Amylase (enzyme) - sources & its applications
- 1. AMYLASE sources & clinical applications - NEERAJA.A
- 2. DEFINITION • Amylase is an enzyme that helps digest carbohydrates. • It is made in the pancreas and the glands that make saliva. When the pancreas is diseased or inflamed, amylase releases into the blood. • A test can be done to measure the level of this enzyme in blood. • Amylase may also be measured with an amylase urine test. • Amylase was the first enzyme to be discovered and isolated (by Anselme Payen in 1833).
- 3. TYPES • All amylases are glycoside hydrolases and act on α-1,4-glycosidic bonds • Amylase can be classified into 3 types:. 1.α- Amylase 2. β-Amylase 3. γ-Amylase
- 4. α- AMYLASE • Alternative names: 1,4-α-D-glucan glucanohydrolase; glycogenase. • They are calcium metalloenzymes, completely unable to function in the absence of calcium. • α-amylase breaks down long-chain carbohydrates, ultimately yielding maltotriose and maltose from amylose, or maltose, glucose and "limit dextrin" from amylopectin. • Iit 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. • In human physiology, both the salivary and pancreatic amylases are α- amylases.
- 5. β-AMYLASE • Alternative names: 1,4-α-D-glucan maltohydrolase; glycogenase; saccharogen amylase. • 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). • During the ripening of fruit, β-amylase breaks starch into maltose, resulting in the sweet flavor of ripe fruit. • 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. • Microbes also produce amylase to degrade extracellular starches. • The optimum pH for β-amylase is 4.0–5.0.
- 6. γ-AMYLASE • Alternative names: Glucan 1,4-α-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 linkages at the nonreducing end of amylose and amylopectin, yielding glucose. • The γ-amylase has most acidic optimum pH of all amylases because it is most active around pH 3.
- 7. SOURCES • Amylase is obtained from the following sources: 1.Pancreas 2.Salivary glands 3.Microorganisms
- 8. BACTERIAL SOURCE • Amylase is produced by different species of bacteria, but commercially it is produced by the following species. 1. Bacillus licheniformis 2. B. sterothermophilis 3. B. amyloliquefaciens 4. B. subtilis 5. B. polymyxia 6. B. vulgarus.
- 9. FUNGAL AMYLASE • Amylase is produced by different species of fungi, but commercially it is produced by the following species. 1. Aspergillus orizae 2. A. niger 3. Penicillium sps. 4. Thermomyces lanuginosus
- 10. SIGNIFICANCES • Amylase is used in: 1. Textile industry- for desizing process, weaving process. 2. Paper industry- modification of starch. 3. Food industry- brewing, strarch syrup. 4. Baking industry- to prepare dough of bread.
- 11. SIGNIFICANCES • This formula contains digestive enzymes which help digest fats (lipids), sugars, proteins, carbohydrates, gluten, fruits and vegetables, cereals, legumes, bran, nuts and seeds, soy, dairy and all other food sources. • VeganZyme may also be used as a systemic enzyme blend to break down excess mucus, fibrin, various toxins, allergens, as well as excess clotting factors throughout your body.
- 12. CLINICAL SIGNIFICANCES • Used in diagnosis and monitoring pancreatitis. • 1.Acute: transient increase in activity with 2- 12 hours. • 2.Serum amylase may be raised in bile duct obstruction. • 3.Raising amylase activity in salivary gland diseases.
- 13. The Health Benefits of Amylase 1. Help Lower Autoimmune Responses 2. Resistant to Swelling and Redness 3. Compromised Health Support
- 14. Help Lower Autoimmune Responses • Amylase could help slow the aggregations of antigens (molecules that trigger immune responses), as well as the resulting tissue damage from the heightened conglomeration of antibodies (immune system proteins that neutralize foreign cells). • Aamylase can play a role in boosting immunomodulatory activity halting these strong immune states.
- 15. Resistant to Swelling and Redness • Patients with rheumatic diseases taking amylase enzyme experienced anti-swelling effects.
- 16. Compromised Health Support • The amylase enzyme in particular was found to show amazing abilities in inhibiting the growth of tumor cells with metastatic capacities. • Enzyme therapy can reduce the adverse effects caused by radiotherapy and chemotherapy. • There is also evidence that, in some types of tumors, survival may be prolonged.
- 17. CAUSES • Signs of deficiency may include skin rash, allergies, gas, constipation, mood imbalances, and general digestive upset. • What is more, having sufficient amylase activity reduces contributors to some degenerative diseases, as it helps the body digest and excrete dead white blood cells. • Without proper amylase activity, irritation can be excessive. • Low amylase is also thought to be a factor in a variety of diseases including type II diabetes, blood sugar imbalances, hypoglycemia, carbohydrate and sugar cravings, and many forms of food sensitivities.
- 18. CONCLUSION • Use of amylase in starch based industries have been prevalent for many decade. • Selected strains of fungi and bacteria only meet the criteria for commercial production. • New development in amylase purification technique enables application in pharmaceutical and clinical sectors.