The synergy between LPMOs and cellulases in enzymatic saccharification of cellulose is both enzyme- and substrate-depend
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ORIGINAL RESEARCH PAPER
The synergy between LPMOs and cellulases in enzymatic saccharification of cellulose is both enzyme- and substratedependent Radina Tokin . Johan Ørskov Ipsen . Peter Westh . Katja Salomon Johansen
Received: 14 February 2020 / Accepted: 20 May 2020 Ó Springer Nature B.V. 2020
Abstract Objectives The synergistic effects between cellulases and lytic polysaccharide monooxygenases (LPMOs) were investigated systematically in terms of their degree of synergy (DS) on amorphous and crystalline cellulose. Synergy curves were obtained for enzyme pairs containing a cellulase from Trichoderma reesei (Cel6A and Cel7A) and three LPMOs from Thermoascus aurantiacus (TaAA9A), Lentinus similis (LsAA9A) and Thielavia terrestris (TtAA9E). Results The synergistic experiments showed that the three LPMOs significantly improved the hydrolytic efficiency of Cel6A, on both cellulosic substrates; a more pronounced effect being seen for TtAA9E on
amorphous cellulose at low cellulase:LPMO ratios. In contrast, the highly processive, reducing-end acting Cel7A synergised with the C1-C4 oxidising LPMOs, TaAA9A and LsAA9A, but was inhibited by the presence of C1-oxidizing TtAA9E. Conclusions The degree of synergy exhibited by the cellulase-LPMO mixtures was enzyme- and substratespecific. The observed Cel7A inhibition, rather than synergy, by the C1-oxidizing LPMO, TtAA9E, warrants further investigations. Keywords
AA9 Cellulase LPMO Synergy
Introduction Electronic supplementary material The online version of this article (https://doi.org/10.1007/s10529-020-02922-0) contains supplementary material, which is available to authorized users. R. Tokin J. Ø. Ipsen P. Westh K. S. Johansen Department of Plant and Environmental Sciences, University of Copenhagen, 1871 Frederiksberg, Denmark P. Westh Department of Biotechnology and Biomedicine, Technical University of Denmark, 2800 Kgs Lyngby, Denmark K. S. Johansen (&) Department of Geoscience and Natural Resource Management, University of Copenhagen, 1958 Frederiksberg, Denmark e-mail: [email protected]
Overcoming the recalcitrance of the plant cell wall, and of cellulose in particular, is important for the more effective use of lignocellulosic biomass as an industrial feedstock. It has long been clear that cellulose is enzymatically hydrolysed by a variety of cellulases (b1,4-glycoside hydrolases) that act in concert to produce glucose (Mandels and Reese 1965). This concerted effect is observed when the combination of two or more cellulases leads to a higher degree of glucosidic-bond cleavage than the sum of cleavages by each of the individual cellulases. In the conventional understanding of this synergistic action between cellulases, enzymes with endolytic character create
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Biotechnol Lett
new chain ends in the substrate, improving accessibility and increasing the number of attack sites for exolytic cellulases (Va¨ljama¨e et al. 1999; Boisset et al. 2001). Furthermore, synergy can also result from the underlying diff
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