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Xylanase

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Endo-1,4-β-xylanase
Identifiers
EC no.3.2.1.8
CAS no.9025-57-4
Databases
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BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
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Endo-1,4-β-xylanase (EC 3.2.1.8, systematic name 4-β-D-xylan xylanohydrolase) is any of a class of enzymes that degrade the linear polysaccharide xylan into xylose,[1] thus breaking down hemicellulose, one of the major components of plant cell walls:

Endohydrolysis of (1→4)-β-D-xylosidic linkages in xylans

Xylanase 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;[4] in wheat flour for improving dough handling and quality of baked products [1]; 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. A good quantity 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][5][6][7][8][9][10][11][12][13] High resilience to heating is required for some applications of xylanase, which can be achieved through selection of suitable microbial enzymes[4] or by cyclization of the termini by SpyTag/SpyCatcher reaction.[14]

Additionally, xylanase is the key ingredient in the dough conditioners s500 and us500 manufactured by Puratos [nl].[15] These enzymes are used to improve the dough's workability and absorption of water.[15]

In the future, xylanase may be used for the production of biofuel from unusable plant material.[16]

Synonyms

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Endo-(1→4)-β-xylan 4-xylanohydrolase, endo-1,4-xylanase, endo-1,4-β-xylanase, β-1,4-xylanase, endo-1,4-β-D-xylanase, 1,4-β-xylan xylanohydrolase, β-xylanase, β-1,4-xylan xylanohydrolase, β-D-xylanase

References

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  1. ^ a b 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): 326–338. doi:10.1007/s002530100704. PMID 11548999. S2CID 21581967.
  2. ^ a b c 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): 577–591. doi:10.1007/s00253-005-1904-7. PMID 15944805. S2CID 22956.
  3. ^ Gulzar, Production and partial purification of Xylanase from Trichoderma longibrachiatum. Published in international conference on biotechnology and neurosciences. CUSAT, 2004.P33[verification needed]
  4. ^ a b Baker JT, Duarte ME, Holanda DM, Kim SW (February 2021). "Friend or Foe? Impacts of Dietary Xylans, Xylooligosaccharides, and Xylanases on Intestinal Health and Growth Performance of Monogastric Animals". Animals. 11 (3): 609. doi:10.3390/ani11030609. PMC 7996850. PMID 33652614.
  5. ^ 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. S2CID 13386317.
  6. ^ Kulkarni N, Shendye A, Rao M (July 1999). "Molecular and biotechnological aspects of xylanases". FEMS Microbiology Reviews. 23 (4): 411–456. doi:10.1111/j.1574-6976.1999.tb00407.x. PMID 10422261.
  7. ^ 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. S2CID 8548871.
  8. ^ 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): 257–281. doi:10.1385/MB:24:3:257. PMID 12777693. S2CID 34083448.
  9. ^ 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): 333–346. doi:10.1007/s12010-009-8823-5. PMID 19898784. S2CID 8378197.
  10. ^ Prade RA (1996). "Xylanases: from biology to biotechnology". Biotechnology & Genetic Engineering Reviews. 13: 101–131. doi:10.1016/S0140-6701(97)80292-5. PMID 8948110.
  11. ^ 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.
  12. ^ Chávez R, Bull P, Eyzaguirre J (June 2006). "The xylanolytic enzyme system from the genus Penicillium". Journal of Biotechnology. 123 (4): 413–433. doi:10.1016/j.jbiotec.2005.12.036. hdl:10533/177866. PMID 16569456.
  13. ^ 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.
  14. ^ Gilbert C, Howarth M, Harwood CR, Ellis T (June 2017). "Extracellular Self-Assembly of Functional and Tunable Protein Conjugates from Bacillus subtilis". ACS Synthetic Biology. 6 (6): 957–967. doi:10.1021/acssynbio.6b00292. hdl:10044/1/45032. PMID 28230977.
  15. ^ a b "- Enzymes". Archived from the original on July 19, 2006. Retrieved March 29, 2006.[full citation needed]
  16. ^ Lee CC, Wong DW, Robertson GH (January 2005). "Cloning and characterization of the xyn11A gene from Lentinula edodes". The Protein Journal. 24 (1): 21–26. doi:10.1007/s10930-004-0602-0. PMID 15756814. S2CID 5823517.

Further reading

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