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Side-by-side biochemical comparison of two lytic polysaccharide monooxygenases from the white-rot fungus Heterobasidion irregulare on their activity against crystalline cellulose and glucomannan
Department of Molecular Sciences, Swedish University of Agricultural Sciences, Uppsala.
Department of Molecular Sciences, Swedish University of Agricultural Sciences, Uppsala.
Luleå University of Technology, Department of Civil, Environmental and Natural Resources Engineering, Chemical Engineering.ORCID iD: 0000-0003-1336-2396
Department of Forest Mycology and Plant Pathology, Swedish University of Agricultural Sciences, Uppsala.
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2018 (English)In: PLOS ONE, E-ISSN 1932-6203, Vol. 13, no 9, article id e0203430Article in journal (Refereed) Published
Abstract [en]

Our comparative studies reveal that the two lytic polysaccharide monooxygenases HiLP-MO9B and HiLPMO9I from the white-rot conifer pathogen Heterobasidion irregulare display clear difference with respect to their activity against crystalline cellulose and glucomannan. HiLPMO9I produced very little soluble sugar on bacterial microcrystalline cellulose (BMCC). In contrast, HiLPMO9B was much more active against BMCC and even released more soluble sugar than the H. irregulare cellobiohydrolase I, HiCel7A. Furthermore, HiLPMO9B was shown to cooperate with and stimulate the activity of HiCel7A, both when the BMCC was first pretreated with HiLPMO9B, as well as when HiLPMO9B and HiCel7A were added together. No such stimulation was shown by HiLPMO9I. On the other hand, HiLPMO9I was shown to degrade glucomannan, using a C4-oxidizing mechanism, whereas no oxidative cleavage activity of glucomannan was detected for HiLPMO9B. Structural modeling and comparison with other glucomannan-active LPMOs suggest that conserved sugar-interacting residues on the L2, L3 and LC loops may be essential for glucomannan binding, where 4 out of 7 residues are shared by HiLPMO9I, but only one is found in HiLPMO9B. The difference shown between these two H. irregulare LPMOs may reflect distinct biological roles of these enzymes within deconstruction of different plant cell wall polysaccharides during fungal colonization of softwood.

Place, publisher, year, edition, pages
Public Library of Science , 2018. Vol. 13, no 9, article id e0203430
National Category
Bioprocess Technology
Research subject
Biochemical Process Engineering
Identifiers
URN: urn:nbn:se:ltu:diva-70871DOI: 10.1371/journal.pone.0203430ISI: 000443789900061PubMedID: 30183773Scopus ID: 2-s2.0-85052855182OAI: oai:DiVA.org:ltu-70871DiVA, id: diva2:1248588
Note

Validerad;2018;Nivå 2;2018-09-17 (svasva)

Available from: 2018-09-17 Created: 2018-09-17 Last updated: 2023-09-05Bibliographically approved
In thesis
1. Lytic Polysaccharide MonoOxygenases; their role for lignocellulose depolymerization and production of (functional) biobased compounds
Open this publication in new window or tab >>Lytic Polysaccharide MonoOxygenases; their role for lignocellulose depolymerization and production of (functional) biobased compounds
2021 (English)Doctoral thesis, comprehensive summary (Other academic)
Abstract [en]

Increased environmental concerns over petroleum-based products triggered the quest to find a sustainable alternative for fuels, chemicals etc. Lignocellulose biomass, due to its abundance, is considered as one of the most promising sustainable sources for the production of fuels and chemicals, while replacing the traditional petroleum resources. In a biorefinery, by choosing a greener biochemical conversion process with cellulolytic enzymes, cellulose from biomass is depolymerized into monomeric sugars and residual fibers; which can be later converted into a spectra of value added products.

Lytic polysaccharide monooxygenases (LPMOs) are one of the essential groups of enzymes in the bioconversion of lignocellulose. They are copper active enzymes that are produced by different polysaccharide degrading organisms in nature, such as lignocellulolytic fungi. In lignocellulose degradation, they are different from the traditional hydrolytic cellulolytic enzymes with their unique way of oxidative breakage of cellulose, in the presence of a co-substrate such as oxygen, and a reducing agent like lignin in the biomass. Their ability to enhance the action of traditional cellulases in cellulose depolymerization make them an integral part of today’s commercial cellulosic cocktails.

Primary goals of biorefinery research include efficient liquefaction of lignocellulose in order to increase the release of monomeric sugars towards the production of various chemicals and fuels, together with the potential use of residual fibers for the production of value-added products; all by minimizing the release of undesired by-products and the environmental impact of the process. LPMOs, along with other cellulases, have been shown to be very much beneficial in this.

This thesis comprises the study of LPMOs from different fungal origin, in their depolymerization ability on various substrates, including both model substrates and natural biomass samples. The evaluation was done based on their ability to release neutral and oxidized sugars, as well as their capability to promote liquefaction. Effect of various pretreatment methods of lignocellulose on the action of LPMOs was studied, together with their capability to use lignin present in the wood as a reducing agent, which gives a better understanding about their function in nature. Lastly, their role in producing value added materials such as nanocellulose, the prebiotic disaccharide cellobiose, from lignocellulose was also evaluated. 

Place, publisher, year, edition, pages
Luleå University of Technology, 2021
Series
Doctoral thesis / Luleå University of Technology 1 jan 1997 → …, ISSN 1402-1544
National Category
Industrial Biotechnology Bioprocess Technology
Research subject
Biochemical Process Engineering
Identifiers
urn:nbn:se:ltu:diva-82232 (URN)978-91-7790-745-9 (ISBN)978-91-7790-746-6 (ISBN)
Public defence
2021-02-12, A109, 10:00 (English)
Opponent
Supervisors
Funder
Swedish Energy Agency
Available from: 2021-01-11 Created: 2021-01-10 Last updated: 2023-09-05Bibliographically approved

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Muraleedharan, Madhu Nair

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