Healthy Energy (Part 1 – the basics) « Mark Spilmon’s Weblog

Healthy Energy (Part 1 – the basics)

A few days back, I blogged on why I liked the 5 hour energy drink. I would now like to blog a little on what things I’ve found that contribute to your body’s energy and why. I am only passing on the research I’ve done to reach my own concultions on what I should and shouldn’t take to boost my energy. I’m in no way qualified to tell you what is good for you, and it is only hoped that this information maybe handy as part of considering whether you what you should and shouldn’t do to boost your energy. Please remember to treat all things as if they may be harmful to you, and do your own research as well.

“Energy is defined as the ability to do work, and metabolism represents the biochemical reactions that a cell can perform to produce energy.”

The main sources of chemical energy for most organisms are carbohydrates, fats, and protein. Energy content is expressed in calories or joules. The nutritional calorie, or kilocalorie (kcal), in foodstuffs is equivalent to 1000 calories. The energy content per gram of carbohydrate is 4 kcal (16 J); protein, 4 kcal (16 J); and fat, 9 kcal (36 J). The metabolism of foodstuffs yields chemical energy and heat.

Source: http://www.answers.com/topic/energy-metabolism?cat=technology

“Metabolism is the set of chemical reactions that occur in living organisms in order to maintain life.”

Source: http://en.wikipedia.org/wiki/Metabolism

The term metabolism refers to all of the chemical reactions by which complex molecules taken into an organism are broken down to produce energy and by which energy is used to build up complex molecules. All metabolic reactions fall into one of two general categories: catabolic and anabolic reactions, or the processes of breaking down and building up, respectively. The best example of metabolism from daily life occurs in the process of taking in and digesting nutrients, but sometimes these processes become altered, either through a person’s choice or through outside factors, and metabolic disorders follow. Such disorders range from anorexia and bulimia to obesity. These are all examples of an unhealthy, unnatural alteration to the ordinary course of metabolism; on the other hand, hibernation allows animals to slow down their metabolic rates dramatically as a means of conserving energy during times when food is scarce.

Metabolism is like a furnace, in that it burns energy, and that is the aspect most commonly associated with this concept. But metabolism also involves a function that a furnace does not: building new material. All metabolic reactions can be divided into either catabolic or anabolic reactions. Catabolism is the process by which large molecules are broken down into smaller ones with the release of energy, whereas anabolism is the process by which energy is used to build up complex molecules needed by the body to maintain itself and develop new tissue.

Digestion is the process of breaking down food into simpler chemical compounds as a means of making nutrients absorbable by the body. This is a catabolic process, because the molecules of which foods are made are much too large to pass through the lining of the digestive system and directly into the bloodstream. Thanks to the digestive process, smaller molecules are formed and enter the bloodstream, from whence they are carried to individual cells throughout a person’s body.

The smaller molecules into which nutrients are broken down make up the metabolic pool, which consists of simpler substances. The metabolic pool includes simple sugars, made by the breakdown of complex carbohydrates; glycerol and fatty acids, which come from the conversion of lipids, or fats; and amino acids, formed by the breakdown of proteins. Substances in the metabolic pool provide material from which new tissue is constructedan anabolic process.

For the body to function efficiently, there has to be an effective means of controlling and integrating the metabolic processes occurring in all the cells, tissues, and organs. This integration and control is mainly achieved by circulating hormones, with their release being regulated in turn partly by the nervous system and partly by direct effects of substances in the blood on the endocrine glands. An example of this integrated control of metabolism is the way in which blood glucose concentration is regulated to ensure an adequate supply of glucose to the brain. After meals, the hormone insulin acts to promote storage of glucose in the form of glycogen in the liver. The brain continuously extracts glucose from the blood to use as a fuel for its metabolic processes. In the periods between meals, this continued use of blood glucose causes the concentration to fall, which could impair brain function. However, a fall in blood glucose is detected in the pancreas and leads to the release of the hormone glucagon, which acts on the liver to cause breakdown of glycogen and release of glucose into the blood. In addition, if blood glucose falls sufficiently to affect brain metabolism, the sympathetic nervous system is activated, causing the adrenal gland to release adrenaline, which also stimulates the release of glucose from the liver; also the individual feels hungry and is prompted to eat.

The main way in which the energy contained in the macronutrients is used in metabolism is via the substance adenosine triphosphate (ATP). Cells require energy for their metabolic processes, so they contain the enzymes and organelles needed to produce ATP from the catabolism of fats, carbohydrates, and/or proteins. In most cases, the production of ATP occurs in association with the oxidation, so that the final products are ATP, carbon dioxide, and water, as illustrated below for the oxidation of glucose (C6H12O6):

C6H12O6 + 6O2 = 6CO2 + 6H2O + ATP

This is an example of aerobic metabolism, requiring the supply of oxygen and the removal of carbon dioxide from the cells by the circulating blood. Thus, in order for this predominant type of metabolism to proceed effectively in the whole body, there needs to be integration of the respiration, circulation, and supply of nutrients.

In some situations, anaerobic metabolism can occur, ATP is produced without the use of oxygen, but the energy-releasing capacity of these systems is very small compared with that of aerobic metabolism, and the anaerobic reactions lead to the production of waste products such as lactic acid which impair cell function if they are present in high concentrations.

ATP is the single most important molecule for the metabolism of almost all the cells of the body. It is used to release the energy needed for muscles to contract, for chemical bonds to be made during the synthesis of complex molecules, and for other bonds to be broken during catabolic processes. Cells do not store large quantities of ATP, but rather produce it when it is needed. Thus, most cells of the body need to regulate the concentration of ATP within them. This occurs via the effects of ATP, and its immediate breakdown product ADP (adenosine diphosphate), on the enzymes responsible for synthesizing ATP: when more ATP is used, its concentration falls, and that of ADP rises, leading to the activation of the enzyme which synthesizes more ATP. This in turn requires more oxygen to be used, and nutrients to be broken down.

An example of the complex integration of metabolism is provided by considering the processes involved in muscle contraction during exercise. This involves the brain and other parts of the nervous system in the initiation of voluntary muscle contraction and movement. Contraction can occur only if ATP is available within the muscle cells. As the ATP already present is used, so the concentration of ADP will rise, which stimulates more ATP production. At the same time the contraction of the muscles stimulates the breakdown of the intramuscular glycogen, and may also stimulate the uptake of glucose and fatty acids from the blood. The increased availability of these fuels is accompanied by stimulation of their oxidation, so the ATP concentration is maintained, and muscle contraction continues, supported by an increase in aerobic energy metabolism. For this to be possible, it is also necessary for the supply of blood to the muscles to increase, in order to deliver more oxygen and carry away more carbon dioxide and heat; the action of chemical products of local metabolism, which dilate local blood vessels, effectively links flow to requirement.

The above examples illustrate the complexity of metabolism in the human body, and show that for normal function it is essential that local processes are co-ordinated and integrated throughout the body.

Source: http://www.answers.com/Metabolism

“Enzymes are catalysts for virtually every biological and chemical reaction in the body, and digestive enzymes are crucial for the breakdown of food into nutrients that the body can absorb. Digestive enzymes, of which a variety are herbs, are used to treat a number of digestive problems and other conditions.”

The Digestive enzymes are enzymes in the alimentary tract that break down food so that the organism can absorb it. The main sites of action are the oral cavity, the stomach, the duodenum and the jejunum. They are secreted by different glands: the salivary glands, the glands in the stomach, the pancreas, and the glands in the small intestines.

Oral cavity

In the oral cavity, salivary glands secrete ptyalin. It is a type of a-amylase, which digests starch into small segments of multiple sugars and into individual soluble sugars. Secreted by small and large salivary glands.

Salivary glands also secrete lysozyme, which kills bacteria but is not classified as a digestive enzyme.

Esophagus

There are no digestive enzymes secreted in the esophagus.

Stomach

The enzymes that get secreted in the stomach are called gastric enzymes. These are the following:

· Pepsin is the main gastric enzyme. As it breaks proteins into smaller peptide fragments, it is a peptidase.

· Gelatinase, degrades type I and type V gelatin and type IV and V collagen, which are proteoglycans in meat.

· Gastric amylase degrades starch, but is of minor significance.

· Gastric lipase is a tributyrase by its biochemical activity, as it acts almost exclusively on tributyrin, a butter fat.

Small intestine

Pancreatic enzymes

The pancreas is the main digestive gland in our body. It secretes the enzymes:

· Trypsin, is a peptidase, that breaks down peptides in the small intestine.

· Chymotrypsin, also a peptidase

· Steapsin, degrades triglycerides into fatty acids and glycerol.

· Carboxypeptidase, splits peptide fragments into individual amino acids. It is a protease.

· Several elastases that degrade the protein elastin and some other proteins.

· Several nucleases that degrade nucleic acids, like DNAase and RNAase

· Pancreatic amylase that, besides starch, glycogen and cellulose, degrades most other carbohydrates.

· Bile from the liver, which emulsifies fat, allowing more efficient use of lipases in the duodenum; in converting lipids to their component fatty acid and glycerol molecules

Proper small intestine enzymes

Several peptidases.

The jejunum and ileum secretes a juice called succus entericus which contains the following:

Six types of enzymes degrade disaccharides into monosaccharides:

· Sucrase, which breaks down sucrose into glucose and fructose

· Maltase, which breaks down maltose into glucose.

· Isomaltase, which breaks down maltose and isomaltose

· Lactase, which breaks down lactose into glucose and galactose

· Intestinal lipase, which breaks down fatty acids

· Erepsin, also a protein-digesting enzyme

Source: http://www.answers.com/Digestive+enzymes

“Digestive — Pertaining to digestion.”

d. enzymes include salivary (amylase), gastric (pepsin), pancreatic (trypsin, chymotrypsin, amylase, lipase), small intestinal mucosa (carbohydrases including isomaltase, lactase, maltase, sucrase, trehalase).
d. inoculant administered mostly to neonates primarily to provide an inoculum of beneficial bacteria and protozoa essential to proper digestion and usually picked up from the environment. In many commercial products the irresistible temptation to include other materials, including dietary essential vitamins and minerals, clouds the effect of the inoculant, and may, as in iron poisoning in foals, cause disaster.
d. system the organs that have as their particular function the ingestion, digestion and absorption of food or nutritive elements. They include the mouth, teeth, tongue, pharynx, esophagus, stomach and intestines. The accessory organs of digestion, which contribute secretions important to digestion, include the salivary glands, pancreas, liver and gallbladder. Birds have an unusual system in that there are no teeth and no soft palate in most. There is a pregastric buffer, the crop; the stomach is separated into two organs, one secretory and one muscular, and the large intestine is replaced by a dual cecum. The rectum empties into a cloaca which is shared with the urogenital tract. The ruminant system is complicated by the presence of the forestomachs, the reticulum, rumen and omasum, and there are no upper incisor teeth. The peculiarities of horses are the greatly distended large intestine and the absence of a gallbladder.
d. tract the digestive system less the ancillary organs of salivary glands, liver and pancreas; the luminal organs through which food passes. See also alimentary canal.

Source: http://www.answers.com/topic/digestive?nr=1&lsc=true&cat=health

“How can I tell a great digestive enzyme product by its label?”

There are three things to look for on the label. First, you want to make sure the enzymes are plant enzymes… Aspergillus oryzae and niger (these are the most effective digestive enzymes available). Second, look for ionic minerals within the formulation. These minerals help the digestive enzymes become two to three times more active and effective. Third, look closely at the amount of protease, amylase and lipase within the formulation… 75,000 HUT for Protease, 15,000 SKB for Amylase and 5,000 LU for Lipase. These amounts are very important if you really want to help with digestion and cleaning up the blood.

Source: http://breathing.com/articles/enzymes.htm

“Protease – Any of various enzymes, including the endopeptidases and exopeptidases, that catalyze the hydrolytic breakdown of proteins into peptides or amino acids.

Lipase — Any of a group of enzymes that catalyze the hydrolysis of fats into glycerol and fatty acids.

Amylase — Any of a group of enzymes that are present in saliva, pancreatic juice, and parts of plants and catalyze the hydrolysis of starch to sugar to produce carbohydrate derivatives.

Cellulase — Any of several enzymes produced chiefly by fungi, bacteria, and protozoans that catalyze the hydrolysis of cellulose.

Lactase — An enzyme occurring in certain yeasts and in the intestinal juices of mammals and catalyzing the hydrolysis of lactose into glucose and galactose.”

Sources: http://www.answers.com/Protease ; http://www.answers.com/Lipase ; http://www.answers.com/Amylase ; http://www.answers.com/Cellulase ; http://www.answers.com/Lactase?cat=health

“Excess phenylalanine is not stored in the body and has to be broken down by a specific enzyme.”

One of the 22 a-amino acids commonly found in animal proteins. It is one of several essential amino acids needed in the diet; human beings cannot synthesize it from simpler metabolites. Young adults need about 31 mg of this amino acid per day per kg (14 mg per lb) of body weight. Phenylalanine can be degraded into simpler compounds by the enzymes of the body and is readily converted to the amino acid tyrosine. Phenylketonuria (PKU), an inherited disease that, if left untreated, results in retarded mental development in children, has been shown to be associated with the lack of activity of the enzyme that converts phenylalanine to tyrosine. This results in the buildup of phenylalanine in the blood, an event leading to several pathological consequences. The incidence of this disease, about one in every 10,000 births, is high enough to have prompted several states to institute regular screening procedures for the detection of the disease in newborns. If diagnosed early the disease can be controlled to a great extent by administering a diet very low in phenylalanine. Phenylalanine contributes to the structure of proteins into which it has been incorporated by the tendency of its side chain to participate in hydrophobic interactions (see isoleucine). This amino acid was first isolated from a natural source (lupine sprouts) in 1879; it was first chemically synthesized in 1882.

An essential amino acid; in addition to its role in protein synthesis, it is the metabolic precursor of tyrosine (and hence noradrenaline, adrenaline, and the thyroid hormones). Dietary tyrosine spares phenylalanine, so reducing the requirement.

Persons suffering from PKU must monitor their intake of protein to control the buildup of phenylalanine as their bodies convert protein into its component amino acids.

A related issue is the compound present in many sugarless gums and mints, snack foods, sugarless soft drinks (such as diet sodas including CocaCola Zero, Pepsi Max, some forms of Lipton Tea, Clear Splash flavored water), and a number of other low calorie food products. The artificial sweetener aspartame, sold under the names “Equal” and “NutraSweet”, is an ester that is hydrolyzed in the body to give phenylalanine, aspartic acid, and methanol (wood alcohol). The breakdown problems phenylketonurics have with protein and the attendant build up of phenylalanine in the body also occurs with the ingestion of aspartame, although to a lesser degree. Accordingly, all products in the U.S. and Canada that contain aspartame must be labeled: “Phenylketonurics: Contains phenylalanine.” In the UK, foods containing aspartame must carry ingredients panels that refer to the presence of ‘aspartame or E951′, and they must be labeled with a warning “Contains a source of phenylalanine”. These warnings are specifically placed to aid individuals who suffer from PKU so that they can avoid such foods.

Interestingly, the macaque genome was recently sequenced and it was found that macaques naturally have a mutation that is found in humans who have PKU.

DL-Phenylalanine is marketed as a nutritional supplement for its putative analgesic and antidepressant activities. The putative analgesic activity of DL-phenylalanine may be explained by the possible blockage by D-phenylalanine of enkephalin degradation by the enzyme carboxypeptidase A. The mechanism of DL-phenylalanine’s putative antidepressant activity may be accounted for by the precursor role of L-phenylalanine in the synthesis of the neurotransmitters norepinephrine and dopamine. Elevated brain norepinephrine and dopamine levels are thought to be associated with antidepressant effects. D-phenylalanine is absorbed from the small intestine, following ingestion, and transported to the liver via the portal circulation. A fraction of D-phenylalanine appears to be converted to L-phenylalanine. D-phenylalanine is distributed to the various tissues of the body via the systemic circulation. D-phenylalanine appears to cross the blood-brain barrier with less efficiency than L-phenylalanine. A fraction of an ingested dose of D-phenylalanine is excreted in the urine.

Source: http://www.answers.com/Phenylalanine?cat=health

“In addition to its role in proteins, tyrosine is the precursor for the synthesis of melanin (the black and brown pigment of skin and hair), and adrenaline and noradrenaline.”

One of the amino acids, not essential for humans unless they have the hereditary disorder phenylketonuria. It is the biochemical precursor of many important catecholamines. It is found in small amounts in most proteins, especially insulin and papain (found in papaya). It is used in biochemical research and as a dietary supplement.

Tyrosine is a precursor of the adrenal hormones epinephrine and norepinephrine as well as of the thyroid hormones, including thyroxine. Melanin, the skin and hair pigment, is also derived from this amino acid. Tyrosine residues in enzymes have frequently been shown to be associated with active sites. Modification of these residues with various chemicals often results in a change in the specificity of the enzyme toward its substrates or even in total destruction of its activity. In 1846 tyrosine was obtained as a product of the degradation of the protein casein (from cheese). It was synthesized in the laboratory in 1883, and its structure was thus determined.

L-Tyrosine is sometimes recommended by practitioners as helpful for weight loss, clinical depression, Parkinson’s Disease, Attention Deficit Disorder, and phenylketonuria; however, one study found that it had no impact on endurance exercise performance.

Source: http://www.answers.com/Tyrosine?cat=health&nr=1

“One of the problems with some crash diets is that they do not provide enough essential amino acids and, in some extreme cases, have resulted in death.”

An amino acid that must be obtained from the diet so that the body can synthesize vital proteins. Nine amino acids are generally regarded as essential for humans: isoleucine, leucine, lysine, threonine, tryptophan, methionine, histidine, valine and phenylalanine. In addition, the amino acids arginine, cysteine, glycine, glutamine and tyrosine are considered conditionally essential, meaning they are not normally required in the diet, but must be supplied exogenously to specific populations that do not synthesize it in adequate amounts. (Histidine is required by infants, but it has not been fully established that it is essential for adults.) The essential amino acids must be available in the body simultaneously and in the correct proportions for protein synthesis to occur.

Source: http://www.answers.com/topic/essential-amino-acid?cat=health

“Most essential nutrients are substances that are metabolically necessary but cannot be synthesized by the organism.”

An essential nutrient is a nutrient required for normal body functioning that cannot be synthesized by the body and must be obtained from a dietary source. Some categories of essential nutrient include vitamins, dietary minerals, essential fatty acids, and essential amino acids.

All essential nutrients are toxic in large doses (see hypervitaminosis or the nutrient pages themselves below). Some can be taken in amounts larger than required in a typical diet, with no apparent ill effects. Linus Pauling said of vitamin B3, (either niacin or niacinamide), “What astonished me was the very low toxicity of a substance that has such very great physiological power. A little pinch, 5 mg, every day, is enough to keep a person from dying of pellagra, but it is so lacking in toxicity that ten thousand times as much can [sometimes] be taken without harm.” A similar statement can be made about vitamin C and some other vitamins.

List of essential nutrients

· Essential fatty acids:

1. Linolenic acid (the shortest chain omega-3 fatty acid)

2. Linoleic acid (the shortest chain omega-6 fatty acid)

3. Essential amino acids necessary for all humans:

4. Histidine

5. Isoleucine

6. Lysine

7. Leucine

8. Methionine

9. Phenylalanine

10. Threonine

11. Tryptophan

12. Valine

· Essential amino acids necessary for human children and not adults:

1. Arginine

2. Vitamins:

3. Biotin (vitamin B7, vitamin H)

4. Choline (vitamin Bp)

5. Folate (folic acid, vitamin B9, vitamin M)

6. Niacin (vitamin B3, vitamin P, vitamin PP)

7. Pantothenic acid (vitamin B5)

8. Riboflavin (vitamin B2, vitamin G)

9. Thiamine (vitamin B1)

10. Vitamin A (retinol)

11. Vitamin B6 (pyridoxine, pyridoxamine, or pyridoxal)

12. Vitamin B12 (cobalamin)

13. Vitamin C (ascorbic acid)

14. Vitamin D (Cholecalciferol, Ergocalciferol, Calcitriol)

15. Vitamin E (tocopherol)

16. Vitamin K (naphthoquinoids)

· Dietary minerals: Biochemical studies reported in 2006 indicate that the following elements (aside from H, C, N, and O) are required for human health:

1. Calcium (Ca)

2. Chloride (Cl-)

3. Cobalt (Co)

4. Copper (Cu) [3]

5. Iodine (I)

6. Iron (Fe)

7. Magnesium (Mg)

8. Manganese (Mn)

9. Molybdenum (Mo)

10. Phosphorus (P)

11. Potassium (K)

12. Selenium (Se)