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The targeting of starch binding domains from starch synthase III to the cell wall alters cell wall composition and properties

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Starch binding domains of starch synthase III from Arabidopsis thaliana (SBD123) binds preferentially to cell wall polysaccharides rather than to starch in vitro. Transgenic plants overexpressing SBD123 in the cell wall are larger than wild type. Cell wall components are altered in transgenic plants. Transgenic plants are more susceptible to digestion than wild type and present higher released glucose content. Our results suggest that the transgenic plants have an advantage for the production of bioethanol in terms of saccharification of essential substrates.

Abstract

The plant cell wall, which represents a major source of biomass for biofuel production, is composed of cellulose, hemicelluloses, pectins and lignin. A potential biotechnological target for improving the production of biofuels is the modification of plant cell walls. This modification is achieved via several strategies, including, among others, altering biosynthetic pathways and modifying the associations and structures of various cell wall components. In this study, we modified the cell wall of A. thaliana by targeting the starch-binding domains of A. thaliana starch synthase III to this structure. The resulting transgenic plants (E8-SDB123) showed an increased biomass, higher levels of both fermentable sugars and hydrolyzed cellulose and altered cell wall properties such as higher laxity and degradability, which are valuable characteristics for the second-generation biofuels industry. The increased biomass and degradability phenotype of E8-SBD123 plants could be explained by the putative cell-wall loosening effect of the in tandem starch binding domains. Based on these results, our approach represents a promising biotechnological tool for reducing of biomass recalcitrance and therefore, the need for pretreatments.

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Acknowledgments

This work was supported by grants from Agencia Nacional de Promoción Científica y Técnológica (PICT 2010-0543 and PICT 2011-0982), Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET, PIP#237 and #134) and Secretaría de Estado de Ciencia, Tecnología e Innovación de Santa Fe (SECTEI -2010-113-14). MJG and DAP are doctoral fellows from CONICET. HAV, JB, DFGC and MVB are research members from CONICET. The authors thank Ing. Martín Reggiardo-Sobre (CEFOBI) for his technical assistance with the in in vitro dry matter digestibility assays and Bioq. José M. Pellegrino from Instituto de Fisiología Experimental (IFISE) for his advice in general microscopy and image processing.

Author contributions

MJG, DAP, JB, DGC, and MVB designed the conception and delineation of the study; prepared the manuscript and reviewed it before submission. MJG, DAP, HAV and JB conducted the required experiments, performed the acquisition of the data or analyzed such information. All authors read and approved the final manuscript.

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Correspondence to María V. Busi.

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Accession numbers: Starch synthase III, locus name At1g11720; Expansin 8, locus name At2g40610.

Mauricio J. Grisolia and Diego A. Peralta have contributed equally to this work.

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Grisolia, M.J., Peralta, D.A., Valdez, H.A. et al. The targeting of starch binding domains from starch synthase III to the cell wall alters cell wall composition and properties. Plant Mol Biol 93, 121–135 (2017). https://doi.org/10.1007/s11103-016-0551-y

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