Kleistase TU 20
Diastase
CAS: 9000-92-4
Molecular Formula:
Kleistase TU 20 - Names and Identifiers
Kleistase TU 20 - Physico-chemical Properties
| Solubility | Sparingly soluble in water (except when admixed with an insoluble diluents ); insoluble in ethanol (95 per cent) and in ether |
| Appearance | White powder |
| Color | white |
| Odor | Odorless |
| Merck | 599 |
| Storage Condition | 2-8°C |
| Stability | Stable. Incompatible with strong oxidizing agents. |
| Physical and Chemical Properties | Malt amylase is an amylase mixture extracted from malt. It is a light yellow or white amorphous powder, odorless and tasteless. Dissolved in water and slightly turbid. Optimum Ph5.0 ~ 5.5, the aqueous solution is inactivated at Ph1.7 or heated to 860C. |
| Use | Desizing process for textiles |
Kleistase TU 20 - Risk and Safety
| Hazard Symbols | Xn - Harmful |
| Risk Codes | 42 - May cause sensitization by inhalation |
| Safety Description | S22 - Do not breathe dust. S24 - Avoid contact with skin. S36/37 - Wear suitable protective clothing and gloves. |
| WGK Germany | 2 |
| RTECS | BU7430000 |
| FLUKA BRAND F CODES | 3-10 |
| Toxicity | LD50 oral in rat: > 15gm/kg |
Kleistase TU 20 - Upstream Downstream Industry
| Downstream Products | Gentamycin Solution |
Kleistase TU 20 - Reference
| Reference Show more | 1. [IF=6.953] Hui Zhang et al."Interaction between barley β-glucan and corn starch and its effects on the in vitro digestion of starch."Int J Biol Macromol. 2019 Dec;141:240 2. [IF=1.767] Shiguo Liu et al."Hanseniaspora pseudoguilliermondii Improves the Flavor of Tilapia Fish Protein Hydrolysates."J Aquat Food Prod T. 2022;31(4):297-310 3. [IF=4.952] Jie Chen et al."A turn-on fluorescence biosensor for sensitive detection of carbaryl using flavourzyme-stabilized gold nanoclusters."Lwt Food Sci Technol. 2022 Mar;157:113099 |
Kleistase TU 20 - Nature
Open Data Verified Data
This product is an enteric-coated pill made of amylase. Can decompose starch, the strongest role in the acidic environment.
Last Update：2024-01-02 23:10:35
Kleistase TU 20 - Introduction
1 U corresponds to the amount of enzyme which liberates 1 μmol maltose per minute at pH 6.0 and 25°C
Last Update：2022-10-16 17:29:43
Kleistase TU 20 - Use
Open Data Verified Data
- digestive aid.
- formulation pellets each contained 0.2g of amylase. Additional tablets.
- usage and dosage for dyspepsia caused by amylase deficiency. Oral 1~2 tablets, 3 times a day.
- attention should be paid to the long days and the efficacy is reduced, so the new preparation should be used.
Last Update：2022-01-01 11:11:19
Kleistase TU 20 - Safety
Open Data Verified Data
closed storage in the dark.
Last Update：2022-01-01 11:11:19
Kleistase TU 20 - Reference Information
| pH range of acid-base indicator discoloration | 5.5 - 6.0 |
| EPA chemical substance information | information provided by: ofmpeb.epa.gov (external link) |
| Introduction | amylase is a general term for enzymes that hydrolyze starch and glycogen. Amylase is usually used to catalyze the hydrolysis of starch slurry on fabrics, due to the high efficiency and specificity of amylase, the Desizing rate of enzyme Desizing is high, the Desizing rate is fast, the pollution is less, the product is softer than the acid method and the alkali method, and the fiber is not damaged. |
| Primary Function | amylase is a digestive enzyme secreted primarily by the pancreas and salivary glands, but is rarely found in other tissues. Amylase was first described in the 1800s and is considered to be one of the first enzymes to be studied scientifically in history. It was originally called an objectionable digestive juice, but was later renamed amylase in the early 20th century. The main function of amylases is to hydrolyze the glycosidic bonds in starch molecules, converting complex carbohydrates into monosaccharides. Amylases are mainly divided into three categories: α-,β-and γ-amylases act on different parts of the carbohydrate molecule, respectively. Alpha-amylases can be found in humans, animals, plants, and microorganisms. Beta-amylase is present in microorganisms and plants. Gamma-amylase is present in plants and animals. In 1908, a study conducted by wohlgemurs identified the presence of amylase in the urine, which subsequently led to the use of amylase as a diagnostic laboratory test. Amylase is a commonly used assay with lipase, especially in cases of suspected acute pancreatitis. |
| The Source of amylase | There are two main isozymes of amylase in vivo, one is Pancreatic amylase: mainly by the pancreas, testicular cell synthesis, the pancreas is the main organ for the synthesis of amylase; The other is salivary amylase: mainly from the salivary glands are also found in the lung, ovary and other tissues. what can be explained by the distribution source of amylase? (1) These tissue diseases will cause the increase of serum amylase;(2) The pancreas is the main organ of the synthesis of amylase, therefore, diseases of tissues and organs around the pancreas can also involve the pancreas and cause elevated serum amylase. |
| properties | in the enzymology, amylase is a metalloenzyme, specifically calcium ion metalloenzyme. This property of amylase determines:(1) in the pathophysiology, the calcium ion level is closely related to amylase and acute pancreatitis;(2) in clinical laboratory, requirements for amylase test samples, namely, the usual sodium citrate, EDTA, and even heparin (although the main anticoagulant mechanism of heparin is not chelated calcium ions, but heparin also has calcium ion binding sites) samples of calcium-binding anticoagulants are not desirable for the detection of amylase. In terms of molecular weight, the molecular weight of the amylase is about 45KD. The 45KD molecular weight indicates that amylase is a medium molecular weight protein, so amylase can be partially filtered out through the glomerular filtration membrane, which appears in the urine. It also indicates that the renal filtration ability will affect the level of urine amylase, diseases that decrease glomerular filtration capacity may cause a mild increase in blood amylase. |
| pathophysiology | The primary function of amylases is to catalyze the hydrolysis of starch to sugars. Several amylase isoforms have been found, but the most abundant are Pancreatic amylase (P-amylase) and salivary amylase (S-amylase), synthesized by acinar cells and then secreted into the gastrointestinal tract. S-amylase is mainly produced in the salivary glands, but can also be produced in the ovaries, fallopian tubes, gastrointestinal tract, lungs, striated muscles, and malignant tumors. Serum amylase is tightly regulated in vivo. There is a balance between productivity and clearance. Increased amylase may be due to decreased clearance due to increased pancreatic or extra-pancreatic production. amylases have a molecular weight of about 50 to 55 kDa, an optimal physiological pH of 6.7 to 7.0, and require calcium and chloride ions to achieve optimal enzyme activity. The small size makes it easy to filter through the glomerulus. Amylase is cleared by the kidney and the reticuloendothelial system. |
| Clinical significance | amylase is mainly used in the diagnosis of pancreatic diseases. Amylase is a commonly used enzyme because it provides an inexpensive, easily automated process. Although amylase is a sensitive indicator of acute pancreatitis, it is not specific because it can be elevated in several cases that are not associated with the pancreas. Pancreatitis can be defined by two of the following three criteria: Abdominal Pain, serum amylase and/or lipase levels above three times the upper limit of normal, and abdominal imaging to support the characteristic findings of pancreatitis. Therefore, its clinical significance has been questioned. If the level of amylase is elevated and there is little support for pancreatitis, other causes of hyperamylasemia should be considered. Amylase cannot be used to predict the severity of an acute pancreatic attack or to monitor the condition. amylase inhibitors such as acarbose have been used to treat type 2 diabetes and have been shown to reduce hemoglobin A1C and postprandial blood glucose spikes. Acarbose has also been shown to improve remission of dumping syndrome in obese patients. The drug has also been shown to improve the risk of cardiovascular disease by slowing the thickening of the carotid artery. Elevated amylases can be observed under a variety of conditions. When hyperamyloidaemia is found, it is important for the clinician to take a clear, step-by-step approach. This will help to avoid unnecessary hospitalization and delayed or inappropriate treatment. |
| toxicity | FAO/WHO(2001) regulation by Bacillus licheniformis (B.licheni formis), et al., produced α-amylase, ADI without limitation (see 16028,α-amylase). GRAS(FDA,§ 184.1027.2000). |
| Use limit | GB 2760-2002 fungal amylase preparation: baked products, fermented wine, starch sugar industry, fruit juice, vegetable processing, alcohol industry, all GMP. Alpha-amylase (Aspergillus oryzae): baked products, starch industry, alcohol, brewing, juice industry, isomaltooligosaccharide production process, GMP." Amylase (eosinophilic Prussian Bacillus): GMP for brewing and juice industry. Shovel amylase (Bacillus amyloliquefaciens): starch, alcohol, baking, brewing industry, GMP. Namely amylase (Bacillus licheniformis): Brewing, alcohol, starch industry, GMP." Amylase (Bacillus subtilis): starch, baking industry, GMP. Beta-amylase: starch and food processing industries, GMF,. |
| Use | enzyme preparation for Desizing process of textiles. Enzyme preparation is the most widely used, one of the largest consumption. It is mainly used for dough improvement in bread production (reducing dough viscosity, accelerating fermentation process, increasing sugar content, easing bread aging); Pretreatment of cereal raw materials in infant food (Starch Hydrolysis); saccharification and decomposition of undecomposed starch in beer manufacturing; Liquefaction and saccharification of starch in sake production; Saccharification and decomposition of undecomposed starch in alcohol industry; starch decomposition and increase the filtration rate in juice processing; And vegetable processing, syrup manufacturing, sugar production, powder dextrin, glucose and other processing manufacturing. |
| production method | by Aspergillus niger var. Aspergillus oryzae (Asp.orzae vsr.) rhizopus oryzae. Trichoderma (Tricho-derma roesei; var.) variety of bacteria, mold in the appropriate conditions after the culture, the mother liquor: 1. After spray drying, pulverization; 2. After salting out with salt, separation, drying and pulverization; 3. Adding a solvent such as ethanol to precipitate the enzyme, followed by separation, drying, and pulverization; 4. The enzyme was adsorbed with a refined starch and then dried. maltogenic amylase is a digestive enzyme. Starch in food is a high molecular compound that must be produced by the digestive tract enzymes to produce small molecules of glucose before it can be absorbed. This product can promote the digestion of starch in food. Suitable for loss of appetite, indigestion, gastric mucosal inflammation. Oral, 100 ~ 500mg each time, each time 1~2 tablets, 3 times a day. Cold dark place, avoid humidity, closed storage. |
Last Update：2024-04-09 20:52:54
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CAS: 9000-92-4
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Product Name: Diastase Request for quotation
CAS: 9000-92-4
Tel: 17505222756
Email: pules.cn@gmail.com
Mobile: +86-17551318830
Wechat: 17505222756
CAS: 9000-92-4
Tel: 17505222756
Email: pules.cn@gmail.com
Mobile: +86-17551318830
Wechat: 17505222756
Spot supply
Product Name: Diastase from Aspergillus oryzae Visit Supplier Webpage Request for quotationCAS: 9000-92-4
Tel: 18301782025
Email: 3008007409@qq.com
Mobile: 18021002903
QQ: 3008007409
Wechat: 18301782025
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Downstream Products for Kleistase TU 20