Cellulase

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Cellulase
Cellulase 1JS4.jpg
Model of cellulase enzyme, produced by T. fusca, based on PDB structure 1JS4
Identifiers
EC number 3.2.1.4
CAS number 9012-54-8
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / EGO
Ribbon representation of the Streptomyces lividans beta-1,4-endoglucanase catalytic domain - an example from the family 12 glycoside hydrolases[1]

Cellulase (EC 3.2.1.4, endo-1,4-beta-D-glucanase, beta-1,4-glucanase, beta-1,4-endoglucan hydrolase, celluase A, cellulosin AP, endoglucanase D, alkali cellulase, cellulase A 3, celludextrinase, 9.5 cellulase, avicelase, pancellase SS, 1,4-(1,3, 1,4)-beta-D-glucan 4-glucanohydrolase) refers to a suite of enzymes produced chiefly by fungi, bacteria, and protozoans that catalyze cellulolysis (i.e. the hydrolysis of cellulose). However, there are also cellulases produced by a few other types of organisms, such as some termites and the microbial intestinal symbionts of other termites.[2] Several different kinds of cellulases are known, which differ structurally and mechanistically.

Reaction: Hydrolysis of 1,4-beta-D-glycosidic linkages in cellulose, lichenin and cereal beta-D-glucans.

Other names for 'endoglucanases' are: endo-1,4-beta-glucanase, carboxymethyl cellulase (CMCase), endo-1,4-beta-D-glucanase, beta-1,4-glucanase, beta-1,4-endoglucan hydrolase, and celludextrinase. The other types of cellulases are called exocellulases. The expression 'avicelase' refers almost exclusively to exo-cellulase activity as avicel is a highly micro-crystalline substrate. Cellulase action is considered to be synergistic as all three classes of cellulase can yield much more sugar than the addition of all three separately. Beta-glucosidases can also be considered as yet another group of cellulases.

Types and action[edit]

Five general types of cellulases based on the type of reaction catalyzed:

  • Endocellulase (EC 3.2.1.4) randomly cleaves internal bonds at amorphous sites that create new chain ends.
  • Exocellulase (EC 3.2.1.91) cleaves two to four units from the ends of the exposed chains produced by endocellulase, resulting in the tetrasaccharides[3] or disaccharides, such as cellobiose. There are two main types of exocellulases [or cellobiohydrolases (CBH)] - CBHI works processively from the reducing end, and CBHII works processively from the nonreducing end of cellulose.
  • Cellobiase (EC 3.2.1.21) or beta-glucosidase hydrolyses the exocellulase product into individual monosaccharides.
  • Oxidative cellulases depolymerize cellulose by radical reactions, as for instance cellobiose dehydrogenase (acceptor).
  • Cellulose phosphorylases depolymerize cellulose using phosphates instead of water.

In the most familiar case of cellulase activity, the enzyme complex breaks down cellulose to beta-glucose. This type of cellulase is produced mainly by symbiotic bacteria in the ruminating chambers of herbivores. Aside from ruminants, most animals (including humans) do not produce cellulase in their bodies and can only partially break down cellulose through fermentation, limiting their ability to use energy in fibrous plant material. Enzymes that hydrolyze hemicellulose are usually referred to as hemicellulase and are usually classified under cellulase in general. Enzymes that cleave lignin are occasionally classified as cellulase, but this is usually considered erroneous.

Within the above types there are also progressive (also known as processive) and nonprogressive types. Progressive cellulase will continue to interact with a single polysaccharide strand, nonprogressive cellulase will interact once then disengage and engage another polysaccharide strand.

Most fungal cellulases have a two-domain structure, with one catalytic domain and one cellulose binding domain, that are connected by a flexible linker. This structure is adapted for working on an insoluble substrate, and it allows the enzyme to diffuse two-dimensionally on a surface in a caterpillar-like fashion. However, there are also cellulases (mostly endoglucanases) that lack cellulose binding domains. These enzymes might have a swelling function.

In many bacteria, cellulases in-vivo are complex enzyme structures organized in supramolecular complexes, the cellulosomes. They contain roughly five different enzymatic subunits representing namely endocellulases, exocellulases, cellobiases, oxidative cellulases and cellulose phosphorylases wherein only endocellulases and cellobiases participate in the actual hydrolysis of the β(1→ 4) linkage. Recent work on the molecular biology of cellulosomes had led to the discovery of numerous cellulosome-related “signature” sequences known as dockerins and cohesins. Depending on their amino acid sequence and tertiary structures, cellulases are divided into clans and families.[4]

Mechanism of cellulolysis[edit]

The three types of reaction catalyzed by cellulases:1. Breakage of the noncovalent interactions present in the amorphous structure of cellulose (endocellulase) 2. Hydrolysis of chain ends to break the polymer into smaller sugars (exocellulase) 3. Hydrolysis of disaccharides and tetrasaccharides into glucose (beta-glucosidase).
Mechanistic details of beta-glucosidase activity of cellulase

Uses[edit]

Cellulase is used for commercial food processing in coffee. It performs hydrolysis of cellulose during drying of beans. Furthermore, cellulases are widely used in textile industry and in laundry detergents. They have also been used in the pulp and paper industry for various purposes, and they are even used for pharmaceutical applications. Cellulase is used in the fermentation of biomass into biofuels, although this process is relatively experimental at present. Cellulase is used as a treatment for phytobezoars, a form of cellulose bezoar found in the human stomach.

References[edit]

  • Chapin III, F.S., P.A. Matson, H.A. Mooney. Principles of Terrestrial Ecosystem Ecology. Springer-Verlag New York, NY. 2002
  • The Merck Manual of Diagnosis and Therapy, Chapter 24
  • Enhancement of Cellulase Activity from a New Strain of Bacillus subtilis by Medium Optimization and Analysis with Various Cellulosic Substrates, Deepmoni Deka, P. Bhargavi, Ashish Sharma, Dinesh Goyal, M. Jawed, and Arun Goyal. Volume 2011 (2011), Article ID 151656, 8 pages
  1. ^ PDB 1NLR; Sulzenbacher G, Shareck F, Morosoli R, Dupont C, and Davies GJ (1997). "The Streptomyces lividans family 12 endoglucanase: construction of the catalytic cre, expression, and X-ray structure at 1.75 Å resolution". Biochemistry 36: 16032–16039. doi:10.1021/bi972407v. PMID 9440876. ; rendered with PyMOL
  2. ^ A cellulase gene of termite origin. Watanabe H., Hiroaki Noda, Tokuda G., Lo N. 1998 Nature 394, 330-331; Andreas Brune and Moriya Ohkuma, "Role of the termite gut macrobiota in symbiotic digestion", in David Edward Bignell, ed., Biology of Termites: A Modern Synthesis 2010: ch. 16.
  3. ^ Zverlov, V. V., Schantz,N., & Schwarz, W. H. (2005) A major new component in the cellulosome of Clostridium thermocellum is a processive endo-beta-1,4-glucanase producing cellotetraose. FEMS Microbiol. Lett 249, 353-358.
  4. ^ [1] Bayer E.A, Chanzy H., Lamed R., Shoham Y. (1998): Cellulose, Cellulases and Cellulosomes, Curr Opin Struc Biol 8: 548–557

See also[edit]