キシラナーゼ、キシラン分解酵素
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出典(authority):フリー百科事典『ウィキペディア(Wikipedia)』「2013/03/05 20:14:51」(JST)
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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 |
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proteins |
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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 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 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.[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
- ^ Gulzar, Production and partial purification of Xylanase fromTrichoderma 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).
Further reading
- Dashek, William V (1997). "Xylanase". Methods in Plant Biochemistry and Molecular Biology. CRC Press. pp. 313–5. ISBN 0-8493-9480-5. http://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
English Journal
- Bleach boosting effect of xylanase A from Bacillus halodurans C-125 in ECF bleaching of wheat straw pulp.
- Lin XQ, Han SY, Zhang N, Hu H, Zheng SP, Ye YR, Lin Y.SourceGuangdong Key Laboratory of Fermentation and Enzyme Engineering, School of Bioscience and Bioengineering, South China University of Technology, Guangzhou 510006, PR China.
- Enzyme and microbial technology.Enzyme Microb Technol.2013 Feb 5;52(2):91-8. doi: 10.1016/j.enzmictec.2012.10.011. Epub 2012 Nov 9.
- Past studies have revealed major difficulties in applications of xylanase in the pulp and paper industry as enzymes isolated from many different species could not tolerate high temperatures or highly alkaline conditions. The thermostable xylanase A from Bacillus halodurans C-125 (C-125 xylanase A) w
- PMID 23273277
- Characterization of a novel xylanase from Armillaria gemina and its immobilization onto SiO(2) nanoparticles.
- Dhiman SS, Kalyani D, Jagtap SS, Haw JR, Kang YC, Lee JK.SourceDepartment of Chemical Engineering, Konkuk University, 1 Hwayang-Dong, Gwangjin-Gu, Seoul, 143-701, Republic of Korea.
- Applied microbiology and biotechnology.Appl Microbiol Biotechnol.2013 Feb;97(3):1081-91. doi: 10.1007/s00253-012-4381-9. Epub 2012 Sep 7.
- Enhanced catalytic activities of different lignocellulases were obtained from Armillaria gemina under statistically optimized parameters using a jar fermenter. This strain showed maximum xylanase, endoglucanase, cellobiohydrolase, and β-glucosidase activities of 1,270, 146, 34, and 15 U mL(-1), res
- PMID 22955325
- Characterisation of two bifunctional cellulase-xylanase enzymes isolated from a bovine rumen metagenome library.
- Rashamuse KJ, Visser DF, Hennessy F, Kemp J, Roux-van der Merwe MP, Badenhorst J, Ronneburg T, Francis-Pope R, Brady D.SourceCSIR Biosciences, PO Box 395, Pretoria, South Africa.
- Current microbiology.Curr Microbiol.2013 Feb;66(2):145-51. doi: 10.1007/s00284-012-0251-z. Epub 2012 Oct 20.
- Ruminant digestive tract microbes hydrolyse plant biomass, and the application of metagenomic techniques can provide good coverage of their glycosyl hydrolase enzymes. A metagenomic library of circa 70,000 fosmids was constructed from bacterial DNA isolated from bovine rumen and subsequently screene
- PMID 23086538
Japanese Journal
- Purification and characterization of alkaline xylanase from Thermoascus aurantiacus var. levisporus KKU-PN-I2-1 cultivated by solid-state fermentation
- Chanwicha Nantawan,Katekaew Somporn,Aimi Tadanori [他]
- Mycoscience : official journal of the Mycological Society of Japan 56(3), 309-318, 2015-05
- NAID 40020464385
- Putative endoglucanase PcGH5 from Phanerochaete chrysosporium is a β-xylosidase that cleaves xylans in synergistic action with endo-xylanase
- Huy Nguyen Due,Nguyen Cu Le,Seo Jeong-Woo [他]
- Journal of bioscience and bioengineering 119(4), 416-420, 2015-04
- NAID 40020435218
- 米飯の食味形成に関与する米胚乳酵素の活性量の品種および栽培地域による変動の解析
- 辻井 良政,高野 克己
- 日本食品科学工学会誌 62(1), 34-40, 2015
- … 域等により活性量が変化すると考えられる.我々は,米胚乳酵素活性量の様相と米の品種などとの関係を検討した.酵素活性の測定は,αおよびβ-amylase,α-glucosidase,β-glucanase,β-galactosidase,α-mannosidase,β-xylanase活性量を敏速に測定できる合成基質を用いて,高感度に定量した.得られた活性量を変数としてケモメトリックス解析を行った.<BR>その結果,米胚乳酵素活性はコシヒカリ近縁種間で差異があった.α …
- NAID 130004779808
Related Links
- Xylanase is the name given to a class of enzymes which degrade the linear polysaccharide beta-1,4-xylan into xylose, thus breaking down hemicellulose, one of the major components of plant cell walls. As such, it plays a major role in ...
- 9 Sep 2011 ... Xylanase is a naturally-occurring enzyme that plays an important role in digestion . Learn more about the health benefits of Xylanase, and how it can help you.
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