Xylanases from fungi: properties and industrial applications - PubMed (original) (raw)
Review
Xylanases from fungi: properties and industrial applications
M L T M Polizeli et al. Appl Microbiol Biotechnol. 2005 Jun.
Abstract
Xylan is the principal type of hemicellulose. It is a linear polymer of beta-D-xylopyranosyl units linked by (1-4) glycosidic bonds. In nature, the polysaccharide backbone may be added to 4-O-methyl-alpha-D-glucuronopyranosyl units, acetyl groups, alpha-L-arabinofuranosyl, etc., in variable proportions. An enzymatic complex is responsible for the hydrolysis of xylan, but the main enzymes involved are endo-1,4-beta-xylanase and beta-xylosidase. These enzymes are produced by fungi, bacteria, yeast, marine algae, protozoans, snails, crustaceans, insect, seeds, etc., but the principal commercial source is filamentous fungi. Recently, there has been much industrial interest in xylan and its hydrolytic enzymatic complex, as a supplement in animal feed, for the manufacture of bread, food and drinks, textiles, bleaching of cellulose pulp, ethanol and xylitol production. This review describes some properties of xylan and its metabolism, as well as the biochemical properties of xylanases and their commercial applications.
Similar articles
- Properties and applications of microbial beta-D-xylosidases featuring the catalytically efficient enzyme from Selenomonas ruminantium.
Jordan DB, Wagschal K. Jordan DB, et al. Appl Microbiol Biotechnol. 2010 May;86(6):1647-58. doi: 10.1007/s00253-010-2538-y. Epub 2010 Mar 30. Appl Microbiol Biotechnol. 2010. PMID: 20352422 Review. - Screening and production study of microbial xylanase producers from Brazilian Cerrado.
Alves-Prado HF, Pavezzi FC, Leite RS, de Oliveira VM, Sette LD, Dasilva R. Alves-Prado HF, et al. Appl Biochem Biotechnol. 2010 May;161(1-8):333-46. doi: 10.1007/s12010-009-8823-5. Epub 2009 Nov 8. Appl Biochem Biotechnol. 2010. PMID: 19898784 - Xylanolytic enzymes from fungi and bacteria.
Sunna A, Antranikian G. Sunna A, et al. Crit Rev Biotechnol. 1997;17(1):39-67. doi: 10.3109/07388559709146606. Crit Rev Biotechnol. 1997. PMID: 9118232 Review. - Insights into the mechanism of enzymatic hydrolysis of xylan.
Moreira LR, Filho EX. Moreira LR, et al. Appl Microbiol Biotechnol. 2016 Jun;100(12):5205-14. doi: 10.1007/s00253-016-7555-z. Epub 2016 Apr 25. Appl Microbiol Biotechnol. 2016. PMID: 27112349 Review.
Cited by
- Biochemical and biophysical characterization of purified thermophilic xylanase isoforms in Cereus pterogonus plant spp.
Vikramathithan J, Muthuraman P, Ravikumar S, Shayamala S, Kumar GN, Srikumar K. Vikramathithan J, et al. Protein J. 2012 Feb;31(2):141-9. doi: 10.1007/s10930-011-9383-4. Protein J. 2012. PMID: 22231627 - Optimization, purification, and characterization of xylanase production by a newly isolated Trichoderma harzianum strain by a two-step statistical experimental design strategy.
Dhaver P, Pletschke B, Sithole B, Govinden R. Dhaver P, et al. Sci Rep. 2022 Oct 22;12(1):17791. doi: 10.1038/s41598-022-22723-x. Sci Rep. 2022. PMID: 36273028 Free PMC article. - Production of xylanases by mangrove fungi from the Philippines and their application in enzymatic pretreatment of recycled paper pulps.
Torres JM, Dela Cruz TE. Torres JM, et al. World J Microbiol Biotechnol. 2013 Apr;29(4):645-55. doi: 10.1007/s11274-012-1220-1. Epub 2012 Dec 4. World J Microbiol Biotechnol. 2013. PMID: 23208600 - Bagasse minority pathway expression: Real time study of GH2 β-mannosidases from bacteroidetes.
Leonel TF, Pepe ESG, Castellane TCL, Vantini JDS, Funnicelli MIG, Lemos EGM. Leonel TF, et al. PLoS One. 2021 Mar 17;16(3):e0247822. doi: 10.1371/journal.pone.0247822. eCollection 2021. PLoS One. 2021. PMID: 33730062 Free PMC article. - Cell surface xylanases of the glycoside hydrolase family 10 are essential for xylan utilization by Paenibacillus sp. W-61 as generators of xylo-oligosaccharide inducers for the xylanase genes.
Fukuda M, Watanabe S, Yoshida S, Itoh H, Itoh Y, Kamio Y, Kaneko J. Fukuda M, et al. J Bacteriol. 2010 Apr;192(8):2210-9. doi: 10.1128/JB.01406-09. Epub 2010 Feb 12. J Bacteriol. 2010. PMID: 20154127 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Medical