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The rational design of beta-1,4-glycanases with improved catalytic properties
Reference
MOL04564
Principal Investigator / Supervisor
Professor Harry Gilbert
Co-Investigators /
Co-Supervisors
Institution
Newcastle University
Department
Agriculture Food and Rural Development
Funding type
Research
Value (£)
158,011
Status
Completed
Type
Research Grant
Start date
01/10/1995
End date
01/10/1998
Duration
36 months
Abstract
The proposed research programme is designed to test the following hypotheses: i) The thermostabilising domain of xylanase Y can be used to improve the thermostability of Family 10 xylanases. ii) The association of endo- and side chain-cleaving glycanases enhances their synergistic interactions. iii) Rationally design modifications to a beta-1,4-glycanase that a) increases the pH optimum of the enzyme and; b) changes the mode of xylan hydrolysis.
Summary
unavailable
Committee
Closed Committee - Biomolecular Sciences (BMS)
Research Topics
X – not assigned to a current Research Topic
Research Priority
X – Research Priority information not available
Research Initiative
Molecules (Ropa) (MOL) [1994]
Funding Scheme
X – not Funded via a specific Funding Scheme
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