Hyperthermostable Thermotoga maritima xylanase XYN10B shows high activity at high temperatures in the presence of biomass-dissolving hydrophilic ionic liquids

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dc.contributor Aalto-yliopisto fi
dc.contributor Aalto University en
dc.contributor.author Yu, Tianyi
dc.contributor.author Anbarasan, Sasikala
dc.contributor.author Wang, Yawei
dc.contributor.author Telli, Kübra
dc.contributor.author Aslan, Aşkın Sevinç
dc.contributor.author Su, Zhengding
dc.contributor.author Zhou, Yin
dc.contributor.author Zhang, Li
dc.contributor.author Iivonen, Piia
dc.contributor.author Havukainen, Sami
dc.contributor.author Mentunen, Tero
dc.contributor.author Hummel, Michael
dc.contributor.author Sixta, Herbert
dc.contributor.author Binay, Baris
dc.contributor.author Turunen, Ossi
dc.contributor.author Xiong, Hairong
dc.date.accessioned 2016-10-12T11:18:59Z
dc.date.issued 2016-07
dc.identifier.citation Yu , T , Anbarasan , S , Wang , Y , Telli , K , Aslan , A S , Su , Z , Zhou , Y , Zhang , L , Iivonen , P , Havukainen , S , Mentunen , T , Hummel , M , Sixta , H , Binay , B , Turunen , O & Xiong , H 2016 , ' Hyperthermostable Thermotoga maritima xylanase XYN10B shows high activity at high temperatures in the presence of biomass-dissolving hydrophilic ionic liquids ' EXTREMOPHILES , vol 20 , no. 4 , pp. 515–524 . DOI: 10.1007/s00792-016-0841-y en
dc.identifier.issn 1431-0651
dc.identifier.other PURE UUID: fb54891b-a6c3-4be0-82d7-91c26b77eb71
dc.identifier.other PURE ITEMURL: https://research.aalto.fi/en/publications/hyperthermostable-thermotoga-maritima-xylanase-xyn10b-shows-high-activity-at-high-temperatures-in-the-presence-of-biomassdissolving-hydrophilic-ionic-liquids(fb54891b-a6c3-4be0-82d7-91c26b77eb71).html
dc.identifier.other PURE LINK: http://www.scopus.com/inward/record.url?scp=84973149468&partnerID=8YFLogxK
dc.identifier.other PURE FILEURL: https://research.aalto.fi/files/4369417/art_3A10.1007_2Fs00792_016_0841_y.pdf
dc.identifier.uri https://aaltodoc.aalto.fi/handle/123456789/22785
dc.description.abstract The gene of Thermotoga maritima GH10 xylanase (TmXYN10B) was synthesised to study the extreme limits of this hyperthermostable enzyme at high temperatures in the presence of biomass-dissolving hydrophilic ionic liquids (ILs). TmXYN10B expressed from Pichia pastoris showed maximal activity at 100 °C and retained 92 % of maximal activity at 105 °C in a 30-min assay. Although the temperature optimum of activity was lowered by 1-ethyl-3-methylimidazolium acetate ([EMIM]OAc), TmXYN10B retained partial activity in 15–35 % hydrophilic ILs, even at 75–90 °C. TmXYN10B retained over 80 % of its activity at 90 °C in 15 % [EMIM]OAc and 15–25 % 1-ethyl-3-methylimidazolium dimethylphosphate ([EMIM]DMP) during 22-h reactions. [EMIM]OAc may rigidify the enzyme and lower Vmax. However, only minor changes in kinetic parameter Km showed that competitive inhibition by [EMIM]OAc of TmXYN10B is minimal. In conclusion, when extended enzymatic reactions under extreme conditions are required, TmXYN10B shows extraordinary potential. en
dc.format.extent 10
dc.format.extent 515–524
dc.format.mimetype application/pdf
dc.language.iso en en
dc.relation.ispartofseries EXTREMOPHILES en
dc.relation.ispartofseries Volume 20, issue 4 en
dc.rights openAccess en
dc.subject.other Molecular Medicine en
dc.subject.other Microbiology en
dc.subject.other 220 Industrial biotechnology en
dc.subject.other Biochemistry, biophysics en
dc.title Hyperthermostable Thermotoga maritima xylanase XYN10B shows high activity at high temperatures in the presence of biomass-dissolving hydrophilic ionic liquids en
dc.type A1 Alkuperäisartikkeli tieteellisessä aikakauslehdessä fi
dc.description.version Peer reviewed en
dc.contributor.department South-Central University for Nationalities
dc.contributor.department Department of Biotechnology and Chemical Technology
dc.contributor.department Hubei University
dc.contributor.department Wuhan Sunhy Biology Co., Ltd
dc.contributor.department Department of Forest Products Technology
dc.contributor.department Gebze Technical University
dc.contributor.department Department of Bioproducts and Biosystems en
dc.subject.keyword Competitive inhibition
dc.subject.keyword Expression in Pichia pastoris
dc.subject.keyword Extreme stability
dc.subject.keyword GH10 xylanase
dc.subject.keyword Ionic liquids
dc.subject.keyword Thermotoga maritima
dc.subject.keyword Molecular Medicine
dc.subject.keyword Microbiology
dc.subject.keyword 220 Industrial biotechnology
dc.subject.keyword Biochemistry, biophysics
dc.identifier.urn URN:NBN:fi:aalto-201610124824
dc.identifier.doi 10.1007/s00792-016-0841-y
dc.type.version publishedVersion


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