Biology:Xylanase
Endo-1,4-β-xylanase | |||||||||
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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 | ||||||||
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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
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
- ↑ 1.0 1.1 "Microbial xylanases and their industrial applications: a review". Applied Microbiology and Biotechnology 56 (3–4): 326–338. August 2001. doi:10.1007/s002530100704. PMID 11548999.
- ↑ 2.0 2.1 2.2 "Xylanases from fungi: properties and industrial applications". Applied Microbiology and Biotechnology 67 (5): 577–591. June 2005. doi:10.1007/s00253-005-1904-7. PMID 15944805.
- ↑ Gulzar, Production and partial purification of Xylanase from Trichoderma longibrachiatum. Published in international conference on biotechnology and neurosciences. CUSAT , 2004.P33[verification needed]
- ↑ 4.0 4.1 "Friend or Foe? Impacts of Dietary Xylans, Xylooligosaccharides, and Xylanases on Intestinal Health and Growth Performance of Monogastric Animals". Animals 11 (3): 609. February 2021. doi:10.3390/ani11030609. PMID 33652614.
- ↑ "Biotechnology of microbial xylanases: enzymology, molecular biology, and application". Critical Reviews in Biotechnology 22 (1): 33–64. 2002. doi:10.1080/07388550290789450. PMID 11958335.
- ↑ "Molecular and biotechnological aspects of xylanases". FEMS Microbiology Reviews 23 (4): 411–456. July 1999. doi:10.1111/j.1574-6976.1999.tb00407.x. PMID 10422261.
- ↑ "Molecular cloning of fungal xylanases: an overview". Applied Microbiology and Biotechnology 84 (1): 19–35. August 2009. doi:10.1007/s00253-009-2079-4. PMID 19568746.
- ↑ "A new look at xylanases: an overview of purification strategies". Molecular Biotechnology 24 (3): 257–281. July 2003. doi:10.1385/MB:24:3:257. PMID 12777693.
- ↑ "Screening and production study of microbial xylanase producers from Brazilian Cerrado". Applied Biochemistry and Biotechnology 161 (1–8): 333–346. May 2010. doi:10.1007/s12010-009-8823-5. PMID 19898784.
- ↑ "Xylanases: from biology to biotechnology". Biotechnology & Genetic Engineering Reviews 13: 101–131. 1996. doi:10.1016/S0140-6701(97)80292-5. PMID 8948110.
- ↑ "Xylanolytic enzymes from fungi and bacteria". Critical Reviews in Biotechnology 17 (1): 39–67. 1997. doi:10.3109/07388559709146606. PMID 9118232.
- ↑ "The xylanolytic enzyme system from the genus Penicillium". Journal of Biotechnology 123 (4): 413–433. June 2006. doi:10.1016/j.jbiotec.2005.12.036. PMID 16569456.
- ↑ "Identification of an endo-1,4-beta-xylanase of Ustilago maydis". BMC Biotechnology 13: 59. July 2013. doi:10.1186/1472-6750-13-59. PMID 23889751.
- ↑ "Extracellular Self-Assembly of Functional and Tunable Protein Conjugates from Bacillus subtilis". ACS Synthetic Biology 6 (6): 957–967. June 2017. doi:10.1021/acssynbio.6b00292. PMID 28230977.
- ↑ 15.0 15.1 "- Enzymes". http://www.puratos.us/products_solutions/bakery/enzymes/default.aspx.[full citation needed]
- ↑ "Cloning and characterization of the xyn11A gene from Lentinula edodes". The Protein Journal 24 (1): 21–26. January 2005. doi:10.1007/s10930-004-0602-0. PMID 15756814.
- Marcia Wood (November 29, 2005). "Shiitake Mushrooms' Secret May Benefit Earth-Friendly Fuels". http://www.ars.usda.gov/is/pr/2005/051129.htm.
Further reading
- "Xylanase". Methods in Plant Biochemistry and Molecular Biology. CRC Press. 1997. pp. 313–5. ISBN 0-8493-9480-5. https://books.google.com/books?id=oO9UTAhYDt0C&pg=PA314. "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
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