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Purification and characterisation of esterase capable of degrading plant cell walls
Reference
BBS/E/F/02150910
Principal Investigator / Supervisor
Dr Paul Kroon
Co-Investigators /
Co-Supervisors
Institution
Quadram Institute Bioscience
Department
Quadram Institute Bioscience Department
Funding type
Research
Value (£)
4,355
Status
Completed
Type
Institute Project
Start date
01/04/1997
End date
30/06/1997
Duration
3 months
Abstract
Previous work on cell wall-degrading esterases has led to the isolation and characterisation of several enzymes, the most studied being FAE-III and CinnAE from Aspergillus niger. Of all the enzymes so far purified however, none shows a preference for one of the feruloyl-sugar linkages found in certain plant cell walls (a-1,6-linkages to galactose). FAE-III shows highest activity on 1,5-links to arabinose, whereas CinnAE is most efficient on 1,2-links to arabinose. We have recently detected an enzyme which is active on esters of sinapic acid (hence the name, sinapic acid esterase, SAE) and preliminary experiments show that it has a preference for 1,6 linked feruloylated galactose oligosaccharides derived from cell walls. We intend to purify SAE, and to determine its precise substrate for cell wall structures.
Summary
unavailable
Committee
Closed Committee - Agri-food (AF)
Research Topics
X – not assigned to a current Research Topic
Research Priority
X – Research Priority information not available
Research Initiative
X - not in an Initiative
Funding Scheme
X – not Funded via a specific Funding Scheme
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