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Molecular analysis of multidomain bacterial and fungal cellulases and hemicellulases

ReferenceP01592
Principal Investigator / Supervisor Professor Harry Gilbert
Co-Investigators /
Co-Supervisors
Institution Newcastle University
DepartmentAgriculture Food and Rural Development
Funding typeResearch
Value (£) 535,683
StatusCompleted
TypeResearch Grant
Start date 04/11/1994
End date 01/07/2001
Duration78 months

Abstract

Our previous study (LRG13/138) demonstrated that plant cell wall hydrolases from a range of bacteria, have a modular structure consisting of a catalytic domain (CD) which is linked by hydroxyamino acid-rich sequences to a non-catalytic cellulose binding domain CBD). The aims of this projects are as follows: (1) Evaluate whether CBDs located in different enzymes fulfil similar roles; (II) Establish whether spatial separation of CDs and CBDs is essential for enzymic hydrolysis of native plant cell walls; (III) determine the role of the C-terminal non-catalytic domains of Neocallimastix cellulases and xylanases, and establish whether the structure of the Neocallimastix plant cell wall hydrolases provides a good paradigm for anaerobic fungal cellulases and hemicellulases; (IV) investigate the molecular architecture of non-xylanase hemicellulases. It is anticipated that the data generated in this project will underpin the industrial exploitation of these enzymes.

Summary

unavailable
Committee Closed Committee - Plant & Microbial Sciences (PMS)
Research TopicsX – not assigned to a current Research Topic
Research PriorityX – Research Priority information not available
Research Initiative X - not in an Initiative
Funding SchemeX – not Funded via a specific Funding Scheme
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