogen output

    Nitrogen Balance = Nitrogen intake - Nitrogen loss

    Nitrogen is a fundamental component of amino acids, which are the molecular building blocks of protein. Measuring nitrogen inputs and losses can be used to study protein metabolism. 

  • Phenylalanine

    Phenylalanine is an essential amino acid.

    Provided by diet, phenylalanine can be converted into another amino acid, tyrosine, in the body. Tyrosine is used to synthesize two key neurotransmitters that promote alertness: dopamine and norepinephrine. 

    It has 3 forms:

    • D-phenylalanine;
    • L-phenylalanine - most common, the form in which phenylalanine is incorporated into the body’s proteins;
    • DL-phenylalanine.

  • Plant Protein Balance

    Mixtures of plant proteins can serve as a complete and well-balanced source of amino acids for meeting human physiological requirements. 

    Plant protein foods contribute ~ 65% of the per capita supply of protein on a worldwide basis, and ~ 32% in the North American region.

  • Protein Digestibility-Corrected Amino Acid Score

    The protein digestibility-corrected amino acid score (PDCAAS) has been adopted by FAO/WHO as the preferred method for the measurement of the protein value in human nutrition. 

    PDCAAS = Amino Acid Score x Digestibility

    The method is based on comparison of the concentration of the first limiting essential amino acid in the test protein with the concentration of that amino acid in a reference (scoring) pattern. This scoring pattern is derived from the essential amino acid requirements of the preschool-age child.

    Although the principle of the PDCAAS method has been widely accepted, critical questions have been raised in the scientific community:

    1. the validity of the preschool-age child amino acid requirement values (more than 4 times greater than the EAA requirement for an adult),
    2. the validity of correction for fecal instead of ileal digestibility,
    3. the truncation of PDCAAS values to 100%.

    The reference scoring pattern was based on studies performed more than 25 years ago on a limited number of 2-year-old children recovering from malnutrition.

    According to the current official recommendations, a 2-year old child needs ~ 3x higher essential-to-non-essential amino acid ratio, and needs essential amino acids in different proportions than adult. Methionine/cysteine is the limiting essential amino acids for adults, and for children it is lysine or tryptophan.

    The use of fecal digestibility overestimates the nutritional value of a protein because amino acid nitrogen entering the colon is lost for protein synthesis in the body and is, at least in part, excreted in urine as ammonia.

Isaac Bashevis Singer

When a human kills an animal for food, he is neglecting his own hunger for justice. Man prays for mercy, but is unwilling to extend it to others. 

Protein Structure, Cooked and Denatured Proteins

Proteins are chains of amino acids. The sequence of amino acids in a chain is known as the primary structure of a protein. The chains fold up to form complex three dimensional shapes. The chains can fold on themselves locally (secondary structure) and wrap around themselves to form a specific three dimensional shape (tertiary structure).

The secondary / tertiary structure of a folded protein is directly related to its function. For example, enzymes are proteins that catalyze reactions. They have binding sites that interact with other molecules. These binding sites are created through the folding of the amino acid chains that gives rise to the three dimensional shape of the enzyme.

Denatured Protein

Denaturation of proteins involves the disruption and possible destruction of both the secondary and tertiary structures. Since denaturation reactions are not strong enough to break the peptide bonds, the primary structure (sequence of amino acids) remains the same after a denaturation process. Denaturation disrupts the normal sheets in a protein and uncoils it into a random shape.

Denaturation occurs because the bonding interactions responsible for the secondary structure (hydrogen bonds to amides) and tertiary structure are disrupted. In tertiary structure there are four types of bonding interactions between "side chains" including: hydrogen bonding, salt bridges, disulfide bonds, and non-polar hydrophobic interactions. which may be disrupted. 

Proteins can be denatured through exposure to heat or chemicals. Denatured proteins lose their three dimensional structure and thus their function. 

Digestion of Proteins and Cooking

Protein digestion begins in the stomach, where the acidic environment favors protein denaturation. Denatured proteins are more accessible as substrates for proteolysis than are native proteins. The primary proteolytic enzyme of the stomach is pepsin, a nonspecific protease that is maximally active at pH 2. Thus, pepsin can be active in the highly acidic environment of the stomach, even though other proteins undergo denaturation there.

Heat disrupts hydrogen bonds and non-polar hydrophobic interactions. This occurs because heat increases the kinetic energy and causes the molecules to vibrate so rapidly and violently that the bonds are disrupted

Foods are cooked to denature the proteins to make it easier for enzymes to digest them. Cooking food denatures some of the proteins in it and makes digestion more efficient. Heating to denature proteins in bacteria and thus destroy the bacteria.

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