Amylase Levels, Testing and It Role in Our Health

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Amylase, protease and lipase are the three main and most vital digestive enzymes your body utilizes to digest food. A growing number of health problems can be linked to nutrient malabsorption due to a lack of digestive enzymes.

Amylase has the responsibility of helping your body process carbohydrates into simple sugars while protease breaks down protein and lipase is in charge of fat breakdown.

The role of digestive enzymes is to act as catalysts in speeding up specific, life-preserving chemical reactions in the body. Essentially, digestive enzymes assist in breaking down larger molecules into more easily absorbed particles that the body can use to survive and thrive. Without proper levels of amylase and other digestive enzymes, it really is impossible to have your health be at its best.

What Is Amylase?

By definition, it&#;s the primary starch-digesting enzyme secreted in the body. To be more specific, it digests carbohydrates (polysaccharides) into smaller disaccharide units, eventually converting them into monosaccharides, such as glucose. Alpha-amylase (α-Amylase) is the major form of amylase found in humans and other mammals and is mainly made the pancreas and salivary glands, but it&#;s also produced by the small intestine mucosa, ovaries, placenta, liver and fallopian tubes.

The amylase secreted by the salivary glands kicks off the the enzymatic digestion of starches in the mouth as food is chewed and mixed with saliva. It might be surprising, but it&#;s true that the breakdown of larger, more complex starches into simpler sugars actually starts in your mouth with simple chewing. This is why chewing food thoroughly is truly key to good digestion and optimal overall health.

Amylase is part of a six-step digestive process that begins with chewing in the mouth and triggers the start of a domino effect in firing off mechanisms and secretions:

1. Salivary amylase released in the mouth is the first digestive enzyme to assist in breaking down food into its component molecules, and that process continues after food enters the stomach.

2. The parietal cells of the stomach are then triggered into releasing acids, pepsin and other enzymes, including gastric amylase, and the process of degrading the partially digested food into chyme (a semifluid mass of partly digested food) begins.

3. The acid also has the effect of neutralizing the salivary amylase, allowing gastric amylase to take over.

4. After an hour or so, the chyme is propelled into the duodenum (upper small intestine), where the acidity acquired in the stomach triggers the release of the hormone secretin.

5. That, in turn, notifies the pancreas to release hormones, bicarbonate, bile and numerous pancreatic enzymes, of which the most relevant are lipase, trypsin, amylase and nuclease.

6. The bicarbonate changes the acidity of the chyme from acid to alkaline, which has the effect of not only allowing the enzymes to degrade food, but also bacteria not capable of surviving in the acid environment of the stomach to break it down further.

At this point, if you don&#;t have a deficit of digestive enzymes, then most of the work is done. However, for many people digestive enzyme supplementation is needed and helps this whole process take place as it should.

Health Benefits

What are some of the ways that amylase can benefit your health? Well, aside from the most key and central function to properly digest carbohydrates, it also holds a lot of other valuable health benefits that will probably surprise you.

1. Improved Digestion

Your mouth is the place where both the mechanical and chemical breakdown of your food occurs through the combined use of your teeth, jaws and saliva. Amylases are vital to your digestive process because they&#;re needed to process any starches in your diet, which are a main source from which people derive glucose, the primary sugar molecule the body uses for energy.

It&#;s key that you combine your body&#;s natural amylase-producing ability with your natural ability to chew. Why is this important? Because if food is not properly broken down in the mouth, then your body has more work to do in order to digest and extract nutrients and energy from whatever you eat. By chewing thoroughly, you give the amylase more time to process any carbs that you have consumed, and the more time amylase has to work the better and quicker your overall digestion will be.

In addition, cells in your pancreas make another form of amylase called pancreatic amylase, which passes through a duct to reach your small intestine. Pancreatic amylase completes the digestion of carbohydrates.

2. More Energy

Food not only provides your body with nutrients, but it also provides it with the energy it needs to keep you going on a daily basis. Glucose is the primary sugar molecule that the body uses for energy, and while you never want to have high glucose levels (think diabetes), you want to obtain some glucose in your diet from healthy sources.

The amylases in your body break starch down into two sugar units, maltose and isomaltose, and then other enzymes, called maltase and isomaltase, hydrolyze these two sugars into the individual monosaccharide glucose. Foods that are high in starch include breads, grains, cereals, pasta, rice, beans, corn, potatoes and peas. If it wasn&#;t for amylase, your body wouldn&#;t be able to use foods like these so efficiently to fuel you.

3. Anti-Diabetic

A study published in the Journal of Clinical & Diagnostic Research was designed to determine the serum amylase, blood glucose and the serum lipid profile in 110 type 2 diabetes patients compared to healthy individuals of the same age and sex. The research showed that for the diabetic subjects wherever blood sugar levels were higher, serum amylase activity was found to be significantly lower. This finding was reflective of pancreas malfunction and speaks to the importance of a healthy pancreas producing healthy amounts of amylase.

Another study found that low serum amylase levels are associated with an increased risk of metabolic abnormalities like diabetes as well as metabolic syndrome. Together, these studies show the ability of this digestive enzyme to maintain normal blood sugar levels and help treat or reverse diabetes symptoms.

4. Stress Monitoring

Stress is by far one of the worst things in the world for your health, particularly chronic stress. Research is showing that amylase can be a very helpful and accurate marker of stress levels.

One study looked at the whether or not the salivary enzyme alpha-amylase could indicate stress-reactive bodily changes. Researchers repeatedly measured salivary alpha-amylase and salivary cortisol as well as plasma catecholamines and cardiovascular activity before, during and after 30 young men underwent the Trier Social Stress Test (TSST).

Results indicated that salivary alpha-amylase is sensitive to psychosocial stress and may be a very helpful additional parameter for the measurement of stress in humans.

Amylase Levels

Possible reasons for high amylase levels include:

• Pancreatitis (inflammation of the pancreas), a pancreatic cyst or pancreatic cancer
• Gallstones that are causing pancreatitis
• Inflammation of the salivary glands, such as mumps
• Bowel obstruction or strangulation
• A stomach ulcer that has caused a hole in the stomach wall
• Diabetic ketoacidosis
• Kidney failure
• A ruptured ectopic pregnancy
• Appendicitis or peritonitis
• Macroamylasemia, an uncommon and harmless condition in which amylase is bound to a protein in the blood

Low amylase levels are also something to be concerned about. The following common health issues could actually be a sign of amylase deficiency:

• Allergies
• Skin rashes
• Gas and constipation
• Mood swings
• Carbohydrate and sugar cravings
• Blood sugar imbalances
• Type 2 diabetes

Testing

Testing can be conducted to measure the level of amylase as well as other enzymes in your blood. Amylase level testing can be done with a blood or urine test. For a urine test, it&#;s likely a two-hour or 24-hour sampling. For a blood test, blood is taken from a vein in your arm. There is more work involved with collecting your urine over a period of time, but there are also no risks, pain or side effects associated with collecting urine samples. If you don&#;t like needles then the urine test can be a good option.

Typically, there are only low levels of amylase found in the urine or blood. However, if the pancreas or salivary glands become damaged or blocked then more amylase is often released into the bloodstream and urine. When it comes to blood, amylase levels rise for only a short time. In the urine, amylase may remain high for several days.

Why would a doctor ever test your amylase levels? A test might be conducted for several reasons, including:

• To evaluate the cause of swollen and inflamed salivary glands
• To find out if a patient has pancreatitis or another pancreatic disease
• To determine if a treatment for pancreatitis or other pancreatic diseases is working

If you&#;re preparing to have your amylase levels tested then you should not consume any alcohol for at least 24 hours prior to testing. If you&#;re having a blood test then do not eat or drink anything except water for at least two hours before testing. For a 24-hour urine test, make sure that you drink enough fluids during the test to prevent dehydration and to ensure that you collect enough samples.

There are a lot of medications that can affect amylase test results so prior to testing be sure to let your doctor know about any medications or supplements.

A lipase test is often used along with an amylase test to help diagnose and monitor acute pancreatitis, chronic pancreatitis, celiac disease, Crohn&#;s disease, cystic fibrosis and pancreatic cancer. Increases in the level of lipase may signal the worsening of these diseases. A lipase test along with an amylase test can help monitor treatment effectiveness and outcomes.

Amylase Test Results

Testing results are usually available within 72 hours. Normal value ranges can vary slightly among different laboratories. For a urine test, the normal range is typically 2.6 to 21.2 international units per hour (IU/h). For a blood test, the normal range is usually 23 to 85 units per liter (U/L).

Food and Supplement Sources

Natural dietary sources of amylase include raw fruits and vegetables, along with sprouted seeds, nuts, legumes and whole grains. Both short- and long-term sprouting helps the body regulate amylase-enzyme activity that&#;s needed to properly digest glucose, which is especially helpful to diabetics. Royal jelly is also another excellent source.

When it comes to supplements, you&#;ll find amylase in a general digestive enzyme supplement that includes the other key digestive enzymes as well. A common variety is a full-spectrum enzyme blend for general digestive improvement. You can opt for a supplement that is vegetarian or animal-based.

Risks and Side Effects

Digestive enzymes are essentially nontoxic and typically don&#;t cause side effects. Occasional side effects of digestive enzymes can include mild gastrointestinal distress, diarrhea or allergic reactions. If any of these effects persist or worsen, you should discontinue use of the supplement and speak with your health care provider.

If you take a supplement that includes the digestive enzyme bromelain, then you should know that it has possible cross-reactivity and can provoke allergic symptoms in people who are sensitive to wheat, celery, papain, carrot, fennel, cypress pollen and grass pollen, as well as the plant family that includes ragweed, chrysanthemums, marigolds, daisies and echinacea. If you&#;re allergic to any of these foods or plant, then you may find that you&#;re allergic to bromelain and vice versa.

Digestive enzymes should only be combined with blood-thinning drugs like warfarin (Coumadin) under a doctor&#;s supervision. Combining bromelain and papain with blood-thinning prescriptions can further increase the risk of bruising and bleeding. Some evidence also suggests that bromelain may increase the absorption of certain antibiotics, specifically amoxicillin and tetracycline. Digestive enzymes may also enhance absorption of sedative medicines like benzodiazepines so digestive enzyme supplements should not be combined with sedatives.

Tell your doctor immediately if you have any serious side effects after taking digestive enzymes, including severe abdominal discomfort, joint pain, frequent or painful urination, or allergic reaction.

Final Thoughts

• Amylase, protease and lipase are the three main and most vital enzymes your body utilizes to digest food.
• Amylase is the primary starch-digesting enzyme secreted in the body.
• It&#;s possible to have your amylase levels tested via a blood or urine sample.
• Having amylase levels that are too high or too low are both problematic.
• You can increase your intake of amylase and other digestive enzymes by following a whole foods diet loaded with fresh, raw fruits and vegetables, as well as sprouted nuts, grains, seeds and beans.
• If you need help increasing your digestive enzyme levels, you can supplement your diet with a full-spectrum enzyme blend that can help improve your digestive health as well as your overall health.

Class of enzymes

An amylase ( ) is an enzyme that catalyses the hydrolysis of starch (Latin amylum) into sugars. Amylase is present in the saliva of humans and some other mammals, where it begins the chemical process of digestion. Foods that contain large amounts of starch but little sugar, such as rice and potatoes, may acquire a slightly sweet taste as they are chewed because amylase degrades some of their starch into sugar. The pancreas and salivary gland make amylase (alpha amylase) to hydrolyse dietary starch into disaccharides and trisaccharides which are converted by other enzymes to glucose to supply the body with energy. Plants and some bacteria also produce amylase. Specific amylase proteins are designated by different Greek letters. All amylases are glycoside hydrolases and act on α-1,4-glycosidic bonds.

Classification

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α-amylase β-amylase γ-amylase Source Animals, plants, microbes Plants, microbes Animals, microbes Tissue Salivary gland, pancreas Seeds, fruits Small intestine Cleavage site Random α-1,4 glycosidic bond Second α-1,4 glycosidic bond Last α-1,4 glycosidic bond Reaction products Maltose, dextrin, etc. Maltose Glucose Optimum pH 6.7&#;7.0 5.4&#;5.5 4.0&#;4.5 Optimum temperature in brewing 68&#;74 °C (154&#;165 °F) 58&#;65 °C (136&#;149 °F) 63&#;68 °C (145&#;154 °F)

The α-amylases (EC 3.2.1.1 ) (CAS &#;71&#;5) (alternative names: 1,4-α-D-glucan glucanohydrolase; glycogenase) are calcium metalloenzymes. By acting at random locations along the starch chain, α-amylase breaks down long-chain saccharides, ultimately yielding either maltotriose and maltose from amylose, or maltose, glucose and "limit dextrin" from amylopectin. They belong to glycoside hydrolase family 13 (https://www.cazypedia.org/index.php/Glycoside_Hydrolase_Family_13).

Because it can act anywhere on the substrate, α-amylase tends to be faster-acting than β-amylase. In animals, it is a major digestive enzyme, and its optimum pH is 6.7&#;7.0.[3]

In human physiology, both the salivary and pancreatic amylases are α-amylases.

The α-amylase form is also found in plants, fungi (ascomycetes and basidiomycetes) and bacteria (Bacillus).

Another form of amylase, β-amylase (EC 3.2.1.2 ) (alternative names: 1,4-α-D-glucan maltohydrolase; glycogenase; saccharogen amylase) is also synthesized by bacteria, fungi, and plants. Working from the non-reducing end, β-amylase catalyzes the hydrolysis of the second α-1,4 glycosidic bond, cleaving off two glucose units (maltose) at a time. During the ripening of fruit, β-amylase breaks starch into maltose, resulting in the sweet flavor of ripe fruit. They belong to glycoside hydrolase family 14.

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Both α-amylase and β-amylase are present in seeds; β-amylase is present in an inactive form prior to germination, whereas α-amylase and proteases appear once germination has begun. Many microbes also produce amylase to degrade extracellular starches. Animal tissues do not contain β-amylase, although it may be present in microorganisms contained within the digestive tract. The optimum pH for β-amylase is 4.0&#;5.0.[4]

γ-Amylase (EC 3.2.1.3 ) (alternative names: Glucan 1,4-a-glucosidase; amyloglucosidase; exo-1,4-α-glucosidase; glucoamylase; lysosomal α-glucosidase; 1,4-α-D-glucan glucohydrolase) will cleave α(1&#;6) glycosidic linkages, as well as the last α-1,4 glycosidic bond at the nonreducing end of amylose and amylopectin, yielding glucose. The γ-amylase has the most acidic optimum pH of all amylases because it is most active around pH 3. They belong to a variety of different glycoside hydrolase families, such as glycoside hydrolase family 15 in fungi, glycoside hydrolase family 31 of human MGAM, and glycoside hydrolase family 97 of bacterial forms.

Uses

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Fermentation

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α- and β-amylases are important in brewing beer and liquor made from sugars derived from starch. In fermentation, yeast ingests sugars and excretes ethanol. In beer and some liquors, the sugars present at the beginning of fermentation have been produced by "mashing" grains or other starch sources (such as potatoes). In traditional beer brewing, malted barley is mixed with hot water to create a "mash", which is held at a given temperature to allow the amylases in the malted grain to convert the barley's starch into sugars. Different temperatures optimize the activity of alpha or beta amylase, resulting in different mixtures of fermentable and unfermentable sugars. In selecting mash temperature and grain-to-water ratio, a brewer can change the alcohol content, mouthfeel, aroma, and flavor of the finished beer.

In some historic methods of producing alcoholic beverages, the conversion of starch to sugar starts with the brewer chewing grain to mix it with saliva.[5] This practice continues to be practiced in home production of some traditional drinks, such as chhaang in the Himalayas, chicha in the Andes and kasiri in Brazil and Suriname.

Flour additive

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Amylases are used in breadmaking and to break down complex sugars, such as starch (found in flour), into simple sugars. Yeast then feeds on these simple sugars and converts it into the waste products of ethanol and carbon dioxide. This imparts flavour and causes the bread to rise. While amylases are found naturally in yeast cells, it takes time for the yeast to produce enough of these enzymes to break down significant quantities of starch in the bread. This is the reason for long fermented doughs such as sourdough. Modern breadmaking techniques have included amylases (often in the form of malted barley) into bread improver, thereby making the process faster and more practical for commercial use.[6][failed verification]

α-Amylase is often listed as an ingredient on commercially package-milled flour. Bakers with long exposure to amylase-enriched flour are at risk of developing dermatitis[7] or asthma.[8]

Molecular biology

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In molecular biology, the presence of amylase can serve as an additional method of selecting for successful integration of a reporter construct in addition to antibiotic resistance. As reporter genes are flanked by homologous regions of the structural gene for amylase, successful integration will disrupt the amylase gene and prevent starch degradation, which is easily detectable through iodine staining.

Medical uses

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Amylase also has medical applications in the use of pancreatic enzyme replacement therapy (PERT). It is one of the components in Sollpura (liprotamase) to help in the breakdown of saccharides into simple sugars.[9]

Other uses

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An inhibitor of alpha-amylase, called phaseolamin, has been tested as a potential diet aid.[10]

When used as a food additive, amylase has E number E, and may be derived from pig pancreas or mold fungi.

Bacilliary amylase is also used in clothing and dishwasher detergents to dissolve starches from fabrics and dishes.

Factory workers who work with amylase for any of the above uses are at increased risk of occupational asthma. Five to nine percent of bakers have a positive skin test, and a fourth to a third of bakers with breathing problems are hypersensitive to amylase.[11]

Hyperamylasemia

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Blood serum amylase may be measured for purposes of medical diagnosis. A higher than normal concentration may reflect any of several medical conditions, including acute inflammation of the pancreas (which may be measured concurrently with the more specific lipase),[12] perforated peptic ulcer, torsion of an ovarian cyst, strangulation, ileus, mesenteric ischemia, macroamylasemia and mumps. Amylase may be measured in other body fluids, including urine and peritoneal fluid.

A January study from Washington University in St. Louis suggests that saliva tests of the enzyme could be used to indicate sleep deficits, as the enzyme increases its activity in correlation with the length of time a subject has been deprived of sleep.[13]

History

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In , Erhard Friedrich Leuchs (&#;) described the hydrolysis of starch by saliva, due to the presence of an enzyme in saliva, "ptyalin", an amylase.[14][15] it was named after the Ancient Greek name for saliva: πτύαλον - ptyalon.

The modern history of enzymes began in , when French chemists Anselme Payen and Jean-François Persoz isolated an amylase complex from germinating barley and named it "diastase".[16][17] It is from this term that all subsequent enzyme names tend to end in the suffix -ase.

In , Russian biochemist Aleksandr Yakovlevich Danilevsky [ru] (&#;) separated pancreatic amylase from trypsin.[18][19]

Evolution

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Salivary amylase

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Saccharides are a food source rich in energy. Large polymers such as starch are partially hydrolyzed in the mouth by the enzyme amylase before being cleaved further into sugars. Many mammals have seen great expansions in the copy number of the amylase gene. These duplications allow for the pancreatic amylase AMY2 to re-target to the salivary glands, allowing animals to detect starch by taste and to digest starch more efficiently and in higher quantities. This has happened independently in mice, rats, dogs, pigs, and most importantly, humans after the agricultural revolution.[20]

Following the agricultural revolution 12,000 years ago, human diet began to shift more to plant and animal domestication in place of hunting and gathering. Starch has become a staple of the human diet.

Despite the obvious benefits, early humans did not possess salivary amylase, a trend that is also seen in evolutionary relatives of the human, such as chimpanzees and bonobos, who possess either one or no copies of the gene responsible for producing salivary amylase.[21]

Like in other mammals, the pancreatic alpha-amylase AMY2 was duplicated multiple times. One event allowed it to evolve salivary specificity, leading to the production of amylase in the saliva (named in humans as AMY1). The 1p21.1 region of human chromosome 1 contains many copies of these genes, variously named AMY1A, AMY1B, AMY1C, AMY2A, AMY2B, and so on.[22]

However, not all humans possess the same number of copies of the AMY1 gene. Populations known to rely more on saccharides have a higher number of AMY1 copies than human populations that, by comparison, consume little starch. The number of AMY1 gene copies in humans can range from six copies in agricultural groups such as European-American and Japanese (two high starch populations) to only two to three copies in hunter-gatherer societies such as the Biaka, Datog, and Yakuts.[22]

The correlation that exists between starch consumption and number of AMY1 copies specific to population suggest that more AMY1 copies in high starch populations has been selected for by natural selection and considered the favorable phenotype for those individuals. Therefore, it is most likely that the benefit of an individual possessing more copies of AMY1 in a high starch population increases fitness and produces healthier, fitter offspring.[22]

This fact is especially apparent when comparing geographically close populations with different eating habits that possess a different number of copies of the AMY1 gene. Such is the case for some Asian populations that have been shown to possess few AMY1 copies relative to some agricultural populations in Asia. This offers strong evidence that natural selection has acted on this gene as opposed to the possibility that the gene has spread through genetic drift.[22]

Variations of amylase copy number in dogs mirrors that of human populations, suggesting they acquired the extra copies as they followed humans around.[23] Unlike humans whose amylase levels depend on starch content in diet, wild animals eating a broad range of foods tend to have more copies of amylase. This may have to do with mainly detection of starch as opposed to digestion.[20]

References

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For more information, please visit Amylase Enzyme.