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Cellulase

Official Full Name
Cellulase
Background
Product exhibits endo-cellulase, β-glucanase activity and β-mannase activities when assayed using insoluble AZCL-linked substrates as well as exo-cellulase and cellobiohydralase activities.
Synonyms
1#4-(1#3:1#4)-β-D-Glucan 4-glucano-hydrolase; EC 3.2.1.4; endo-1#4-β-D-glucanase; β-1#4-glucanase; β-1#4-endoglucan hydrolase; celluase A; cellulosin AP; endoglucanase D; alkali cellulase; cellulase A 3; celludextrinase; 9.5 cellulase; avicelase; pancellase SS

Catalog
ProductName
EC No.
CAS No.
Source
Price
CatalogNATE-1750
EC No.EC 3.2.1.4
CAS No.9012-54-8
Source
CatalogNATE-1749
EC No.EC 3.2.1.4
CAS No.9012-54-8
Source
CatalogEXWM-3902
ProductNamecellulase
EC No.EC 3.2.1.4
CAS No.9012-54-8
Source
CatalogNATE-1606
EC No.
CAS No.
SourceThermobifida ha...
CatalogNATE-1374
EC No.EC 3.2.1.4 & EC 3.2.1.72
CAS No.9012-54-8
SourceE. coli
CatalogNATE-1373
EC No.EC 3.2.1.4
CAS No.9012-54-8
SourceE. coli
CatalogNATE-1372
EC No.EC 3.2.1.4
CAS No.9012-54-8
SourceE. coli
CatalogNATE-1371
EC No.EC 3.2.1.4
CAS No.9012-54-8
SourceE. coli
CatalogNATE-1370
EC No.EC 3.2.1.73 & EC 3.2.1.4
CAS No.
SourceE. coli
CatalogNATE-1369
EC No.EC 3.2.1.4
CAS No.9012-54-8
SourceE. coli
CatalogNATE-1368
EC No.EC 3.2.1.4
CAS No.9012-54-8
SourceE. coli
CatalogNATE-1367
EC No.EC 3.2.1.4
CAS No.9012-54-8
SourceE. coli
CatalogNATE-1366
EC No.EC 3.2.1.4
CAS No.9012-54-8
SourceE. coli
CatalogNATE-1365
EC No.EC 3.2.1.4
CAS No.9012-54-8
SourceE. coli
CatalogNATE-1364
EC No.EC 3.2.1.4
CAS No.9012-54-8
SourceE. coli
CatalogNATE-1363
EC No.EC 3.2.1.4
CAS No.9012-54-8
SourceE. coli
CatalogNATE-1362
EC No.EC 3.2.1.4
CAS No.9012-54-8
SourceE. coli
CatalogNATE-1361
EC No.EC 3.2.1.4
CAS No.9012-54-8
SourceE. coli
CatalogNATE-1360
EC No.EC 3.2.1.4
CAS No.9012-54-8
SourceE. coli
CatalogNATE-1359
EC No.EC 3.2.1.4
CAS No.9012-54-8
SourceE. coli
CatalogNATE-1358
EC No.EC 3.2.1.4
CAS No.9012-54-8
SourceE. coli
CatalogNATE-1357
EC No.EC 3.2.1.4
CAS No.9012-54-8
SourceE. coli
CatalogNATE-1356
EC No.EC 3.2.1.4
CAS No.9012-54-8
SourceE. coli
CatalogNATE-1355
EC No.EC 3.2.1.4
CAS No.9012-54-8
SourceE. coli
CatalogNATE-1354
EC No.EC 3.2.1.-
CAS No.9012-54-8
SourceE. coli
CatalogNATE-1353
EC No.EC 3.2.1.4
CAS No.9012-54-8
SourceE. coli
CatalogNATE-1352
EC No.EC 3.2.1.4
CAS No.9012-54-8
SourceE. coli
CatalogNATE-1351
EC No.EC 3.2.1.4
CAS No.9012-54-8
SourceE. coli
CatalogNATE-1350
EC No.EC 3.2.1.4
CAS No.9012-54-8
SourceE. coli
CatalogNATE-1349
EC No.EC 3.2.1.4
CAS No.9012-54-8
SourceE. coli
CatalogNATE-1348
EC No.EC 3.2.1.4
CAS No.9012-54-8
SourceE. coli
CatalogNATE-1347
EC No.EC 3.2.1.4
CAS No.9012-54-8
SourceE. coli
CatalogNATE-1346
EC No.EC 3.2.1.4
CAS No.9012-54-8
SourceE. coli
CatalogNATE-1345
EC No.EC 3.2.1.4 and EC 3.2.1.151
CAS No.9012-54-8
SourceE. coli
CatalogNATE-1344
EC No.EC 3.2.1.4 and EC 3.2.1.78
CAS No.9012-54-8
SourceE. coli
CatalogNATE-1343
EC No.EC 3.2.1.4
CAS No.9012-54-8
SourceE. coli
CatalogNATE-1342
EC No.EC 3.2.1.4
CAS No.9012-54-8
SourceE. coli
CatalogNATE-1341
EC No.EC 3.2.1.4
CAS No.9012-54-8
SourceE. coli
CatalogNATE-1338
EC No.EC 3.2.1.4
CAS No.9012-54-8
SourceE. coli
CatalogNATE-1337
EC No.EC 3.2.1.4
CAS No.9012-54-8
SourceE. coli
CatalogNATE-1336
EC No.EC 3.2.1.4
CAS No.9012-54-8
SourceE. coli
CatalogNATE-1335
EC No.EC 3.2.1.-
CAS No.9012-54-8
SourceE. coli
CatalogNATE-1334
EC No.EC 3.2.1.4
CAS No.9012-54-8
SourceE. coli
CatalogNATE-1333
EC No.EC 3.2.1.4
CAS No.9012-54-8
SourceE. coli
CatalogNATE-1200
EC No.EC 3.2.1.4
CAS No.9012-54-8
SourceCellvibrio mixt...
CatalogNATE-1058
EC No.EC 3.2.1.4
CAS No.9012-54-8
SourceTalaromyces eme...
CatalogNATE-1057
EC No.EC 3.2.1.4
CAS No.9012-54-8
SourceTrichoderma lon...
CatalogNATE-1056
EC No.EC 3.2.1.4
CAS No.9012-54-8
SourceBacillus amylol...
CatalogNATE-1055
EC No.EC 3.2.1.4
CAS No.9012-54-8
SourceThermotoga mari...
CatalogNATE-0121
EC No.EC 3.2.1.4
CAS No.9012-54-8
SourceE. coli
CatalogNATE-0120
EC No.EC 3.2.1.4
CAS No.9012-54-8
SourceTrichoderma ree...
CatalogNATE-0119
EC No.EC 3.2.1.4
CAS No.9012-54-8
SourceTrichoderma sp.
CatalogNATE-0118
EC No.EC 3.2.1.4
CAS No.9012-54-8
SourceAspergillus nig...
Related Reading

Cellulase is a generic term for a group of enzymes that degrade cellulose to produce glucose. It is not a monomer enzyme, but a multi-component enzyme system that acts synergistically. Cellulase is a complex enzyme mainly composed of exo-β-glucanase, endo-β-glucanase and β-glucosidase, as well as a highly active xylanase. Cellulases act on cellulose and products derived from cellulose. Microbial cellulase is of great importance in converting insoluble cellulose into glucose and destroying the cell wall in fruit and vegetable to increase the yield of juice.

Sources

Cellulase is widely present in natural organisms. Cellulases can be produced in bacteria, fungi, and animals. Cellulase from different sources differ greatly in their structure and function. Due to the high yield and high acivity, cellulases generally used in production are derived from fungi, typically Trichoderma, Aspergillus and Penicillium. The yield of cellulase produced by bacteria is less, mainly endoglucanase. Most of them have no degrading activity to crystalline cellulose, and are intracellular enzymes or adsorbed on the cell wall with no secretion into the culture fluid, which increase the difficulty of extraction and purification. Therefore, there has been less studies on bacteria cellulase. However, cellulase produced by bacteria generally has an optimum pH of neutral to alkaline. In the past 20 years, with the successful application of neutral cellulase and alkaline cellulase in the cotton fabric washing finishing and detergent industry, bacterial cellulase preparations have shown good application prospects.

Classification

Cellulases can be classified into endoglucanases (1,4-β-D-glucan glucanohydrolase or endo-1,4-β-D-glucanase, EC3.2.1.4), exoglucanase (1,4-β-D-glucan cellobilhydrolase or exo-1,4-β-D-glucannase, EC.3.2.1.91), and β-glucosidase (EC.3.2.1.21). Endoglucanases randomly cleave the amorphous regions inside the cellulose polysaccharide chains, producing oligosaccharides with different lengths. Exoglucanases act on the ends of these reducing and non-reducing cellulose polysaccharide chains to release glucose or cellobiose. β-glucosidases hydrolyze cellobiose to produce two glucoses.

Catalytic Mechanism

The cellulase reaction is not the same as general enzyme reaction. The main difference is that cellulase is a multi-component enzyme system and the structure of the substrate is extremely complicated. Due to the water insolubility of the substrate, the adsorption of cellulase replaces the process of ES complex formation by the enzyme and the substrate. The cellulase is specifically adsorbed on the cellulose first, and then the cellulose is decomposed into glucose under the synergistic action of several components. In 1950, scientists proposed the C1-Cx hypothesis, which states that it is necessary to act synergistically with different enzymes in order to completely hydrolyze cellulose to glucose. Synergy is generally thought to be that the C1 enzyme first attacks the amorphous region of cellulose, forming the new free ends needed for Cx. Then, the Cx enzyme cuts cellobiose units from the reducing or non-reducing ends of the polysaccharide chains. Finally, the cellobiose is hydrolyzed into two glucose by β-glucanase. However, the order of synergy of cellulases is not absolute. In subsequent studies, it was found that C1-Cx and β-glucosidase must be present together to hydrolyze native cellulose.

Applications

Food industry: Cellulase is used for peeling in the processing of soybean paste, which greatly reduces the cost while improving product quality. The use of cellulase can also improve the baking and nutritional quality of the noodle products and extend the shelf life. Fruit and vegetables contain a lot of cellulose. If you use traditional methods to process fruits and vegetables, it will destroy the taste and loss of nutrition. However, if treated with cellulase, the plant tissue will be softened and good for absorbing by the body. Therefore, the use of food-grade enzyme preparations for the effective degradation of fruits can increase the yield of juices, improve the color of the products and increase the stability.

Brewing industry: Cellulase is used in beer fermentation. Addition of cellulase to a small amount of barley germination can effectively degrade β-1,3-glycosidic bonds and β-1,4-glycosidic bonds, thus aiding the germination of barley. In addition, cellulase can also degrade distiller's grains and increase beer filtration efficiency. The cellulase acts directly on the plant cell wall and can increase the reaction speed during vinegar fermentation, and the output of the main product also increases.

Feed industry: Cellulase can be used for saccharification of various cellulosic raw materials. When the amount of cellulase added is 0.1% to 0.3%, it can decompose structurally complex cellulose for the production of protein feed and increase the source of feed. Cellulase can degrade cellulose that is not easily digested in feed into sugar and bacterial protein, which improves the utilization rate and value of feed and utilization. At the same time, it can increase the appetite of animals and promote the growth and development.

Other industries: The proper treatment of pulp with cellulase can increase the production of microfibers and improve the water retention, and may increase the paper's tensile strength. Fabrics with the treatment of cellulase has the characteristics of smoothness, clear pattern, good drape, and strong hygroscopicity.


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