Evidence map›Paper›PMID 27240671›Full record

ArticleExtremophiles : life under extreme conditions2016

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

Tianyi Yu, Sasikala Anbarasan, Yawei Wang, Kübra Telli, Aşkın Sevinç Aslan, Zhengding Su, Yin Zhou, Li Zhang, Piia Iivonen, Sami Havukainen and 6 more

Abstract read
In one paragraph

Article in Extremophiles : life under extreme conditions, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

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Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

10 citing papers in PubMed.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

16 authors.

Tianyi YuSouth-Central University for Nationalities, College of Life Science, Wuhan, 430074, China.
Sasikala AnbarasanDepartment of Biotechnology and Chemical Technology, School of Chemical Technology, Aalto University, 00076, Aalto, Finland.
Yawei WangSouth-Central University for Nationalities, College of Life Science, Wuhan, 430074, China.
Kübra TelliDepartment of Biotechnology and Chemical Technology, School of Chemical Technology, Aalto University, 00076, Aalto, Finland.
Aşkın Sevinç AslanDepartment of Biotechnology and Chemical Technology, School of Chemical Technology, Aalto University, 00076, Aalto, Finland.
Zhengding SuHubei University of Technology, Wuhan, 430068, China.
Yin ZhouWuhan Sunhy Biology Co., Ltd, Wuhan, 430074, China.
Li ZhangSouth-Central University for Nationalities, College of Life Science, Wuhan, 430074, China.
Piia IivonenDepartment of Biotechnology and Chemical Technology, School of Chemical Technology, Aalto University, 00076, Aalto, Finland.
Sami HavukainenDepartment of Biotechnology and Chemical Technology, School of Chemical Technology, Aalto University, 00076, Aalto, Finland.
Tero MentunenDepartment of Biotechnology and Chemical Technology, School of Chemical Technology, Aalto University, 00076, Aalto, Finland.
Michael HummelDepartment of Forest Products Technology, School of Chemical Technology, Aalto University, 00076, Aalto, Finland.
Herbert SixtaDepartment of Forest Products Technology, School of Chemical Technology, Aalto University, 00076, Aalto, Finland.
Baris BinayDepartment of Bioengineering, Gebze Technical University, 41400, Gebze Kocaeli, Turkey.
Ossi TurunenDepartment of Biotechnology and Chemical Technology, School of Chemical Technology, Aalto University, 00076, Aalto, Finland. ossi.turunen@aalto.fi.
Hairong XiongSouth-Central University for Nationalities, College of Life Science, Wuhan, 430074, China. xionghr@mail.scuec.edu.cn.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

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 V max. However, only minor changes in kinetic parameter K m 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.

Indexed as

Hot TemperatureBacterial ProteinsBiomassEndo-1,4-beta XylanasesEnzyme InhibitorsEnzyme StabilityIndustrial MicrobiologyIonic LiquidsPichiaThermotoga maritimaBacterial ProteinsEndo-1,4-beta XylanasesEnzyme InhibitorsIonic LiquidsCompetitive inhibitionExpression in Pichia pastorisExtreme stabilityGH10 xylanaseIonic liquidsThermotoga maritima

Identifiers

PMID27240671
PMCPMC4921120

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.