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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Laccase-derived lignin compounds boost cellulose oxidative enzymes AA9

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Author(s):
Brenelli, Livia [1, 2, 3] ; Squina, Fabio M. [2] ; Felby, Claus [3] ; Cannella, David [1, 3, 4]
Total Authors: 4
Affiliation:
[1] Brazilian Ctr Res Energy & Mat CNPEM, Brazilian Bioethanol Sci & Technol Lab CTBE, Campinas, SP - Brazil
[2] Univ Sorocaba, Programa Proc Tecnol & Ambientais, Sorocaba - Brazil
[3] Univ Copenhagen, Dept Geosci & Nat Resource Management, Fac Sci, Frederiksberg C - Denmark
[4] ULB, Interfac Sch Bioengn, Campus Plaine CP242, Blvd Triomphe, B-1050 Brussels - Belgium
Total Affiliations: 4
Document type: Journal article
Source: BIOTECHNOLOGY FOR BIOFUELS; v. 11, JAN 17 2018.
Web of Science Citations: 25
Abstract

Background: The discovery of lignin as activator for the redox enzyme lytic polysaccharide monooxygenases (LPMOs) for the oxidation of cell-wall polysaccharides opens a new scenario for investigation of the interplay between different lignocellulose-degrading enzymes. The lignin-active enzymes in one hand, and the carbohydrate active in the other, are linked through a variety of electrons carrier molecules either derived from lignin or enzymatically transferred. Likewise, in nature, many lignocellulose-degrading organisms are expressing those enzymes simultaneously, and we wanted to test if a major commercial available lignin oxidase enzyme, i.e., laccase could benefit and synergize the activity of the LPMOs by depolymerizing the insoluble lignin. Results: In this work, two fungal laccases together with a mediator (ABTS) were used to isolate low-molecular-weight lignin from lignocellulosic biomass. The isolated lignins were used as electron donors for activation of LPMOs. A direct correlation between the low-molecular-weight lignin isolated with laccases and an increased activity of a cellulolytic cocktail containing LPMO was found when pure cellulose was hydrolyzed. We then tried to implement existing commercial cellulases cocktail with laccase enzymes, but under the conditions tested, the co-incubation of laccases with LPMOs showed a substrate competition towards oxygen inhibiting the LPMO. In addition, we found that laccase treatment may cause other modifications to pure cellulose, rendering the material more recalcitrant for enzymatic saccharification. Conclusions: Laccase-mediated system was able to depolymerize lignin from pre-treated and native sugarcane bagasse and wheat straw, and the released phenolic molecules were able to donate electrons to LPMO enzymes boosting the overall enzymatic hydrolysis of cellulose. Likewise, other poly-phenol oxidase, we might have just started showing possible pros or cons in applying several oxidase enzymes for a simultaneous degradation of cellulose and lignin, and we found that the competition towards oxygen and their different consumption rates must be taken into account for any possible co-application. (AU)

FAPESP's process: 15/07008-2 - Understanding the complex structure of lignin from sugarcane bagasse and the impact on the antioxidant capacity and its biochemical conversion into value added products
Grantee:Lívia Beatriz Brenelli de Paiva
Support type: Scholarships abroad - Research Internship - Doctorate