All about fruitarianism with a long-term fruitarian, Lena

Nutrients

Nutrients are component in foods that an organism uses for maintenance and growth.

  • 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.

  • 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 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.

  • 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. 

  • 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.

  • Gluten is Digestible by Healthy People

    Depending on which measurement system they used, wheat gluten protein was 80-100% digestible by (healthy) humans.

  • Gluten and Other Proteins in Grains

    Based on what is currently known, it's a big leap to attributing autism and other problems to gluten, and an even bigger one to prescribing gluten-free eating as a treatment. It's possible that some people benefit from a gluten-free regimen for reasons that have less to do with gluten and much more to do with the structure involved in planning and sticking to such a strict eating plan.

    In the context of celiac disease, gluten refers to the protein of grains capable of provoking an autoimmune response. Other grains also contain protein, but wheat, barley, rye, and spelt contain varieties that aren't broken down by digestive enzymes:

    • in wheat, the difficult-to-digest protein is gliadin;
    • in rye- secalin; 
    • in barley - hordein.

    In people with celiac disease, when they get absorbed into the walls of the small intestine, the immune system misreads the situation, views them as intruders, and unleashes a furious inflammatory response that damages tissue. 

  • Drink Water to Satisfy Thirst

    The latest recommendations say that we no longer need to worry about drinking specific amounts of water. Instead, we can simply satisfy our thirst with any beverage. As it turns out, there really was no scientific evidence for the 64-ounce daily recommendation that was based on survey data of usual consumption.

    The new guidelines remove the eight-glasses-a-day recommendation, and say healthy adults may use thirst to determine their fluid needs. Exceptions to this rule include anyone with a medical condition requiring fluid control; athletes; and people taking part in prolonged physical activities or whose living conditions are extreme."

  • Vitamins B12, B9, B6 and Heart Disease

    Vitamin B9 (folate, folic acid) works with vitamins B6 and B12 (cobalamin) and other nutrients to control blood levels of the amino acidhomocysteine. 

    Elevated homocysteine levels in blood are a risk factor for cardiovascular disease. Although B vitamin supplementation has been proven effective to control homocysteine levels, current data from intervention trials have not shown that lowering homocysteine levels decreases cardiovascular disease risk. Researchers are not sure whether homocysteine is a cause of heart disease or just a marker that indicates someone may have heart disease.

  • Choline Recommended Intake from Seeds and Fruits

    Choline is an essential vitamin-like (vitamin B4) nutrient, synthesized in human body, but not sufficiently.

    The recommended adequate intake (AI) of choline is set at 425 milligrams (mg)/day for women and 550 mg/day for men.

    Choline deficiency causes muscle damage and abnormal deposition of fat in the liver, which results in a condition called nonalcoholic fatty liver disease. Genetic predispositions and gender can influence individual variation in choline requirements.

    Example Plant Fruitarian Sources of Choline

    Seeds (including legumes and nuts), high in choline, milligrams per 100 g portion: 

    • Soybeans - 124 mg 
    • Lima beans - 97 mg 
    • Lentils - 96 mg
    • Peas (mature) - 96 mg
    • Flaxseeds - 79 mg 
    • Pistachio nuts - 71 mg 
    • Quinoa - 70 mg 
    • Pumpkin and squash seed kernels (pepitas) -  63 mg 
    • Cashew nuts - 61 mg 
    • Pine nuts - 56 mg 
    • Sunflower seed kernels - 55 mg 
    • Buckwheat - 54 mg 
    • Almonds - 52 mg 

    Fruits, high in choline, milligrams per 100 g portion: 

    • Tomatoes, sun-dried - 105 mg 
    • Apples - 18 mg 
    • Figs - 16 mg 
    • Avocados - 14 mg 

Albert Einstein

If people are good only because they fear punishment, then we are a sorry lot indeed. 

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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