Why is amylase important

Enzymes create chemical reactions in the body. They actually speed up the rate of a chemical reaction to help support life. The enzymes in your body help to perform very important tasks. These include building muscle, destroying toxins, and breaking down food particles during digestion. Heat, disease, or harsh chemical conditions can damage enzymes and change their shape. This affects the body processes the enzyme helped support.

For example, enzymes are required for proper digestive system function. Digestive enzymes are mostly produced in the pancreas, stomach, and small intestine. There are three main types of digestive enzymes.

Enzymes are essential for healthy digestion and a healthy body. They work with other chemicals in the body, such as stomach acid and bile, to help break down food into molecules for a wide range of bodily functions. Carbohydrates, for instance, are needed for energy, while protein is necessary to build and repair muscle, among other functions.

But they must be converted into forms that can be absorbed and utilized by your body. Amylase is produced in the salivary glands, pancreas, and small intestine. One type of amylase, called ptyalin, is made in the salivary glands and starts to act on starches while food is still in your mouth. It remains active even after you swallow. Pancreatic amylase is made in the pancreas and delivered to the small intestine. Here it continues to break down starch molecules to sugars, which are ultimately digested into glucose by other enzymes.

Protease is produced in the stomach, pancreas, and small intestine. Most of the chemical reactions occur in the stomach and small intestine. In the stomach, pepsin is the main digestive enzyme attacking proteins. Several other pancreatic enzymes go to work when protein molecules reach the small intestine. Lipase is produced in the pancreas and small intestine.

A type of lipase is also found in breast milk to help a baby more easily digest fat molecules when nursing. Lipids play many roles, including long-term energy storage and supporting cellular health.

Enzymes work best at your normal body temperature. The average body temperature is If you run a fever and your temperature increases too much, the structure of enzymes breaks down. They no longer function properly. Restoring your body temperature to its optimal range will help restore enzyme health. Certain health conditions, such as pancreatitis , which is inflammation of the pancreas, hurts your pancreas and can also reduce the number and effectiveness of certain digestive enzymes.

A low pH means something is very acidic. At this transition point, a second rise was initiated. In LSB trials Fig. Peptic digestion was relatively slow and incomplete. This result is in accordance with findings reported by other researchers indicating that gluten proteins can be quite resistant to in vitro gastric digestion. By comparing the CSB results Fig. However, as previously stated, the second rise in the starch release profile in the absence of HSA Fig.

Indeed, this increase coincided with pepsin activation and degradation of the gluten network, which probably could have led to the release of starch fractions initially entrapped within it. Moreover, these molecular arrangements can also explain, at least in part, the fact that the proportion of starch remaining intact by the end of the gastric digestion trials was about 5 times higher than the fraction of resistant starch found in this bread. This explanation is supported by the distinct protocols used in the resistant starch and digestion experiments.

To determine the resistant starch fraction section 2. Due to this inversion of the proteolytic and amylolytic processes, by the time amylolysis starts, the protein was already digested and the gluten network disrupted, facilitating the hydrolysis of starch which may explain the finding of a smaller fraction of resistant starch. Finally, our results offer a key insight into the digestive process of starchy foods and show the need for accurately replicating the dynamic character of digestive conditions in in vitro studies in order to correctly determine the contribution of each mechanism.

DOI: Received 25th September , Accepted 2nd December Total and resistant starch determination assays were carried out in our laboratory in triplicate. Oral phase. After cutting each crumb cylinder into four lengthwise , a standard volume of baguette crumb was artificially chewed using a domestic kitchen food chopper Multi-Moulinette W, Moulinex, France for 4 segments of 5 s to simulate food comminution through human mastication no liquid was added at this stage.

Each saliva-based bolus was formed by transferring one artificially chewed bread portion into an individual plastic syringe with a cut end, and mixing with 1. The mixing time was set in accordance with in vivo data from a previous work with the same bread 17 and other results from the literature, 31 both reporting chewing times between 18 and 41 s for white wheat bread. Particular attention was paid to prevent an overestimation of HSA's role by defining a bolus hydration level at 0.

Proportion of starch released during the digestion of in vivo and in vitro formed bread boli. Gastric phase. After a 30 s stirring period followed by a 30 s sedimentation step no stirring , the first sample was collected from the supernatant and the in vitro gastric digestion was initiated by activating the influx of pepsin and HCl through the software.

Due to practical experimental limitations e. This was the shortest possible time to complete all the preparatory tasks and initiate the gastric phase. Other parameters were selectively modified to investigate the respective influences of HSA, pepsin and gastric pH reduction kinetics, leading to 4 different types of trials. Released starch.

The samples were treated as solutions of solubilized starch as described in section 2. This method accounts for both solubilized starch fractions and products of starch hydrolysis. The rate of starch digestion was expressed as the percentage of total starch released as a function of time for each type of trial. Released protein.

The maximum activity, found at pH 6. While abnormal amylase levels are often due to problems associated with the pancreas, this isn't always the case. Eating disorders, alcoholism, high triglyceride levels and some medications, including certain diuretics, birth control pills and aspirin, may cause high levels of amylase. High levels could also be due to a condition called macroamylasia, which is usually benign and mostly affects middle-aged men.

Based in Massachusetts, Jessica Bruso has been writing since She holds a master of science degree in food policy and applied nutrition and a bachelor of arts degree in international relations, both from Tufts University. By Jessica Bruso Updated December 17,