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Title: Suppression of CINNAMOYL-CoA REDUCTASE increases the level of monolignol ferulates incorporated into maize lignins

Abstract

Background.The cell wall polymer lignin provides structural support and rigidity to plant cell walls, and therefore to the plant body. However, the recalcitrance associated with lignin impedes the extraction of polysaccharides from the cell wall to make plant-based biofuels and biomaterials. The cell wall digestibility can be improved by introducing labile ester bonds into the lignin backbone that can be easily broken under mild base treatment at room temperature. The FERULOYL-CoA MONOLIGNOL TRANSFERASE (FMT) enzyme, which may be naturally found in many plants, uses feruloyl-CoA and monolignols to synthesize the ester-linked monolignol ferulate conjugates. A mutation in the first lignin-specific biosynthetic enzyme, CINNAMOYL-CoA REDUCTASE (CCR), results in an increase in the intracellular pool of feruloyl-CoA. Results. Maize (Zea mays) has a native putative FMT enzyme, and its ccr mutants produce an increased pool of feruloyl-CoA that can be used for conversion to monolignol ferulate conjugates. The decreased lignin content and monomers did not, however, impact the plant growth or biomass. The increase in monolignol conjugates correlated with an improvement in the digestibility of maize stem rind tissue. Conclusions. Together, increased monolignol ferulates and improved digestibility in ccr1 mutant plants suggests that they may be superior biofuel crops.

Authors:
 [1];  [2];  [3];  [3];  [3];  [3];  [3];  [4];  [3];  [2];  [1];  [1]
  1. Univ. of Wisconsin, Madison, WI (United States). Wisconsin Energy Institute. Dept. of Energy Great Lakes Bioenergy Research Center; Univ. of Wisconsin, Madison, WI (United States). Dept. of Biochemistry
  2. Illinois State Univ., Normal, IL (United States). Dept. of Energy Great Lakes Bioenergy Research Center, School of Biological Sciences
  3. Univ. of Wisconsin, Madison, WI (United States). Wisconsin Energy Institute. Dept. of Energy Great Lakes Bioenergy Research Center; Univ. of Wisconsin, Madison, WI (United States). Dept. of Agronomy
  4. Univ. of British Columbia, Vancouver, BC (Canada). Dept. of Wood Science
Publication Date:
Research Org.:
Univ. of Wisconsin, Madison, WI (United States). Wisconsin Energy Institute
Sponsoring Org.:
USDOE
OSTI Identifier:
1393539
Grant/Contract Number:  
FC02-07ER64494
Resource Type:
Accepted Manuscript
Journal Name:
Biotechnology for Biofuels
Additional Journal Information:
Journal Volume: 10; Journal Issue: 1; Journal ID: ISSN 1754-6834
Publisher:
BioMed Central
Country of Publication:
United States
Language:
English
Subject:
09 BIOMASS FUELS; Zea mays; Mass spectrometry; Cell wall digestibility; Biofuels

Citation Formats

Smith, Rebecca A., Cass, Cynthia L., Mazaheri, Mona, Sekhon, Rajandeep S., Heckwolf, Marlies, Kaeppler, Heidi, de Leon, Natalia, Mansfield, Shawn D., Kaeppler, Shawn M., Sedbrook, John C., Karlen, Steven D., and Ralph, John. Suppression of CINNAMOYL-CoA REDUCTASE increases the level of monolignol ferulates incorporated into maize lignins. United States: N. p., 2017. Web. doi:10.1186/s13068-017-0793-1.
Smith, Rebecca A., Cass, Cynthia L., Mazaheri, Mona, Sekhon, Rajandeep S., Heckwolf, Marlies, Kaeppler, Heidi, de Leon, Natalia, Mansfield, Shawn D., Kaeppler, Shawn M., Sedbrook, John C., Karlen, Steven D., & Ralph, John. Suppression of CINNAMOYL-CoA REDUCTASE increases the level of monolignol ferulates incorporated into maize lignins. United States. doi:10.1186/s13068-017-0793-1.
Smith, Rebecca A., Cass, Cynthia L., Mazaheri, Mona, Sekhon, Rajandeep S., Heckwolf, Marlies, Kaeppler, Heidi, de Leon, Natalia, Mansfield, Shawn D., Kaeppler, Shawn M., Sedbrook, John C., Karlen, Steven D., and Ralph, John. Tue . "Suppression of CINNAMOYL-CoA REDUCTASE increases the level of monolignol ferulates incorporated into maize lignins". United States. doi:10.1186/s13068-017-0793-1. https://www.osti.gov/servlets/purl/1393539.
@article{osti_1393539,
title = {Suppression of CINNAMOYL-CoA REDUCTASE increases the level of monolignol ferulates incorporated into maize lignins},
author = {Smith, Rebecca A. and Cass, Cynthia L. and Mazaheri, Mona and Sekhon, Rajandeep S. and Heckwolf, Marlies and Kaeppler, Heidi and de Leon, Natalia and Mansfield, Shawn D. and Kaeppler, Shawn M. and Sedbrook, John C. and Karlen, Steven D. and Ralph, John},
abstractNote = {Background.The cell wall polymer lignin provides structural support and rigidity to plant cell walls, and therefore to the plant body. However, the recalcitrance associated with lignin impedes the extraction of polysaccharides from the cell wall to make plant-based biofuels and biomaterials. The cell wall digestibility can be improved by introducing labile ester bonds into the lignin backbone that can be easily broken under mild base treatment at room temperature. The FERULOYL-CoA MONOLIGNOL TRANSFERASE (FMT) enzyme, which may be naturally found in many plants, uses feruloyl-CoA and monolignols to synthesize the ester-linked monolignol ferulate conjugates. A mutation in the first lignin-specific biosynthetic enzyme, CINNAMOYL-CoA REDUCTASE (CCR), results in an increase in the intracellular pool of feruloyl-CoA. Results. Maize (Zea mays) has a native putative FMT enzyme, and its ccr mutants produce an increased pool of feruloyl-CoA that can be used for conversion to monolignol ferulate conjugates. The decreased lignin content and monomers did not, however, impact the plant growth or biomass. The increase in monolignol conjugates correlated with an improvement in the digestibility of maize stem rind tissue. Conclusions. Together, increased monolignol ferulates and improved digestibility in ccr1 mutant plants suggests that they may be superior biofuel crops.},
doi = {10.1186/s13068-017-0793-1},
journal = {Biotechnology for Biofuels},
number = 1,
volume = 10,
place = {United States},
year = {2017},
month = {5}
}

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Figures / Tables:

Figure 1 Figure 1: An abbreviated version of the lignin biosynthetic pathway highlighting the effects of the ccrl mutation.The mutated CCR/ gene results in reduced CCR/ transcript, and presumably less CCRl enzyme, and a pool offeruloyl-CoA (FA reserv oir).The conjugates formed between the monol­ ignols and feruloyl-CoA by ZmFMT are incorporated intomore » the lignin polymer, generating a zip-ligni n in which the ester bonds in the backbone are readily cleaved by base« less

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    Works referencing / citing this record:

      Figures/Tables have been extracted from DOE-funded journal article accepted manuscripts.