Award details

Protein unfolding and aggregation and the mechanical stability of interfaces

Reference	BBS/B/12393
Principal Investigator / Supervisor	Professor Clare Mills
Co-Investigators / Co-Supervisors	Dr John Anthony Jenkins, Mr Neil Rigby, Professor Peter Wilde
Institution	Quadram Institute Bioscience
Department	Food Materials Science Division
Funding type	Research
Value (£)	131,028
Status	Completed
Type	Research Grant
Start date	01/07/2004
End date	31/12/2007
Duration	42 months

Abstract

The extent of intermolecular interactions within the absorbed protein layer at an interface determines its mechanical properties, affecting the stability and shelf life of protein-stabilised foams and emulsions. Using the whey protein alpha-lactalbumin and the non-specific lipid transfer protein of barley as model systems, partially folded states (induced by thermal processing or as a consequence of absorption) will be characterised and the role they play in determining the mechanical properties of a protein-stabilised interface will be studied. The knowledge gained will underpin the development of predictive models of interfacial behaviour required for rational design of food structures and improve manufacturing efficiency. (Joint BBS/B/12466)

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

Associated awards:

BBS/B/12466 Protein unfolding and aggregation and the mechanical stability of interfaces

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