Award details

Studies of the conformational stability of beta-lactoglobulin

Reference	D01314
Principal Investigator / Supervisor	Professor Lindsay Sawyer
Co-Investigators / Co-Supervisors
Institution	University of Edinburgh
Department	Inst of Cell and Molecular Biology
Funding type	Research
Value (£)	103,091
Status	Completed
Type	Research Grant
Start date	01/03/1994
End date	01/04/1997
Duration	37 months

Abstract

The thermal denaturation of the whey proteins and their subsequent interaction with casein plays a key part in limiting milk processing possibilities. For example, the binding of denatured beta-lactoglobulin to casein micelles limits the time and temperature of heating used for sterilisation of liquid milk products. Likewise, incorporation of whey proteins into cheese to improve yield renders the casein resistant to renneting. It is important, therefore, to understand the mechanism by which beta-lactoglobulin unfolds to become capable of unlimited aggregation reactions. We wish to apply the techniques of protein crystallography and thermochemistry linked by molecular dynamics simulations to a variety of beta-lactoglobulin structures and mutants at different pHs and ionic strengths, in order to understand the stability and conformational mobility of the protein.

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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