Radina Tokin1, Johan Ørskov Ipsen1, Peter Westh1,2, Katja Salomon Johansen3,4. 1. Department of Plant and Environmental Sciences, University of Copenhagen, 1871, Frederiksberg, Denmark. 2. Department of Biotechnology and Biomedicine, Technical University of Denmark, 2800, Kgs Lyngby, Denmark. 3. Department of Plant and Environmental Sciences, University of Copenhagen, 1871, Frederiksberg, Denmark. ksj@ign.ku.dk. 4. Department of Geoscience and Natural Resource Management, University of Copenhagen, 1958, Frederiksberg, Denmark. ksj@ign.ku.dk.
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 substrate-specific. The observed Cel7A inhibition, rather than synergy, by the C1-oxidizing LPMO, TtAA9E, warrants further investigations.
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 substrate-specific. The observed Cel7A inhibition, rather than synergy, by the C1-oxidizing LPMO, TtAA9E, warrants further investigations.
Authors: Johan Ø Ipsen; Magnus Hallas-Møller; Søren Brander; Leila Lo Leggio; Katja S Johansen Journal: Biochem Soc Trans Date: 2021-02-26 Impact factor: 5.407
Authors: Monika Tõlgo; Olav A Hegnar; Heidi Østby; Anikó Várnai; Francisco Vilaplana; Vincent G H Eijsink; Lisbeth Olsson Journal: Appl Environ Microbiol Date: 2022-01-26 Impact factor: 4.792
Authors: Heidi Østby; Line Degn Hansen; Svein J Horn; Vincent G H Eijsink; Anikó Várnai Journal: J Ind Microbiol Biotechnol Date: 2020-08-25 Impact factor: 3.346