Official Full Name
Alkaline Amylase
Background
Alkaline amylase is a kind of alpha-amylase, incision glucosidase. It can hydrolyze starch into short chain dextrine and a small quantity of low molecular saccharide and rapidly reduce viscosity of starch. The function of alkaline amylase as follows: It can effectively decompose starch polysaccharide remains and remove dirt on fabric. Alkaline amylase can improve washing effect at 30°C. For better effect, alkaline amylase can be used with other detergents.
Synonyms
Alkaline Amylase; for detergent; Alkaline amylase; reduce viscosity of starch; decompose starch polysaccharide remains; remove dirt; fabric; Detergent Enzymes; Detergents; Alkaline Amylase for detergent; DETE-2622
Amylase is the general term for enzymes that hydrolyze starch and glycogen. It usually catalyzes the hydrolysis of starch slurry on fabrics by amylase. Due to the high efficiency and specificity of amylase, the desizing rate of enzyme desizing is high, and desizing is fast. Less pollution, the product is softer than acid method, alkali method, and does not damage the fiber. There are many types of amylase. Depending on the fabric, the equipment combination is different, and the process flow is also different. The currently used desizing methods include dipping, stacking, jig dyeing, continuous washing, etc. Because of the small mechanical effect of amylase desizing, the water consumption is small, and the desizing effect can be achieved under low temperature conditions, and it has distinctive environmental protection characteristics.
Figure 1. Protein structure of amylase.
Alkaline amylase
Alkaline amylase is a hydrolytic enzyme that is stable in an alkaline environment (pH 9.0~11.0) and can efficiently hydrolyze starch by cleaving α-1,4-glycosidic bonds. Alkaline amylase can be used in textile desizing, detergent addition and other fields. Studies have found that the application of alkaline amylase in the field of textile desizing can save a lot of time, reduce environmental pollution, and at the same time minimize the damage to the textile fabric itself. This greatly improves the efficiency of the textile pretreatment process and realizes the maximum economic benefits of production. It is one of the key enzyme preparations to promote the rapid development of the textile pretreatment process in the future. At present, the research on alkaline amylase mainly focuses on the screening of production strains, the separation and purification of enzymes and the study of enzymatic properties. When alkaline amylase is used in the textile desizing process and detergent addition process, alkaline amylase is required to have strong oxidation resistance and high catalytic efficiency. However, wild-type alkaline amylase has poor oxidation resistance and low catalytic efficiency, and molecular modification is needed to improve its oxidation resistance and catalytic efficiency.
Clinical significance
Increased serum amylase is more common in acute pancreatitis, it is one of the important diagnostic indicators of acute pancreatitis. Activity begins to increase 6 to 12 hours after onset, peaks at 24 hours, begins to decrease at 48 hours, and returns to normal after 3 to 5 days. Although the degree of increase in amylase activity is not necessarily related to the degree of pancreatic injury, the greater the degree of increase, the greater the possibility of acute pancreatitis, so although amylase is still used as a diagnosis of acute pancreatitis The index is preferred, but its specificity and sensitivity are not high enough. When acute pancreatitis is suspected, the patient's serum and urine amylase activities should be continuously and dynamically observed, and combined with clinical conditions and other tests, such as pancreatic lipase, trypsin and other measurements, to make a diagnosis.
References
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Ramasubbu N.; et al. Structure of human salivary alpha-amylase at 1.6 Å resolution: implications for its role in the oral cavity. Acta Crystallographica D. 1996, 52 (3): 435–446.
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Rejzek M.; et al. Chemical genetics and cereal starch metabolism: structural basis of the non-covalent and covalent inhibition of barley β-amylase. Molecular BioSystems. 2011, 7 (3): 718–730.