When we eat food, we are digesting polymeric macromolecules called Digestive Enzymes. These enzymes break down these large molecules into smaller building blocks so that they can be easily absorbed by the body. There are several types of Digestive Enzymes. Here are a few of them:
The production of commercial phytase is limited by the price and availability of fungal hosts. The enzyme has higher titers and can be produced with post-translational modifications such as N-linked glycosylation. Phytase is also inactive at high temperatures, which makes its use in feed limited. To overcome these limitations, natural phytase has been considered as a feed additive. Its activity is high enough to hydrolyze phytate in the fish gut.
The phosphorus-releasing effect of phytase was enhanced by super-dosing. This enzyme released more phosphorus during bone development. The extra phosphoric effect of phytase is attributed to its ability to release amino acids, phosphorus and calcium from phytate. Furthermore, it enhanced feed utilisation and conversion in animals. Optiphos was found to have these super-dosing effects when dosed twice.
The digestive enzyme amylase is produced by the salivary glands and pancreas. The main function of amylase is to break down starches in food. Amylase levels in the blood can indicate the underlying cause of sudden abdominal pain. Although amylase levels in the blood may not be an indication of a disease, they may indicate the presence of pancreatic issues. Amylase is found in saliva and in low levels in the liver and other body tissues.
There are two types of amylase. Amylases belong to the glycoside hydrolase family and act at random locations along the chain of starch. Amylase breaks down starch into maltose and maltotriose. Both types are present in the body and are produced by fungi, bacteria, and plants. Amylases can be found in saliva, the pancreas, and other body fluids.
The role of proteolytic enzymes in digestion is often overlooked, but they have important health benefits. Among other things, proteolytic enzymes reduce the risk of cancer, reduce inflammation, and help the body produce more life-extending enzymes. They are particularly useful for people with inflammatory bowel disease, coeliac disease, and ulcers. The best form of proteolytic enzymes for humans is a delayed release capsule, which has an enteric coating that prevents premature breakdown in the stomach.
These enzymes break down long chains of protein into smaller fragments, which are then broken down into amino acids. They are produced by the pancreas and are often referred to as protease or proteinase. Some of these enzymes work on specific sites and are called exopeptidases. Proteolytic enzymes are also produced naturally in plants. They include bromelain and papaya, as well as glutamic, metalloendopeptidases, and serine and threonine enzymes.
The role of trypsinogen is unclear in pancreatitis, an inflammatory disease that starts in the acinar cells of the pancreas. This disease is associated with considerable morbidity and mortality. Despite the fact that the mechanism behind pancreatitis is unclear, some evidence suggests that premature trypsinogen activation plays a role. Although premature activation of trypsinogen is considered a major cause of pancreatitis, recent studies suggest that other factors are also involved. For example, the results of Trypsinogen-7 knockout mice have demonstrated that local inflammation proceeds independently of systemic inflammation in hereditary pancreatitis.
The role of trypsinogen in pancreatitis is unclear, but there is evidence that the enzyme can stimulate the production of other pancreatic enzymes. In fact, a German pathologist first observed that intra-pancreatic digestive enzymes are activated in pancreas autopsies. Since that time, animal models of pancreatitis have been developed. Most of them exhibit early activation of trypsinogen, and this prompted pancreatitis research to focus on the mechanisms that activate it.