Water-soluble chlorophyll-binding proteins from Brassica oleracea allow for stable photobiocatalytic oxidation of cellulose by a lytic polysaccharide monooxygenase
Abstract Background Lytic polysaccharide monooxygenases (LPMOs) are indispensable redox enzymes used in industry for the saccharification of plant biomass. LPMO-driven cellulose oxidation can be enhanced considerably through photobiocatalysis using chlorophyll derivatives and light. Water soluble ch...
Main Authors: | , , , , , , , |
---|---|
Format: | Article |
Language: | English |
Published: |
BMC
2020-11-01
|
Series: | Biotechnology for Biofuels |
Subjects: | |
Online Access: | https://doi.org/10.1186/s13068-020-01832-7 |
id |
doaj-e555ec3e221443aba099e546cd2b0d58 |
---|---|
record_format |
Article |
spelling |
doaj-e555ec3e221443aba099e546cd2b0d582020-12-06T12:53:12ZengBMCBiotechnology for Biofuels1754-68342020-11-0113111210.1186/s13068-020-01832-7Water-soluble chlorophyll-binding proteins from Brassica oleracea allow for stable photobiocatalytic oxidation of cellulose by a lytic polysaccharide monooxygenaseN. Dodge0D. A. Russo1B. M. Blossom2R. K. Singh3B. van Oort4R. Croce5M. J. Bjerrum6P. E. Jensen7Department of Food Science, University of CopenhagenDepartment of Bioorganic Analytics, Institute for Inorganic and Analytical Chemistry, Friedrich Schiller University JenaDepartment of Geosciences and Natural Resource Management, University of CopenhagenDepartment of Chemistry, University of CopenhagenBiophysics of Photosynthesis, Department of Physics and Astronomy, Faculty of Sciences, and LaserLaB Amsterdam, Vrije Universiteit AmsterdamBiophysics of Photosynthesis, Department of Physics and Astronomy, Faculty of Sciences, and LaserLaB Amsterdam, Vrije Universiteit AmsterdamDepartment of Chemistry, University of CopenhagenDepartment of Food Science, University of CopenhagenAbstract Background Lytic polysaccharide monooxygenases (LPMOs) are indispensable redox enzymes used in industry for the saccharification of plant biomass. LPMO-driven cellulose oxidation can be enhanced considerably through photobiocatalysis using chlorophyll derivatives and light. Water soluble chlorophyll binding proteins (WSCPs) make it is possible to stabilize and solubilize chlorophyll in aqueous solution, allowing for in vitro studies on photostability and ROS production. Here we aim to apply WSCP–Chl a as a photosensitizing complex for photobiocatalysis with the LPMO, TtAA9. Results We have in this study demonstrated how WSCP reconstituted with chlorophyll a (WSCP–Chl a) can create a stable photosensitizing complex which produces controlled amounts of H2O2 in the presence of ascorbic acid and light. WSCP–Chl a is highly reactive and allows for tightly controlled formation of H2O2 by regulating light intensity. TtAA9 together with WSCP–Chl a shows increased cellulose oxidation under low light conditions, and the WSCP–Chl a complex remains stable after 24 h of light exposure. Additionally, the WSCP–Chl a complex demonstrates stability over a range of temperatures and pH conditions relevant for enzyme activity in industrial settings. Conclusion With WSCP–Chl a as the photosensitizer, the need to replenish Chl is greatly reduced, enhancing the catalytic lifetime of light-driven LPMOs and increasing the efficiency of cellulose depolymerization. WSCP–Chl a allows for stable photobiocatalysis providing a sustainable solution for biomass processing.https://doi.org/10.1186/s13068-020-01832-7CelluloseLight-drivenMonooxygenasesPhotobiocatalysisChlorophyll-binding protein |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
N. Dodge D. A. Russo B. M. Blossom R. K. Singh B. van Oort R. Croce M. J. Bjerrum P. E. Jensen |
spellingShingle |
N. Dodge D. A. Russo B. M. Blossom R. K. Singh B. van Oort R. Croce M. J. Bjerrum P. E. Jensen Water-soluble chlorophyll-binding proteins from Brassica oleracea allow for stable photobiocatalytic oxidation of cellulose by a lytic polysaccharide monooxygenase Biotechnology for Biofuels Cellulose Light-driven Monooxygenases Photobiocatalysis Chlorophyll-binding protein |
author_facet |
N. Dodge D. A. Russo B. M. Blossom R. K. Singh B. van Oort R. Croce M. J. Bjerrum P. E. Jensen |
author_sort |
N. Dodge |
title |
Water-soluble chlorophyll-binding proteins from Brassica oleracea allow for stable photobiocatalytic oxidation of cellulose by a lytic polysaccharide monooxygenase |
title_short |
Water-soluble chlorophyll-binding proteins from Brassica oleracea allow for stable photobiocatalytic oxidation of cellulose by a lytic polysaccharide monooxygenase |
title_full |
Water-soluble chlorophyll-binding proteins from Brassica oleracea allow for stable photobiocatalytic oxidation of cellulose by a lytic polysaccharide monooxygenase |
title_fullStr |
Water-soluble chlorophyll-binding proteins from Brassica oleracea allow for stable photobiocatalytic oxidation of cellulose by a lytic polysaccharide monooxygenase |
title_full_unstemmed |
Water-soluble chlorophyll-binding proteins from Brassica oleracea allow for stable photobiocatalytic oxidation of cellulose by a lytic polysaccharide monooxygenase |
title_sort |
water-soluble chlorophyll-binding proteins from brassica oleracea allow for stable photobiocatalytic oxidation of cellulose by a lytic polysaccharide monooxygenase |
publisher |
BMC |
series |
Biotechnology for Biofuels |
issn |
1754-6834 |
publishDate |
2020-11-01 |
description |
Abstract Background Lytic polysaccharide monooxygenases (LPMOs) are indispensable redox enzymes used in industry for the saccharification of plant biomass. LPMO-driven cellulose oxidation can be enhanced considerably through photobiocatalysis using chlorophyll derivatives and light. Water soluble chlorophyll binding proteins (WSCPs) make it is possible to stabilize and solubilize chlorophyll in aqueous solution, allowing for in vitro studies on photostability and ROS production. Here we aim to apply WSCP–Chl a as a photosensitizing complex for photobiocatalysis with the LPMO, TtAA9. Results We have in this study demonstrated how WSCP reconstituted with chlorophyll a (WSCP–Chl a) can create a stable photosensitizing complex which produces controlled amounts of H2O2 in the presence of ascorbic acid and light. WSCP–Chl a is highly reactive and allows for tightly controlled formation of H2O2 by regulating light intensity. TtAA9 together with WSCP–Chl a shows increased cellulose oxidation under low light conditions, and the WSCP–Chl a complex remains stable after 24 h of light exposure. Additionally, the WSCP–Chl a complex demonstrates stability over a range of temperatures and pH conditions relevant for enzyme activity in industrial settings. Conclusion With WSCP–Chl a as the photosensitizer, the need to replenish Chl is greatly reduced, enhancing the catalytic lifetime of light-driven LPMOs and increasing the efficiency of cellulose depolymerization. WSCP–Chl a allows for stable photobiocatalysis providing a sustainable solution for biomass processing. |
topic |
Cellulose Light-driven Monooxygenases Photobiocatalysis Chlorophyll-binding protein |
url |
https://doi.org/10.1186/s13068-020-01832-7 |
work_keys_str_mv |
AT ndodge watersolublechlorophyllbindingproteinsfrombrassicaoleraceaallowforstablephotobiocatalyticoxidationofcellulosebyalyticpolysaccharidemonooxygenase AT darusso watersolublechlorophyllbindingproteinsfrombrassicaoleraceaallowforstablephotobiocatalyticoxidationofcellulosebyalyticpolysaccharidemonooxygenase AT bmblossom watersolublechlorophyllbindingproteinsfrombrassicaoleraceaallowforstablephotobiocatalyticoxidationofcellulosebyalyticpolysaccharidemonooxygenase AT rksingh watersolublechlorophyllbindingproteinsfrombrassicaoleraceaallowforstablephotobiocatalyticoxidationofcellulosebyalyticpolysaccharidemonooxygenase AT bvanoort watersolublechlorophyllbindingproteinsfrombrassicaoleraceaallowforstablephotobiocatalyticoxidationofcellulosebyalyticpolysaccharidemonooxygenase AT rcroce watersolublechlorophyllbindingproteinsfrombrassicaoleraceaallowforstablephotobiocatalyticoxidationofcellulosebyalyticpolysaccharidemonooxygenase AT mjbjerrum watersolublechlorophyllbindingproteinsfrombrassicaoleraceaallowforstablephotobiocatalyticoxidationofcellulosebyalyticpolysaccharidemonooxygenase AT pejensen watersolublechlorophyllbindingproteinsfrombrassicaoleraceaallowforstablephotobiocatalyticoxidationofcellulosebyalyticpolysaccharidemonooxygenase |
_version_ |
1724398548748861440 |