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Cellulase


Official Full Name
Cellulase
Background
Cellulase is any of several enzymes produced chiefly by fungi, bacteria, and protozoans that catalyze cellulolysis, the decomposition of cellulose and of some related polysaccharides. The name is also used for any naturally occurring mixture or complex of various such enzymes, that act serially or synergistically to decompose cellulosic material. Cellulases break down the cellulose molecule into monosaccharides ("simple sugars") such as beta-glucose, or shorter polysaccharides and oligosaccharides. Cellulose breakdown is of considerable economic importance, because it makes a major constituent of plants available for consumption and use in chemical reactions. The specific reaction involved is the hydrolysis of the 1,4-beta-D-glycosidic linkages in cellulose, hemicellulose, lichenin, and cereal beta-D-glucans. Because cellulose molecules bind strongly to each other, cellulolysis is relatively difficult compared to the breakdown of other polysaccharides such as starch.
Synonyms
Cellulase# thermostable; 1#4-(1#3:1#4)-β-D-Glucan 4-glucano-hydrolase; EC 3.2.1.4; Cellulase; 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
Product Name
EC No.
CAS No.
Source
Price
CatalogNATE-1928
EC No.EC 3.2.1.4
CAS No.9012-54-8
SourceE. coli
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-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-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 (β-1,4-glucan-4-glucanohydrolase) is a general term for a group of enzymes that degrade cellulose to produce glucose. It is not a single enzyme, but a multi-component that acts synergistically enzyme system is a composite enzyme, mainly composed of exo-β-glucanase, endo-β-glucanase and β-glucosidase, as well as high-activity xylanase. Acts on cellulose and products derived from cellulose. Microbial cellulase is of great significance in converting insoluble cellulose into glucose and destroying cell walls in fruit and vegetable juice to improve the yield of juice.

Classifications

Structure

Most fungal cellulases have a two-domain structure, in which a catalytic domain and a cellulose binding domain are connected by a flexible linker. This structure is suitable for working on insoluble substrates and allows enzymes to spread two-dimensionally on the surface in a manner similar to caterpillars. However, there are also cellulases (mainly endoglucanases) that lack a cellulose binding domain. Both substrate binding and catalysis depend on the three-dimensional structure of the enzyme, which is the result of the level of protein folding. The amino acid sequence occurring in the active site and the arrangement of its residues (the position where the substrate binds) may affect various factors, such as the binding affinity of the ligand, the stabilization and catalysis of the substrate in the active site. The structure of the substrate is complementary to the precise active site structure of the enzyme. Changes in residue positions may cause distortions in one or more of these interactions.

Protein structure of cellulase. Figure 1. Protein structure of cellulase.

Factors affecting the action of cellulase

The optimum pH of cellulase is generally 4.5 to 6.5. Gluconolactone can effectively inhibit cellulase. Heavy metal ions such as copper and mercury ions can also inhibit cellulase, but cysteine can eliminate their inhibitory effect and even further activate cellulase. Plant tissues contain natural cellulase inhibitors; it can protect plants from the rot of molds. These inhibitors are phenolic compounds. If there is high oxidase activity in plant tissues, then it can oxidize phenolic compounds into quinone compounds, which can inhibit cellulase.

Agricultural applications

Common livestock and poultry feeds such as grains, beans, wheat and processing by-products contain a lot of cellulose. In addition to ruminant animals that can use some of the rumen microbes, other animals such as pigs, chickens and other monogastric animals cannot use cellulose.

References

  1. Guerriero G.; et al. Novel insights from comparative in silico analysis of green microalgae cellulases. Int. J. Mol. Sci. 2018, 19 (6), 1782.
  2. Liu Y.; et al. Crystal structure of a glycoside hydrolase family 6 enzyme, CcCel6C, a cellulase constitutively produced by Coprinopsis cinerea. The FEBS Journal.2010, 277 (6): 1532–42. 

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