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Thermal behaviour and tolerance to ionic liquid [emim] OAc in GH10 xylanase from Thermoascus aurantiacus SL16W
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- Chawachart, Niwat (författare)
- Department of Biology, Faculty of Science, Chiang Mai University, Chiang Mai, 50200, Thailand
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- Anbarasan, Sasikala (författare)
- Department of Biotechnology and Chemical Technology, School of Chemical Technology, Aalto University, P.O. Box 16100, 00076, Aalto, Finland
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- Turunen, Samuel (författare)
- Department of Biotechnology and Chemical Technology, School of Chemical Technology, Aalto University, P.O. Box 16100, 00076, Aalto, Finland
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- Department of Biology, Faculty of Science, Chiang Mai University, Chiang Mai, 50200, Thailand Department of Biotechnology and Chemical Technology, School of Chemical Technology, Aalto University, PO. Box 16100, 00076, Aalto, Finland (creator_code:org_t)
- 2014-07-30
- 2014
- Engelska.
- Ingår i: Extremophiles. - : Springer Japan. - 1431-0651 .- 1433-4909. ; 18:6, s. 1023-1034
- Tidskriftsartikel (refereegranskat)
Abstract
Ämnesord
Stäng
- GH10 xylanase from Thermoascus aurantiacus strain SL16W (TasXyn10A) showed high stability and activity up to 70–75 C. The enzyme’s half-lives were 101 h, 65 h, 63 min and 6 min at 60, 70, 75 and 80 C, respectively. The melting point (Tm), as measured by DSC, was 78.5 C, which is in line with a strong activity decrease at 75–80 C. The biomass-dissolving ionic liquid 1-ethyl-3-methylimidazolium acetate ([emim]OAc) in 30 % concentration had a small effect on the stability of TasXyn10A; Tm decreased by only 5 C. It was also observed that [emim]OAc inhibited much less GH10 xylanase (TasXyn10A) than the studied GH11 xylanases. The Km of TasXyn10A increased 3.5-fold in 15 % [emim]OAc with xylan as the substrate, whereas the approximate level of Vmax was not altered. The inhibition of enzyme activity by [emim]OAc was lesser at higher substrate concentrations. Therefore, high solid concentrations in industrial conditions may mitigate the inhibition of enzyme activity by ionic liquids. Molecular docking experiments indicated that the [emim] cation has major binding sites near the catalytic residues but in lower amounts in GH10 than in GH11 xylanases. Therefore, [emim] cation likely competes with the substrate when binding to the active site. The docking results indicated why the effect is lower in GH10.
Ämnesord
- TEKNIK OCH TEKNOLOGIER -- Industriell bioteknik -- Biokatalys och enzymteknik (hsv//swe)
- ENGINEERING AND TECHNOLOGY -- Industrial Biotechnology -- Biocatalysis and Enzyme Technology (hsv//eng)
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