title: Improved paper pulp from plants with suppressed cinnamoyl-CoA reductase or cinnamyl alcohol dehydrogenase.
abstract: Transgenic plants severely suppressed in the activity of cinnamoyl-CoA reductase were produced by introduction of a partial sense CCR transgene into tobacco. Five transgenic lines with CCR activities ranging from 2 to 48% of wild-type values were selected for further study. Some lines showed a range of aberrant phenotypes including reduced growth, and all had changes to lignin structure making the polymer more susceptible to alkali extraction. The most severely CCR-suppressed line also had significantly decreased lignin content and an increased proportion of free phenolic groups in non-condensed lignin. These changes are likely to make the lignin easier to extract during chemical pulping. Direct Kraft pulping trials confirmed this. More lignin could be removed from the transgenic wood than from wild-type wood at the same alkali charge. A similar improvement in pulping efficiency was recently shown for poplar trees expressing an antisense cinnamyl alcohol dehydrogenase gene. Pulping experiments performed here on CAD-antisense tobacco plants produced near-identical results--the modified lignin was more easily removed during pulping without any adverse effects on the quality of the pulp or paper produced. These results suggest that pulping experiments performed in tobacco can be predictive of the results that will be obtained in trees such as poplar, extending the utility of the tobacco model. On the basis of our results on CCR manipulation in tobacco, we predict that CCR-suppressed trees may show pulping benefits. However, it is likely that CCR-suppression will not be the optimal target for genetic manipulation of pulping character due to the potential associated growth defects.
authors.affiliation: Syngenta, Jealott's Hill Research Station, Bracknell, UK.
authors.forename: Ann
authors.initials: A
authors.lastname: O'Connell
authors.forename: Karen
authors.initials: K
authors.lastname: Holt
authors.forename: Joël
authors.initials: J
authors.lastname: Piquemal
authors.forename: Jacqueline
authors.initials: J
authors.lastname: Grima-Pettenati
authors.forename: Alain
authors.initials: A
authors.lastname: Boudet
authors.forename: Brigitte
authors.initials: B
authors.lastname: Pollet
authors.forename: Catherine
authors.initials: C
authors.lastname: Lapierre
authors.forename: Michel
authors.initials: M
authors.lastname: Petit-Conil
authors.forename: Wolfgang
authors.initials: W
authors.lastname: Schuch
authors.forename: Claire
authors.initials: C
authors.lastname: Halpin
mesh_terms: D000429:Alcohol Oxidoreductases / Q000235:genetics / Q000378:metabolism*; D000445:Aldehyde Oxidoreductases / Q000235:genetics / Q000378:metabolism*; D002473:Cell Wall / Q000737:chemistry; D015536:Down-Regulation; D008031:Lignin / Q000235:genetics / Q000378:metabolism*; D008854:Microscopy, Electron; D010209:Paper; D010636:Phenols / Q000378:metabolism; D010641:Phenotype; D010940:Plant Proteins / Q000235:genetics / Q000378:metabolism*; D018517:Plant Roots / Q000378:metabolism; D030821:Plants, Genetically Modified; D014026:Nicotiana / Q000201:enzymology* / Q000235:genetics; D019076:Transgenes
chemical_list: D010636:Phenols; D010940:Plant Proteins; D008031:Lignin; D000429:Alcohol Oxidoreductases; C018656:cinnamyl alcohol dehydrogenase; D000445:Aldehyde Oxidoreductases; C019904:cinnamoyl CoA reductase