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endo-1,4-β-xylanase |
Identifiers |
EC number |
3.2.1.8 |
CAS number |
9025-57-4 |
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 |
Search |
PMC |
articles |
PubMed |
articles |
NCBI |
proteins |
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Xylanase (EC 3.2.1.8, endo-(1->4)-beta-xylan 4-xylanohydrolase, endo-1,4-xylanase, endo-1,4-beta-xylanase, beta-1,4-xylanase, endo-1,4-beta-D-xylanase, 1,4-beta-xylan xylanohydrolase, beta-xylanase, beta-1,4-xylan xylanohydrolase, beta-D-xylanase) is the name given to a class of enzymes which degrade the linear polysaccharide beta-1,4-xylan into xylose[1], thus breaking down hemicellulose, one of the major components of plant cell walls.
As such, it plays a major role in micro-organisms thriving on plant sources (mammals, conversely, do not produce xylanase). Additionally, xylanases are present in fungi such as from the GRAS recognized fungus C1, Myceliophthora thermophila [2]for the degradation of plant matter into usable nutrients.
Commercial applications for xylanase include the chlorine-free bleaching of wood pulp prior to the papermaking process, and the increased digestibility of silage (in this aspect, it is also used for fermentative composting).[1]
Apart from its use in the pulp and paper industry, xylanases from commercially relevant fungi such as Myceliophthora thermophila, C1 and Trichoderma are also used as food additives to poultry, in wheat flour for improving dough handling and quality of baked products [3], for the extraction of coffee, plant oils, and starch, in the improvement of nutritional properties of agricultural silage and grain feed, and in combination with pectinase and cellulase for clarification of fruit juices and degumming of plant fiber sources such as flax, hemp, jute, and ramie. Good number of scientific literature is available on key features of xylanase enzymes in biotechnology ranging from their screening in microbial sources to production methods, characterization, purification and applications in commercial sector.[2][3][4][5][6][7][8][9][10][11][improper synthesis?]
Additionally, it is the key ingredient in the dough conditioners s500 and us500 manufactured by Puratos.[12] These enzymes are used to improve the dough's workability and absorption of water.[12]
In the future, xylanase may be used for the production of biofuel from unusable plant material.[13]
References[edit source | edit]
- ^ Gulzar, Production and partial purification of Xylanase from Trichoderma longibrachiatum. Published in international conference on biotechnology and neurosciences. CUSAT , 2004.P33[verification needed]
- ^ Beg, Q. K.; Kapoor, M.; Mahajan, L.; Hoondal, G. S. (2001). "Microbial xylanases and their industrial applications: A review". Applied Microbiology and Biotechnology 56 (3–4): 326–38. doi:10.1007/s002530100704. PMID 11548999.
- ^ Polizeli, M. L. T. M.; Rizzatti, A. C. S.; Monti, R.; Terenzi, H. F.; Jorge, J. A.; Amorim, D. S. (2005). "Xylanases from fungi: Properties and industrial applications". Applied Microbiology and Biotechnology 67 (5): 577–91. doi:10.1007/s00253-005-1904-7. PMID 15944805.
- ^ Subramaniyan, S.; Prema, P. (2002). "Biotechnology of Microbial Xylanases: Enzymology, Molecular Biology, and Application". Critical Reviews in Biotechnology 22 (1): 33–64. doi:10.1080/07388550290789450. PMID 11958335.
- ^ Kulkarni, Neeta; Shendye, Abhay; Rao, Mala (1999). "Molecular and biotechnological aspects of xylanases". FEMS Microbiology Reviews 23 (4): 411–56. doi:10.1111/j.1574-6976.1999.tb00407.x. PMID 10422261.
- ^ Ahmed, Sibtain; Riaz, Saba; Jamil, Amer (2009). "Molecular cloning of fungal xylanases: An overview". Applied Microbiology and Biotechnology 84 (1): 19–35. doi:10.1007/s00253-009-2079-4. PMID 19568746.
- ^ Sá-Pereira, Paula; Paveia, Helena; Costa-Ferreira, Maria; Aires-Barros, Maria Raquel (2003). "A New Look at Xylanases: An Overview of Purification Strategies". Molecular Biotechnology 24 (3): 257–81. doi:10.1385/MB:24:3:257. PMID 12777693.
- ^ Alves-Prado, Heloiza Ferreira; Pavezzi, Fabiana Carina; Leite, Rodrigo Simões Ribeiro; Oliveira, Valéria Maia; Sette, Lara Durães; Dasilva, Roberto (2009). "Screening and Production Study of Microbial Xylanase Producers from Brazilian Cerrado". Applied Biochemistry and Biotechnology 161 (1–8): 333–46. doi:10.1007/s12010-009-8823-5. PMID 19898784.
- ^ Prade, R. A. (1996). "Xylanases: From biology to biotechnology". Biotechnology & Genetic Engineering Reviews 13: 101–31. doi:10.1016/S0140-6701(97)80292-5. PMID 8948110.
- ^ Sunna, A.; Antranikian, G. (1997). "Xylanolytic Enzymes from Fungi and Bacteria". Critical Reviews in Biotechnology 17 (1): 39–67. doi:10.3109/07388559709146606. PMID 9118232.
- ^ Chávez, Renato; Bull, Paulina; Eyzaguirre, Jaime (2006). "The xylanolytic enzyme system from the genus Penicillium". Journal of Biotechnology 123 (4): 413–33. doi:10.1016/j.jbiotec.2005.12.036. PMID 16569456.
- ^ a b http://www.puratos.us/products_solutions/bakery/enzymes/default.aspx[full citation needed]
- ^ Lee, Charles C.; Wong, Dominic W. S.; Robertson, George H. (2005). "Cloning and Characterization of the Xyn11A Gene from Lentinula edodes". The Protein Journal 24 (1): 21–6. doi:10.1007/s10930-004-0602-0. PMID 15756814. Lay summary – Agricultural Research Service (November 29, 2005).
[4] [5] [6] [7] [8] [9]
Further reading[edit source | edit]
- Dashek, William V (1997). "Xylanase". Methods in Plant Biochemistry and Molecular Biology. CRC Press. pp. 313–5. ISBN 0-8493-9480-5. "Xylans can by hydrolyzed by β-xylanase"
- Risk Assessment Summary, CEPA 1999. Trichoderma reesei 1391A
- Risk Assessment Summary, CEPA 1999. Trichoderma reesei P345A
- Risk Assessment Summary, CEPA 1999. Trichoderma reesei P210A
- Risk Assessment Summary, CEPA 1999. Trichoderma longibrachiatum RM4-100