Use this URL to cite or link to this record in EThOS:
Title: The Pursuit Of A Novel Haloperoxidase For Asymmetric Biocatalysis
Author: Moore , Jonathan K.
ISNI:       0000 0001 3417 0671
Awarding Body: University of Liverpool
Current Institution: University of Liverpool
Date of Award: 2007
Availability of Full Text:
Access from EThOS:
Haloperoxidases are a group of enzymes with the ability to catalyse the halogenation of organic compounds in the presence of peroxides, such as H202, and halides. The most well known of the haloperoxidases is chloroperoxidase (CPO) from Caldariomyces tumago, a heavily glycosylated, monomeric heme protein and versatile catalyst that displays moderate to high levels of enantioselectivity on a number of substrates. The enzyme is extracellular, utilising H20 2 as an oxygen donor and does not require co-factor recycling. The primary aim of this project was to isolate a new haloperoxidase which would complement the capabilities of CPO and be used to catalyse novel reactions in the synthesis of fine chemicals. The recent isolation of a novel haloperoxidase in the basidiomycete Agrocybe aegerita, showing some amino acid sequence homology to CPO, provided evidence that there may be potentially useful enzymes of this nature to be found in other basidiomycetes. Investigation of a putative chloroperoxidase enzyme in the basidiomycete Agaricus bisporus ultimately proved unsuccessful. However, it led to the development of activity screening techniques to enable the identification of any pote.ntial haloperoxidase activity in the basidiomycetes. By combining polyacrylamide gel staining and spectrophotometric techniques, extracellular heme-haloperoxidase activity in the basidiomycete Stropharia aeruginosa was described and attempts to characterise, purify and clone the enzyme responsible were made.
Supervisor: Not available Sponsor: Not available
Qualification Name: Thesis (Ph.D.) Qualification Level: Doctoral
EThOS ID:  DOI: Not available