Dec. 02, 2024
Digestive enzymes are substances that help you digest your food. They are secreted (released) by the salivary glands and cells lining the stomach, pancreas, and small intestine. There are several digestive enzymes, including amylase, maltase, lactase, lipase, sucrase, and proteases.
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Some conditions can result in digestive enzyme deficiencies, such as lactose intolerance or exocrine pancreatic insufficiency. In that case, supplementation with foods, over-the-counter supplements, or prescription digestive enzyme supplements may be necessary.
Keep reading to learn about different types of digestive enzymes and how they work.
What Are Digestive Enzymes?
Digestive enzymes are released when we:
Some foods require certain digestive enzymes to break down the specific nutrients they contain.
A variety of health conditions, especially those that affect the pancreas, can lead to deficiencies in digestive enzymes. This is because the pancreas secretes several key enzymes.
Often these deficiencies can be fixed by changing your diet. You can avoid certain foods or eat foods containing naturally occurring digestive enzymes. You can also take prescription or over-the-counter (OTC) enzyme supplements.
Types of Digestive Enzymes
Each of the many different digestive enzymes targets a specific nutrient and splits it up into a form that can eventually be absorbed.
The most important digestive enzymes include:
Amylase
Amylase is important for digesting carbohydrates. It breaks down starches into sugars.
Amylase is secreted by both the salivary glands and the pancreas. The measurement of amylase levels in the blood is sometimes used as an aid in diagnosing various pancreas or other digestive tract diseases.
High levels of amylase in the blood may mean you have:
Low levels of amylase may mean you have chronic pancreatitis (ongoing inflammation of the pancreas) or liver disease.
Maltase
The small intestine releases maltase, which is responsible for breaking down maltose (malt sugar) into glucose (simple sugar). The body uses glucose for energy.
During digestion, starch is partially transformed into maltose by amylases. The maltase enzyme then changes maltose into glucose. This sugar is then either used immediately by the body or stored in the liver as glycogen for future use.
Lactase
Lactase (also called lactase-phlorizin hydrolase) is an enzyme that breaks down lactose, a sugar found in dairy products. It turns lactose into the simple sugars glucose and galactose.
Lactase is produced by cells known as enterocytes that line the intestinal tract. Lactose that is not absorbed is fermented by bacteria in the gut. This can cause you to have gas and an upset stomach.
Lipase
Lipase is responsible for the breakdown of fats into fatty acids and glycerol (simple sugar alcohol). It's produced in small amounts by your mouth and stomach, and in larger amounts by your pancreas.
Proteases
Also called peptidases, proteolytic enzymes, or proteinases, these digestive enzymes break down proteins into amino acids. They also play a role in numerous body processes, including:
Proteases are produced in the stomach and pancreas. The main ones include:
carboxypeptidase
andchymotrypsin
, to help break down peptides.If you are looking for more details, kindly visit Yulin HB™.
Sucrase
Sucrase is secreted by the small intestine, where it breaks down sucrose (the sugar in table sugar) into fructose and glucose. These are simpler sugars that the body can absorb.
Sucrase is found along the intestinal villi. These are tiny hair-like structures that line the intestine and absorb nutrients into the bloodstream.
Probiotics also help with digestion, but they are not the same as digestive enzymes. Probiotics are microbes that help support digestive health. They do not help you digest food.
Digestive Enzyme Deficiencies
There are a variety of health conditions that can interfere with the secretion of enough digestive enzymes to fully digest foods. Some are inherited genetic conditions while others develop over time.
Lactose Intolerance
Lactose intolerance occurs when you aren't able to digest lactose because of insufficient production of lactase by the small intestine. When you consume dairy products, you may experience:
There are several forms of lactose intolerance.
Congenital Lactase Deficiency
Congenital lactase deficiency (also called congenital alactasia) is a rare inherited form of lactose intolerance. It happens when newborns are unable to break down lactose in breast milk or formula. They get severe diarrhea if they aren't given a lactose-free alternative.
Congenital lactase deficiency is caused by mutations in the LCT gene that provides instructions for making the lactase enzyme.
Lactase Non-Persistence
Lactase non-persistence is a common type of lactose intolerance that some people develop as adults. It affects around 65% of people, and it's caused by decreased expression (activity) of the LCT gene. Symptoms typically begin 30 minutes to two hours after eating or drinking dairy.
Most people with lactase non-persistence keep some level of lactase activity and can continue to include a small amount of lactose in their diets. This may be in the form of cheese or yogurt since both tend to be tolerated better than fresh milk.
Secondary Lactose Intolerance
Secondary lactose intolerance develops when lactase production is reduced because of diseases that can damage the small intestine. These diseases include celiac disease or Crohn's disease as well as other illnesses or injuries that affect the intestinal wall.
Exocrine Pancreatic Insufficiency
The pancreas produces the key digestive enzymes amylase, protease, and lipase. People with exocrine pancreatic insufficiency (EPI) have a deficiency of these enzymes. As a result, they are unable to digest food properly, especially fats.
The health conditions that affect the pancreas and are associated with EPI are:
Symptoms of Digestive Enzyme Deficiencies
If you have a digestive enzyme deficiency, you may have symptoms such as:
These can also be symptoms of other conditions, some of them serious. Any digestive symptoms that persist for more than a week or two should be evaluated by a healthcare provider.
Foods High in Digestive Enzymes
A variety of foods, especially tropical fruits and fermented vegetables, are naturally high in digestive enzymes that might speed up the digestion of certain nutrients.
It's best to eat them raw since heat can lessen or destroy these plant enzymes.
Because of the existence of two types of linkages, the alpha-1,4 and the alpha-1,6, different structures are possible for starch molecules. An unbranched, single chain polymer of 500 to glucose subunits with only the alpha-1,4 glucosidic bonds is called amylose. On the other hand, the presence of alpha-1,6 glucosidic linkages results in a branched glucose polymer called amylopectin. The degree of branching in amylopectin is approximately one per twenty-five glucose units in the unbranched segments. Another closely related compound functioning as the glucose storage in animal cells is called glycogen, which has one branching per 12 glucose units. The degree of branching and the side chain length vary from source to source, but in general the more the chains are branched, the more the starch is soluble.
Starch is generally insoluble in water at room temperature. Because of this, starch in nature is stored in cells as small granules which can be seen under a microscope. Starch granules are quite resistant to penetration by both water and hydrolytic enzymes due to the formation of hydrogen bonds within the same molecule and with other neighboring molecules. However, these inter- and intra-hydrogen bonds can become weak as the temperature of the suspension is raised. When an aqueous suspension of starch is heated, the hydrogen bonds weaken, water is absorbed, and the starch granules swell. This process is commonly called gelatinization because the solution formed has a gelatinous, highly viscous consistency. The same process has long been employed to thicken broth in food preparation.
Depending on the relative location of the bond under attack as counted from the end of the chain, the products of this digestive process are dextrin, maltotriose, maltose, and glucose, etc. Dextrins are shorter, broken starch segments that form as the result of the random hydrolysis of internal glucosidic bonds. A molecule of maltotriose is formed if the third bond from the end of a starch molecule is cleaved; a molecule of maltose is formed if the point of attack is the second bond; a molecule of glucose results if the bond being cleaved is the terminal one; and so on. As can be seen from the exercises in Experiment No. 3, the initial step in random depolymerization is the splitting of large chains into various smaller sized segments. The breakdown of large particles drastically reduces the viscosity of gelatinized starch solution, resulting in a process called liquefaction because of the thinning of the solution. The final stages of depolymerization are mainly the formation of mono-, di-, and tri-saccharides. This process is called saccharification, due to the formation of saccharides.
Since a wide variety of organisms, including humans, can digest starch, alpha-amylase is obviously widely synthesized in nature, as opposed to cellulase. For example, human saliva and pancreatic secretion contain a large amount of alpha-amylase for starch digestion. The specificity of the bond attacked by alpha-amylases depends on the sources of the enzymes. Currently, two major classes of alpha-amylases are commercially produced through microbial fermentation. Based on the points of attack in the glucose polymer chain, they can be classified into two categories, liquefying and saccharifying.
Because the bacterial alpha-amylase to be used in this experiment randomly attacks only the alpha-1,4 bonds, it belongs to the liquefying category. The hydrolysis reaction catalyzed by this class of enzymes is usually carried out only to the extent that, for example, the starch is rendered soluble enough to allow easy removal from starch-sized fabrics in the textile industry. The paper industry also uses liquefying amylases on the starch used in paper coating where breakage into the smallest glucose subunits is actually undesirable. (One cannot bind cellulose fibers together with sugar!)
On the other hand, the fungal alpha-amylase belongs to the saccharifying category and attacks the second linkage from the nonreducing terminals (i.e. C4 end) of the straight segment, resulting in the splitting off of two glucose units at a time. Of course, the product is a disaccharide called maltose. The bond breakage is thus more extensive in saccharifying enzymes than in liquefying enzymes. The starch chains are literally chopped into small bits and pieces. Finally, the amyloglucosidase (also called glucoamylase) component of an amylase preparation selectively attacks the last bond on the nonreducing terminals. The type to be used in this experiment can act on both the alpha-1,4 and the alpha-1,6 glucosidic linkages at a relative rate of 1:20, resulting in the splitting off of simple glucose units into the solution. Fungal amylase and amyloglucosidase may be used together to convert starch to simple sugars. The practical applications of this type of enzyme mixture include the production of corn syrup and the conversion of cereal mashes to sugars in brewing.
Thus, it is important to specify the source of enzymes when the actions and kinetics of the enzymes are compared. Four types of alpha-amylases from different sources will be employed in this experiment: three of microbial origin and one of human origin. The effects of temperature, pH, substrate concentration, and inhibitor concentration on the kinetics of amylase catalyzed reactions will be studied. Finally, the action of the amylase preparations isolated from microbial sources will be compared to that from human saliva.
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