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Enzymatic degradation of algal 1,3-xylan: from synergism of lytic polysaccharide monooxygenases with β-1,3-xylanases to their intelligent immobilization on biomimetic silica nanoparticles

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Abstract

Lytic polysaccharide monooxygenases (LPMOs) with synergistic effect on polysaccharide hydrolase represent a revolution in biotechnology, which may accelerate the conversion of biomass to the second-generation biofuels. Discovering more hydrolases that have synergism with LPMOs will considerably expand the knowledge and application of biomass degradation. The LPMOs named CgAA9 were verified to exhibit 1.52-fold synergism when incubated with β-1,3-xylanase at a molar ratio of 3:1. The ion chromatography results proved that CgAA9 did not alter the endogenous hydrolysis mode of β-1,3-xylanase. Meanwhile, to decrease the operational cost of enzymes, a novel strategy for immobilizing LPMOs and β-1,3-xylanases based on the biomimetic silica nanoparticles was developed. It enabled preparation of immobilized enzymes directly from the cell lysate. The immobilization efficiency and activity recovery reached 84.6 and 81.4%. They showed excellent reusability for 12 cycles by retaining 68% of initial activity. The optimum temperature for both free and immobilized biocatalyst were 40 and 37 °C, indicating they were ideal candidates for typical simultaneous saccharification and fermentation (SSF) in ethanol production from algea biomass. This was the first report on the synergy between LPMOs and β-1,3-xylanase, and the strategy for enzyme self-immobilization was simple, timesaving, and efficient, which might have great potentials in algae biomass hydrolysis.

Key Points

• The lytic polysaccharide monooxygenases (LPMOs) from Chaetomium globosum were firstly verified to boost the hydrolysis of β-1,3-xylanases for β-1,3-xylan.

• A novel strategy for simple preparation of SpyCather-modifed silica nanopartilcles and intelligent immobilization of target enzymes from the cell lysate was proposed.

• The immobilized LPMOs and β-1,3-xylanases could be reasonable alternatives for typical simultaneous saccharification and fermentation (SSF) in manipulation of algae biomass.

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Acknowledgments

We thank Dr. Li Xialan, Dr. Chen Mingxia, and Dr. Lin Yuanqin for experimental support and helpful comments on the manuscript.

Funding

This study was funded by the China Ocean Mineral Resources Research and Development Association (grant number: DY135-B2-07) and Subsidized Project for Postgraduates’ Innovative Fund in Scientific Research of Huaqiao University (grant number: 17011087001).

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Contributions

LC and GZ designed the experiment and wrote and revised the manuscript; LC and XL purified and immobilized the enzyme; and YQ and ML performed enzyme characterization and helped with experimental analysis. All authors read and approved the final manuscript.

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Correspondence to Guangya Zhang.

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The authors declare that they have no conflict of interest.

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This article does not contain any studies with human participants or animals performed by any of the authors.

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Cai, L., Liu, X., Qiu, Y. et al. Enzymatic degradation of algal 1,3-xylan: from synergism of lytic polysaccharide monooxygenases with β-1,3-xylanases to their intelligent immobilization on biomimetic silica nanoparticles. Appl Microbiol Biotechnol 104, 5347–5360 (2020). https://doi.org/10.1007/s00253-020-10624-w

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  • DOI: https://doi.org/10.1007/s00253-020-10624-w

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