Initial evaluation of sugarcane as a production platform for p-hydroxybenzoic acid

McQualter, Richard B., Fong Chong, Barrie, Meyer, Knut, Van Dyk, Drew E., O'Shea, Michael G., Walton, Nicholas J., Viitanen, Paul V. and Brumbley, Stevens M. (2005) Initial evaluation of sugarcane as a production platform for p-hydroxybenzoic acid. Plant Biotechnology Journal, 3 1: 29-41. doi:10.1111/j.1467-7652.2004.00095.x

Author McQualter, Richard B.
Fong Chong, Barrie
Meyer, Knut
Van Dyk, Drew E.
O'Shea, Michael G.
Walton, Nicholas J.
Viitanen, Paul V.
Brumbley, Stevens M.
Title Initial evaluation of sugarcane as a production platform for p-hydroxybenzoic acid
Formatted title
Initial evaluation of sugarcane as a production platform for p-hydroxybenzoic acid
Journal name Plant Biotechnology Journal   Check publisher's open access policy
ISSN 1467-7644
Publication date 2005
Year available 2005
Sub-type Article (original research)
DOI 10.1111/j.1467-7652.2004.00095.x
Volume 3
Issue 1
Start page 29
End page 41
Total pages 13
Place of publication United Kingdom
Publisher Wiley-Blackwell Publishing
Language eng
Subject 09 Engineering
10 Technology
1007 Nanotechnology
Abstract Sugarcane (Saccharum hybrids) was evaluated as a production platform for p-hydroxybenzoic acid using two different bacterial proteins (a chloroplast-targeted version of Escherichia coli chorismate pyruvate-lyase and 4-hydroxycinnamoyl-CoA hydratase/lyase from Pseudomonas fluorescens) that both provide a one-enzyme pathway from a naturally occurring plant intermediate. The substrates for these enzymes are chorismate (a shikimate pathway intermediate that is synthesized in plastids) and 4-hydroxycinnamoyl-CoA (a cytosolic phenylpropanoid intermediate). Although both proteins have previously been shown to elevate p-hydroxybenzoic acid levels in plants, they have never been evaluated concurrently in the same laboratory. Nor are there any reports on their efficacy in stem tissue. After surveying two large populations of transgenic plants, it was concluded that the hydratase/lyase is the superior catalyst for leaf and stem tissue, and further studies focused on this pathway. p-Hydroxybenzoic acid was quantitatively converted to glucose conjugates by endogenous uridine diphosphate (UDP)-glucosyltransferases and presumably stored in the vacuole. The largest amounts detected in leaf and stem tissue were 7.3% and 1.5% dry weight (DW), respectively, yet there were no discernible phenotypic abnormalities. However, as a result of diverting carbon away from the phenylpropanoid pathway, there was a severe reduction in leaf chlorogenic acid, subtle changes in lignin composition, as revealed by phloroglucinol staining, and an apparent compensatory up-regulation of phenylalanine ammonia-lyase. Although product accumulation in the leaves at the highest level of gene expression obtained in the present study was clearly substrate-limited, additional experiments are necessary before this conclusion can be extended to the stalk.
Keyword Bioplastics
Hydroxycinnamoyl-CoA hydratase/lyase
Metabolic engineering
p-hydroxybenzoic acid
Q-Index Code C1

Document type: Journal Article
Sub-type: Article (original research)
Collections: Excellence in Research Australia (ERA) - Collection
Australian Institute for Bioengineering and Nanotechnology Publications
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Citation counts: TR Web of Science Citation Count  Cited 41 times in Thomson Reuters Web of Science Article | Citations
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Created: Fri, 18 Dec 2009, 14:24:26 EST by Macushla Boyle on behalf of Aust Institute for Bioengineering & Nanotechnology