Award details

Structures and properties of seed proteins and enzymes of plant oxylipin metabolism

Reference	BBS/E/J/00000158
Principal Investigator / Supervisor	Professor Rod Casey
Co-Investigators / Co-Supervisors
Institution	John Innes Centre
Department	John Innes Centre Department
Funding type	Research
Value (£)	700,844
Status	Completed
Type	Institute Project
Start date	01/04/1997
End date	31/12/2006
Duration	117 months

Abstract

This project examines the synthesis, structures and properties of a number of proteins that play key roles in the quality of plant-based foods and in plant defence responses. The pea seed protein legumin is an important component of texturised proteins that are used in vegetarian foods. It is homologous in sequence to soybean glycinin. The `functional¿ properties of legumin and glycinin are key to their behaviour during food processing, but we have little understanding of the molecular basis of these properties, partly because of the inherent difficulties of purifying homogeneous preparations of the proteins, which derive from small gene families and are specifically proteolysed as part of their synthesis and assembly. We are investigating the use of transgenic wheat for the large-scale production of homogeneous, processed and assembled pea legumin in order to better understand its structure and properties. Protein preparations from legume seeds such as soybean and pea can have associated ¿off¿ flavours contributed by short-chain aldehydes that are derived from the combined action of lipoxygenases and hydroperoxide lyases on polyunsaturated fatty acids. This project examines the structures and activities of lipoxygenases and hydroperoxide lyases from legumes, including pea and the model species Medicago truncatula, to better understand their modes of action and their potential role in the determination of food quality. We have removed specific lipoxygenase activities from pea seeds, and potato tubers, and are investigating the consequences of this for the generation of aroma volatiles, antioxidant composition, and responses to pathogens. We also are gaining an understanding of lipoxygenase and hydroperoxide lyase activity through the production and analysis of specific mutants that have been produced in vitro by fermentation in E. coli.

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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