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Suppression of CINNAMOYL-CoA REDUCTASE increases the level of monolignol ferulates incorporated into maize lignins Smith, Rebecca A.; Cass, Cynthia L.; Mazaheri, Mona; Sekhon, Rajandeep S.; Heckwolf, Marlies; Kaeppler, Heidi; de Leon, Natalia; Mansfield, Shawn D., 1969-; Kaeppler, Shawn M.; Sedbrook, John C.; Karlen, Steven D.; Ralph, John

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.

Item Metadata

Title
Suppression of CINNAMOYL-CoA REDUCTASE increases the level of monolignol ferulates incorporated into maize lignins
Creator
Smith, Rebecca A.; Cass, Cynthia L.; Mazaheri, Mona; Sekhon, Rajandeep S.; Heckwolf, Marlies; Kaeppler, Heidi; de Leon, Natalia; Mansfield, Shawn D., 1969-; Kaeppler, Shawn M.; Sedbrook, John C.; Karlen, Steven D.; Ralph, John
Publisher
BioMed Central
Date Issued
2017-05-02
Description
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.
Subject
Zea mays; Mass spectrometry; Cell wall digestibility; Biofuels
Genre
Article
Type
Text
Language
eng
Date Available
2017-05-03
Provider
Vancouver : University of British Columbia Library
Rights
Attribution 4.0 International (CC BY 4.0)
DOI
10.14288/1.0347296
URI
http://hdl.handle.net/2429/61484
Affiliation
Forestry, Faculty of; Non UBC; Wood Science, Department of
Citation
Biotechnology for Biofuels. 2017 May 02;10(1):109
Publisher DOI
10.1186/s13068-017-0793-1
Peer Review Status
Reviewed
Scholarly Level
Faculty
Copyright Holder
The Author(s)
Rights URI
http://creativecommons.org/licenses/by/4.0/
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Attribution 4.0 International (CC BY 4.0)