Engineering of Xylanases for the Development of Biotechnologically Important Characteristics

dc.contributor.author Sürmeli, Yusuf
dc.contributor.author Şanlı Mohamed, Gülşah
dc.date.accessioned 2023-03-17T08:28:02Z
dc.date.available 2023-03-17T08:28:02Z
dc.date.issued 2023
dc.description.abstract Xylanases are the main biocatalysts used for the reduction of the xylan backbone from hemicellulose, randomly splitting off β-1,4-glycosidic linkages between xylopyranosyl residues. Xylanase market has been annually estimated at 500 million US Dollars and they are potentially used in broad industrial process ranges such as paper pulp biobleaching, xylo-oligosaccharide production, and biofuel manufacture from lignocellulose. The highly stable xylanases are preferred in the downstream procedure of industrial processes because they can tolerate severe conditions. Almost all native xylanases can not endure adverse conditions thus they are industrially not proper to be utilized. Protein engineering is a powerful technology for developing xylanases, which can effectively work in adverse conditions and can meet requirements for industrial processes. This study considered state-of-the-art strategies of protein engineering for creating the xylanase gene diversity, high-throughput screening systems toward upgraded traits of the xylanases, and the prediction and comprehensive analysis of the target mutations in xylanases by in silico methods. Also, key molecular factors have been elucidated for industrial characteristics (alkaliphilic enhancement, thermal stability, and catalytic performance) of GH11 family xylanases. The present review explores industrial characteristics improved by directed evolution, rational design, and semi-rational design as protein engineering approaches for pulp bleaching process, xylooligosaccharides production, and biorefinery & bioenergy production. en_US
dc.identifier.doi 10.1002/bit.28339
dc.identifier.issn 0006-3592 en_US
dc.identifier.issn 0006-3592
dc.identifier.issn 1097-0290
dc.identifier.scopus 2-s2.0-85147493474
dc.identifier.uri https://doi.org/10.1002/bit.28339
dc.identifier.uri https://hdl.handle.net/11147/13242
dc.language.iso en en_US
dc.publisher Wiley en_US
dc.relation.ispartof Biotechnology and Bioengineering en_US
dc.rights info:eu-repo/semantics/embargoedAccess en_US
dc.subject Engineering xylanase en_US
dc.subject Biorefinery en_US
dc.subject Industrial characteristics en_US
dc.subject Pulp bleaching en_US
dc.subject XOs production en_US
dc.title Engineering of Xylanases for the Development of Biotechnologically Important Characteristics en_US
dc.type Article en_US
dspace.entity.type Publication
gdc.author.id 0000-0003-0282-4428
gdc.author.id 0000-0003-0282-4428 en_US
gdc.author.institutional Şanlı Mohamed, Gülşah
gdc.bip.impulseclass C4
gdc.bip.influenceclass C5
gdc.bip.popularityclass C4
gdc.coar.access embargoed access
gdc.coar.type text::journal::journal article
gdc.collaboration.industrial false
gdc.contributor.affiliation Namık Kemal Üniversitesi en_US
gdc.contributor.affiliation 01. Izmir Institute of Technology en_US
gdc.description.department İzmir Institute of Technology. Chemistry en_US
gdc.description.endpage 1188
gdc.description.publicationcategory Makale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanı en_US
gdc.description.scopusquality Q2
gdc.description.startpage 1171
gdc.description.volume 120
gdc.description.wosquality Q2
gdc.identifier.openalex W4318542985
gdc.identifier.pmid 36715367
gdc.identifier.wos WOS:000928493700001
gdc.index.type WoS
gdc.index.type Scopus
gdc.index.type PubMed
gdc.oaire.diamondjournal false
gdc.oaire.impulse 16.0
gdc.oaire.influence 3.0189684E-9
gdc.oaire.isgreen false
gdc.oaire.keywords Endo-1,4-beta Xylanases
gdc.oaire.keywords Protein Engineering
gdc.oaire.popularity 1.1837191E-8
gdc.oaire.publicfunded false
gdc.oaire.sciencefields 0301 basic medicine
gdc.oaire.sciencefields 0303 health sciences
gdc.oaire.sciencefields 03 medical and health sciences
gdc.openalex.collaboration National
gdc.openalex.fwci 3.65419514
gdc.openalex.normalizedpercentile 0.9
gdc.openalex.toppercent TOP 10%
gdc.opencitations.count 14
gdc.plumx.crossrefcites 17
gdc.plumx.mendeley 22
gdc.plumx.pubmedcites 6
gdc.plumx.scopuscites 23
gdc.scopus.citedcount 23
gdc.wos.citedcount 21
relation.isAuthorOfPublication.latestForDiscovery eae23f7d-4b68-4072-9e21-c5a4a8c41aa3
relation.isOrgUnitOfPublication.latestForDiscovery 9af2b05f-28ac-4011-8abe-a4dfe192da5e

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