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Specific xylan acti...
Specific xylan activity revealed for AA9 Lytic Polysaccharide Monooxygenases of the thermophilic fungus Malbranchea cinnamomea by functional characterization
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- Hüttner, Silvia, 1984 (författare)
- Chalmers tekniska högskola,Chalmers University of Technology
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- Varnai, Anikó (författare)
- Norges miljø- og biovitenskapelige universitet (NMBU),Norwegian University of Life Sciences (NMBU)
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- Petrović, Dejan (författare)
- Norges miljø- og biovitenskapelige universitet (NMBU),Norwegian University of Life Sciences (NMBU)
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- Xuan Bach, Cao, 1990 (författare)
- Chalmers tekniska högskola,Chalmers University of Technology
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- Dang Thi, Kim Anh, 1990 (författare)
- Chalmers tekniska högskola,Chalmers University of Technology
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Thanh, Vu Nguyen (författare)
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- Eijsink, Vincent G.H. (författare)
- Norges miljø- og biovitenskapelige universitet (NMBU),Norwegian University of Life Sciences (NMBU)
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- Larsbrink, Johan, 1982 (författare)
- Chalmers tekniska högskola,Chalmers University of Technology
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- Olsson, Lisbeth, 1963 (författare)
- Chalmers tekniska högskola,Chalmers University of Technology
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(creator_code:org_t)
- 2019
- 2019
- Engelska.
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Ingår i: Applied and Environmental Microbiology. - 1098-5336 .- 0099-2240. ; 85:23
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Abstract
Ämnesord
Stäng
- The thermophilic biomass-degrader Malbranchea cinnamomea exhibits poor growth on cellulose but excellent growth on hemicelluloses as the sole carbon source. This is surprising considering that its genome encodes eight lytic polysaccharide monooxygenases (LPMOs) from auxiliary activity family 9 (AA9), enzymes known for their high potential in accelerating cellulose depolymerization. We characterized four of the eight ( M. cinnamomea AA9s) Mc AA9s, namely, Mc AA9A, Mc AA9B, Mc AA9F, and Mc AA9H, to gain a deeper understanding about their roles in the fungus. The characterized Mc AA9s were active on hemicelluloses, including xylan, glucomannan, and xyloglucan, and furthermore, in accordance with transcriptomics data, differed in substrate specificity. Of the Mc AA9s, Mc AA9H is unique, as it preferentially cleaves residual xylan in phosphoric acid-swollen cellulose (PASC). Moreover, when exposed to cellulose-xylan blends, Mc AA9H shows a preference for xylan and for releasing (oxidized) xylooligosaccharides. The cellulose dependence of the xylan activity suggests that a flat conformation, with rigidity similar to that of cellulose microfibrils, is a prerequisite for productive interaction between xylan and the catalytic surface of the LPMO. Mc AA9H showed a similar trend on xyloglucan, underpinning the suggestion that LPMO activity on hemicelluloses strongly depends on the polymers’ physicochemical context and conformation. Our results support the notion that LPMO multiplicity in fungal genomes relates to the large variety of copolymeric polysaccharide arrangements occurring in the plant cell wall.
Ämnesord
- TEKNIK OCH TEKNOLOGIER -- Industriell bioteknik (hsv//swe)
- ENGINEERING AND TECHNOLOGY -- Industrial Biotechnology (hsv//eng)
- NATURVETENSKAP -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
- NATURVETENSKAP -- Biologi -- Mikrobiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Microbiology (hsv//eng)
Nyckelord
- hemicellulose
- biomass degradation
- thermophilic
- monooxygenases
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Hüttner, Silvia, ...
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Varnai, Anikó
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Petrović, Dejan
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Xuan Bach, Cao, ...
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Dang Thi, Kim An ...
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Thanh, Vu Nguyen
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visa fler...
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Eijsink, Vincent ...
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Larsbrink, Johan ...
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Olsson, Lisbeth, ...
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