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The laccase-catalyzed modification of lignin for enzymatic hydrolysis
Institution:1. Bioenvironmental Engineering Research Centre (BERC), Department of Biotechnology Engineering, Faculty of Engineering, International Islamic University Malaysia, Jalan Gombak, 50728 Kuala Lumpur, Malaysia;2. International Institute for Halal Research and Training (INHART), IIUM, Malaysia;1. Department of Chemical Engineering, University of North Dakota, Grand Forks, ND, USA;2. Department of Chemistry, University of North Dakota, Grand Forks, ND, USA;3. Department of Chemistry and Applied Biological Sciences, South Dakota School of Mine and Technology, Rapid City, SD, USA;1. Université Clermont Auvergne, Clermont Auvergne INP, CNRS, Institut Pascal, F-63000 Clermont-Ferrand, France;2. Université Clermont Auvergne, INRAE, PIAF, F-63000 Clermont-Ferrand, France;3. Université Clermont Auvergne, Laboratoire de Mathématiques Blaise Pascal, UMR6620- CNRS, 63178 Aubière Cedex, France;4. UMR1163, Biodiversité et Biotechnologie Fongiques, Aix-Marseille Université, INRAE, 13288 Marseille, France
Abstract:The efficient use of cellulases in the hydrolysis of pretreated lignocellulosic biomass is limited due to the presence of lignin. Lignin is known to bind hydrolytic enzymes nonspecifically, thereby reducing their action on carbohydrate substrates. The composition and location of residual lignin therefore seem to be important for optimizing the enzymatic hydrolysis of lignocellulosic substrates. The use of lignin-modifying enzymes such as laccase may have potential in the modification or partial removal of lignin from the biomass. In this study, the effect of lignin modification by laccase on the hydrolysis of pretreated spruce (Picea abies) and giant reed (Arundo donax) was evaluated. The substrates were first treated with laccase and then hydrolyzed with commercial cellulases. Laccase modification improved the hydrolysis yield of spruce by 12%, but surprisingly had an adverse effect on giant reed, reducing the hydrolysis yield by 17%. The binding properties of cellulases on the untreated and laccase-treated lignins were further studied using isolated lignins. The laccase treatment reduced the binding of enzymes on modified spruce lignin, whereas with giant reed, the amount of bound proteins increased after laccase treatment. Further understanding of the reactions of laccase on lignin will help to control the unspecific-binding of cellulases on lignocellulosic substrates.
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