Is Amylase An Enzyme? 9 Interesting Facts (Read This First!)


Amylase is an enzyme or particular protein that aids in the breakdown of carbohydrates. Your pancreas and salivary glands produce the majority of the amylase that is found in your body.

Amylase is an enzyme that aids in the breakdown of starch to produce smaller carbohydrate molecules like maltose. Amylases fall into one of three categories: alpha, beta, or gamma, depending on how they break down the bonds between starch molecules.

  • Why is amylase an enzyme?
  • How is amylase an enzyme?
  • What kind of enzyme is amylase?
  • Where is amylase enzyme found?
  • Functions of amylase enzyme?
  • Structure of amylase enzyme?
  • Is amylase enzyme a protein?
  • What is important about amylase enzyme?
  • How amylase is produced and when?

Why is amylase an enzyme?

A hydrolytic enzyme called amylase converts starch into dextrins and sugars. It is composed of a group of enzymes that break down starch, including alpha-amylase. Beta-amylase.

Our body can utilise the sugar produced by the enzyme amylase to produce energy. The undigested carbs may cause diarrhoea if you don’t have enough amylase.

How is amylase an enzyme?

The hydrolysis (breaking down) of starch, glycogen, and similar polysaccharides into more basic and easily digestible forms of sugar is facilitated by an enzyme called Amylase found in saliva and pancreatic juice. The (1-4) glycosidic connections are broken down.

An essential and significant enzyme known as amylase is crucial to the field of biotechnology.

What kind of enzyme is amylase?

Amylase is a digestive enzyme that is mostly released by the pancreas and salivary glands and is also present in very minute amounts in other tissues. One of the earliest enzymes in human history to receive scientific study, amylase was initially described in the early 1800s.

Amylases are starch-degrading enzymes that limit the amount of dextrins by facilitating the hydrolysis of internal 1-4 glycosidic bonds in polysaccharides.

The essential digestive enzymes amylase. Your body uses amylase to break down starches.

Amylase is a member of the hydrolases family of hydrolytic enzymes. 1,4-D-Glucan glucanohydrolase, EC 3.2.1, is the scientific name for amylase. Maltose (-glucose disaccharides) is created when -amylase hydrolyzes the –(1-4) glycoside bonds of amylase.

Where is amylase enzyme found?

Humans and several other mammals have amylase in their saliva, where it starts the chemical process of digesting. Amylase is also produced by several microorganisms and plants.

Because amylase converts some of the starch in foods that are high in starch but low in sugar, such rice and potatoes, they may taste a little bit sweet when chewed.

To hydrolyze dietary starch into disaccharides and trisaccharides, which are then transformed by other enzymes to glucose to provide the body with energy, the pancreas and salivary gland produce amylase (alpha amylase).

Different Greek letters are used to identify particular amylase proteins. Since they all work on -1,4-glycosidic linkages, amylases are glycoside hydrolases.

Functions of amylase enzyme?

Amylases are utilised to convert complex sugars like starch and sugars like glucose into simple sugars and are also employed in the baking of bread. The waste products ethanol and carbon dioxide are produced as a result of yeast feeding on these simple carbohydrates.This gives the bread flavour and makes it rise.

In the process of making traditional beer, boiling water is added to malted barley to form a “mash,” which is then maintained at a specific temperature to allow the amylases in the malted grain to turn the starch in the barley into sugars.

By incorporating amylases (typically in the form of malted barley) into bread improver, modern breadmaking procedures have sped up and made the process more suitable for commercial use.

The ingredient list for commercially packaged milked flour frequently includes amylase. Long-term exposure to flour supplemented with amylase increases the risk of dermatitis or asthma in bakers.

The presence of amylase can be utilised as a further approach in molecular biology to select for the efficient integration of a reporter construct, in addition to antibiotic resistance.

The amylase gene will be disrupted and prevented from degrading starch, which can be seen through iodine staining, if integration is successful. Homologous portions of the structural amylase gene are located on each side of the reporter gene.

Amylase is used in pancreatic enzyme replacement and other medicinal settings (PERT). One of the ingredients in Sollpura (liprotamase), which aids in the conversion of saccharides into simple sugars, is this ingredient.

Additionally, dishwashing detergents and laundry detergents use bacilliary amylase to break down starches in fabrics and dishes.

Structure of amylase enzyme?

Human amylase protein has a recognised three-domain structure that starts at the amino terminus and is designated as A, B, and C. Calcium binds to the B domain and may stabilise the active site, which is located in the A domain . A globular domain with an unidentified function is the C domain.

Is amylase an enzyme
α-Amylase from Wikipedia

Chloride changes the pH optimal and the maximum activity of several amylases, including human pancreatic amylase. Five subsites in the amylase’s active centre allow it to bind various substrate glucose residues. In, the current state of knowledge on the enzymatic mechanism for glycosidases is reviewed.

Is amylase an enzyme
β-Amylase from Wikipedia

There are more carbohydrate binding sites, according to kinetic evidence. A few of these are surface binding sites that aid in the amylase’s ability to attach to starch granules.

Is amylase enzyme a protein?

The cDNA predicts a protein of 512 amino acids for human pancreatic -amylase, which is produced as a 57 KDa protein.The body makes proteins called enzymes to carry out specific tasks. To convert the complex carbohydrates in diet into simple sugars, the pancreas makes amylase.

The main digestive enzyme operating on starch or glycogen is known as amylase (1,4-D-glucan-glucanohydrolase; EC 3.2.1.1), and it can be found in plants, animals, bacteria, and fungus.

Plant starch is a glucose polymer with a high molecular weight. It is composed of amylopectin, a branched chain polymer with -1,4 connected glucose and branch points made up of -1,6 links, and amylose, a straight-chain -1,4 linked polymer of approximately 105 units.

Animal glycogen has a structure that is comparable to amylopectin but is smaller. When the -1,4 linkage is not close to a branch point or a terminal glucose residue, -amylase breaks it. Thus, its end products are -limit dextrins, maltose (2 glucose residues), and maltotriose (3 glucose residue.

What is important about amylase enzyme?

The primary job of amylases is to hydrolyze the glycosidic linkages in molecules of starch, turning them to simple sugars. The three primary kinds of amylase enzymes—alpha, beta, and gamma—each affect the carbohydrate molecule in a different way.

Your pancreas and salivary glands both produce amylase. When food reaches your small intestine, pancreatic amylase and other digestive enzymes complete the breakdown of the carbohydrates in what you consume, which is started by salivary amylase.

Our body uses the glucose produced after all forms of carbohydrates have been completely metabolised for energy. Glucose is also the preferred fuel for your brain and nervous system.

As food is digested and combined with saliva, the salivary glands’ amylase starts the enzymatic breakdown of starches in the mouth. It may come as a surprise, but basic chewing in your mouth really initiates the breakdown of larger, more complicated carbohydrates into simpler sugars.

Our body’s amylases break down starch into the two sugars maltose and isomaltose, which are then hydrolyzed by the enzymes maltase and isomaltase into the monosaccharide glucose. According to research, amylase can serve as a very reliable and helpful indicator of stress levels.

How amylase is produced and when?

The salivary glands and the pancreas are the primary sources of amylase in the human body. Amylase is also produced by several microorganisms and plants.

Despite having a similar structure, salivary and pancreatic amylases are encoded by separate genes (AMY1 and AMY2, respectively), and their levels of activity against different types of starches differ.

Amylases are known to be active in a wide range of temperature (40–90°C) and pH (4–11). The optimum temperature of this amylase was 50ºC, which is similar to that described for other Bacillus amylases (15, 7).

Physiologic concentrations of norepinephrine enhance amylase release from dispersed pancreatic acini evoked by supramaximal concentrations of cholecystokinin.

Conclusion

Amylase is a digestive enzyme predominantly secreted by the pancreas and salivary glands and found in other tissues in very small levels. Amylase was first described in the early 1800s and is considered one of the first enzymes in history to be scientifically investigated.

Sadiqua Noor

I'm a recent post graduate in biotechnology, my area of interest is molecular biology and genetics, apart from these i have keen interest in scientific article writing in simpler words so that the people from non science background can also understand the beauty and gifts of science. I had 5 years experience as a tutor.

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