| Literature DB >> 22147756 |
Silvia Fornalé1, Montserrat Capellades, Antonio Encina, Kan Wang, Sami Irar, Catherine Lapierre, Katia Ruel, Jean-Paul Joseleau, Jordi Berenguer, Pere Puigdomènech, Joan Rigau, David Caparrós-Ruiz.
Abstract
Cinnamyl alcohol dehydrogenase (CAD) is a key enzyme involved in the last step of monolignol biosynthesis. The effect of CAD down-regulation on lignin production was investigated through a transgenic approach in maize. Transgenic CAD-RNAi plants show a different degree of enzymatic reduction depending on the analyzed tissue and show alterations in cell wall composition. Cell walls of CAD-RNAi stems contain a lignin polymer with a slight reduction in the S-to-G ratio without affecting the total lignin content. In addition, these cell walls accumulate higher levels of cellulose and arabinoxylans. In contrast, cell walls of CAD-RNAi midribs present a reduction in the total lignin content and of cell wall polysaccharides. In vitro degradability assays showed that, although to a different extent, the changes induced by the repression of CAD activity produced midribs and stems more degradable than wild-type plants. CAD-RNAi plants grown in the field presented a wild-type phenotype and produced higher amounts of dry biomass. Cellulosic bioethanol assays revealed that CAD-RNAi biomass produced higher levels of ethanol compared to wild-type, making CAD a good target to improve both the nutritional and energetic values of maize lignocellulosic biomass.Entities:
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Year: 2011 PMID: 22147756 DOI: 10.1093/mp/ssr097
Source DB: PubMed Journal: Mol Plant ISSN: 1674-2052 Impact factor: 13.164