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Site-directed mutagenesis and physical studies of lignin peroxidase

Reference	BCI06255
Principal Investigator / Supervisor	Professor Andrew Trevor Smith
Co-Investigators / Co-Supervisors	Professor Patricia Harvey
Institution	University of Sussex
Department	Sch of Life Sciences
Funding type	Research
Value (£)	136,302
Status	Completed
Type	Research Grant
Start date	01/09/1996
End date	01/02/2000
Duration	41 months

Abstract

We have recently expressed a gene encoding the complete coding sequence (including the pro region ) of lignin peroxidase (isoenzyme H8) from Phanerochaete chrysosporium in E. coli and obtained active recombinant lignin peroxidase by controlled in vitro refolding. The ability to produce designed protein variants offers both the opportunity to explore novel structure/function relationships and to potentially extend the usefulness of this class of enzyme for biobleaching and bioremediation processes. In particular we will investigate: (i) The mechanism of veratryl alcohol enhancement of lignin model compound oxidation. (ii) The requirements for acid/base cataylsis in the formation of Compound I. (iii) The relationship between globins and peroxidases.

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	Biological Chemistry Initiative (BCI) [1995]
Funding Scheme	X – not Funded via a specific Funding Scheme

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