Xylanase

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 / QuickGO

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 for the degradation of plant matter into usable nutrients. Xylanases are produced by fungi, bacteria, yeast, marine algae, protozoans, snails, crustaceans, insect, seeds, etc.,[2] (mammals do not produce xylanases). However, the principal commercial source of xylanases is filamentous fungi.[2]

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).[3]

Apart from its use in the pulp and paper industry, xylanases are also used as food additives to poultry, in wheat flour for improving dough handling and quality of baked products , 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.[1][2][4][5][6][7][8][9][10][11][12]

Additionally, it is the key ingredient in the dough conditioners s500 and us500 manufactured by Puratos.[13] These enzymes are used to improve the dough's workability and absorption of water.[13]

In the future, xylanase may be used for the production of biofuel from unusable plant material.[14]

References

  1. 1 2 Beg QK, Kapoor M, Mahajan L, Hoondal GS (August 2001). "Microbial xylanases and their industrial applications: a review". Applied Microbiology and Biotechnology. 56 (3–4): 326–38. doi:10.1007/s002530100704. PMID 11548999.
  2. 1 2 3 Polizeli ML, Rizzatti AC, Monti R, Terenzi HF, Jorge JA, Amorim DS (June 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.
  3. ↑ Gulzar, Production and partial purification of Xylanase from Trichoderma longibrachiatum. Published in international conference on biotechnology and neurosciences. CUSAT , 2004.P33
  4. ↑ 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.
  5. ↑ Kulkarni N, Shendye A, Rao M (July 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.
  6. ↑ Ahmed S, Riaz S, Jamil A (August 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.
  7. ↑ Sá-Pereira P, Paveia H, Costa-Ferreira M, Aires-Barros M (July 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.
  8. ↑ Alves-Prado HF, Pavezzi FC, Leite RS, de Oliveira VM, Sette LD, Dasilva R (May 2010). "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.
  9. ↑ Prade RA (1996). "Xylanases: from biology to biotechnology". Biotechnology & Genetic Engineering Reviews. 13: 101–31. doi:10.1016/S0140-6701(97)80292-5. PMID 8948110.
  10. ↑ 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.
  11. ↑ Chávez R, Bull P, Eyzaguirre J (June 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.
  12. ↑ Geiser E, Wierckx N, Zimmermann M, Blank LM (July 2013). "Identification of an endo-1,4-beta-xylanase of Ustilago maydis". BMC Biotechnology. 13: 59. doi:10.1186/1472-6750-13-59. PMC 3737115. PMID 23889751.
  13. 1 2 "Archived copy". Archived from the original on July 19, 2006. Retrieved March 29, 2006.
  14. ↑ Lee CC, Wong DW, Robertson GH (January 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).

Further reading

  • Dashek WV (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
This article is issued from Wikipedia. The text is licensed under Creative Commons - Attribution - Sharealike. Additional terms may apply for the media files.